Patent Publication Number: US-10781456-B2

Title: Carbon-neutral and carbon-positive photorespiration bypass routes supporting higher photosynthetic rate and yield

Description:
SUBMISSION OF SEQUENCE LISTING 
     The sequence listing associated with this application is filed in electronic format via EFS-Web and is hereby incorporated by reference into the specification in its entirety. The text file containing the sequence listing, created on Dec. 14, 2017, is named “1111_106_seq_list.TXT” and is 143 kB in size. 
     The present invention relates to an organism, a tissue, a cell or an organelle expressing enzymes which allow the conversion of 2-phosphoglycolate (2-PG; also known as glycolate 2-phosphate) into an intermediate compound of the Calvin-Benson-Bassham Cycle (CBBC) without releasing CO 2 . The organism, tissue, cell or organelle of the invention may be genetically engineered, transgenic and/or transplastomic so as to express at least one enzyme which is involved in this conversion. The present invention further relates to an organism, tissue, cell or organelle which comprises/expresses at least one enzyme which is involved in this conversion. The present invention further relates to a method for producing an organism, tissue, cell or organelle of the invention. The present invention further relates to a method of enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO 2 . The present invention further relates to the use of an organism, tissue, cell or organelle of the invention for enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO 2 . 
     In the today&#39;s world, one in seven people is malnourished (Foley, 2011 , Nature  478, 337-342). This situation is expected to worsen as human population keeps increasing at a staggering rate (Lee R., 2011 , Science  333, 569-573). Feeding 10-15 billion people at the year 2100 is a tremendously challenging task that will only be met by the implementation of drastic measures to increase agricultural productivity (Godfray, H. C. et al., 2010 , Science  327, 812-818; Tester M. and Langridge P., 2010 , Science  327, 818-822). Hence, the seed industry seeks sustainable and economically viable solutions to increase crop yield despite numerous challenges, such as finite arable land and water resources, deleterious environmental conditions (e.g., drought, salinity), reduced availability of fertilizers, climate volatility and depletion of soil nutrients. A fundamental way to improve plant productivity and performance is through the use of plant genomics. 
     The reductive pentose phosphate cycle (rPP), also known as the Calvin-Benson-Bassham Cycle (CBBC), is responsible for the vast majority of the carbon fixed in the biosphere (Hugler M. and Sievert S. M., 2011 , Ann Rev Mar Sci  3, 261-289). This cycle operates in higher plants, algae and many bacteria. Although under an immensely strong selective pressure for eons, this process, however, still displays major inefficiencies (Zhu X. G. et al., 2010 , Rev Plant Biol  61, 235-261). A major constraint limiting the carbon fixation efficiency of the CBBC relates to its CO 2 -fixing enzyme: ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Rubisco exhibits low catalytic rate and hence is required at high cellular concentrations. Moreover, Rubisco&#39;s partial selectivity towards CO 2  results in O 2  being also accepted. This further reduces the CBBC&#39;s effective rate and leads to the formation of 2-PG, a compound which is toxic to plants (Spreitzer R. J. and Salvucci M. E., 2002 , Annu Rev Plant Biol  53, 449-475). Due to an inherent mechanistic trade-off, any decrease in the cross-reactivity towards O 2  leads to a decrease in catalytic rate and vice versa. This makes improvements in photosynthetic yield by engineering Rubisco a daunting challenge (Savir Y. et al., 2010 , Proc Natl Acad Sci USA  107, 3475-3480; Raines C. A., 2006 , Plant Cell Environ  29, 331-339). 
     In a process termed photorespiration, 2-PG is detoxified and reassimilated into the CBBC at the expense of cellular energy, i.e., ATP and NADPH equivalents (Maurino V. G. et al., 2010 , Current Opinion in Plant Biology  13, 249-256). However, the plant photorespiration pathway is inefficient for several reasons (Maurino V. G. et al., 2010 , Current Opinion in Plant Biology  13, 249-256): (i) it dissipates reducing equivalents via the oxidation of glycolate with O 2 ; (ii) it releases NH 3  that needs to be reassimilated at an energetic cost; (iii) it releases CO 2 , thereby counteracting the function of Rubisco and reducing the effective rate of the CBBC. 
     Previous studies indicated that photosynthetic rate and yield can be increased by implementing alternative photorespiration routes in plants (Kebeish R. et al., 2007 , Nat Biotechnol  25, 593-599; Carvalho Jde F. et al., 2011 , BMC Biotechnol  11, 111; Maier A. et al., 2012 , Frontiers in plant science  3, 38). However, these routes focused only on (i) decreasing the ATP cost of photorespiration; (ii) bypassing the release of NH 3 ; (iii) avoiding dissipation of reducing power; and (iv) releasing CO 2  in the chloroplast, instead of the mitochondria, to increase the local CO 2  concentration in the vicinity of Rubisco and reduce the effect of O 2 . In spite of their partial benefits (Peterhansel C. et al., 2013 , Plant Biol  ( Stuttg ) 15, 754-758; Peterhansel C. et al., 2013 , J Exp Bot  64, 709-715), all these bypass routes have, just as natural photorespiration, the major drawback of resulting in the release of CO 2 , thereby counteracting the function of Rubisco and reducing the effective rate of the CBBC. 
     WO2003/100066A1 discloses the re-use of 2-PG produced in photorespiration in a pathway that converts 2-PG into P-glycerate. Further, WO2009/103782A1 describes the conversion of glycolate into malate. However, similar to other alternative photorespiration routes, also the pathways disclosed in WO2003/100066A1 and WO2009/103782A1 result in the release of CO 2  and therefore do not remedy the major deficit of natural photorespiration. 
     Another suggested photorespiration bypass, which was, however, never fully implemented, tried to address this problem by introducing a carboxylation step (Shih P. M., 2014 , J Biol Chem  289, 9493-9500). In this bypass route, glyoxylate, a photorespiration intermediate, is supposedly assimilated via reactions of the carbon fixing 3-hydroxypropionate bicycle (Herter S. et al., 2002 , J Biol Chem  277, 20277-20283). This bypass, however, converts 2-PG into pyruvate, which is not an intermediate of the CBBC. Moreover, it considerably overlaps with the central metabolism, thereby demanding complex regulation. 
     Accordingly, there is a very high unmet need for engineering improved photorespiratory bypass routes, which reduce the deficits and inefficiencies of natural photorespiration and, therefore, a need for providing improved means and methods for reducing the deficits, inefficiencies and resulting negative impacts of photorespiration. It is thereby particularly envisaged that the photosynthetic rate and yield is increased. 
     This need is addressed by providing the embodiments characterized in the claims. 
     Accordingly, in a first aspect, the present invention relates to an organism, a tissue, a cell or an organelle expressing enzymes which allow the conversion of 2-PG into an intermediate compound of the CBBC without releasing CO 2 . 
     In particular, the present invention provides enzymatic pathways that allow for the conversion of 2-PG into an intermediate compound of the CBBC with less deficits, inefficiencies and resulting negative impacts than natural photorespiration or previously suggested photorespiration bypass pathways. The assembled enzymatic pathways are therefore improved photorespiration bypass pathways, which can support a significantly higher photosynthetic rate and yield. It is the major advantage of these pathways that no CO 2  is released. Consequently, these pathways can support a significantly higher photosynthetic rate and yield. 
     In the context of the present invention, “without releasing CO 2 ” means that no net CO 2  is released/produced (as compared to the normal/natural, i.e. the non-alternative, photorespiration). Consequently, the conversion of 2-PG into an intermediate compound of the CBBC without releasing CO 2  may be carbon-neutral, i.e. no net CO 2  is fixed or released, or may even be carbon-positive, i.e. net CO 2  is fixed (both as compared to the normal/natural, i.e. the non-alternative, photorespiration). In the context of a carbon-positive conversion, at least 1 net CO 2  molecule(s) may be fixed per converted 2-PG molecule. 
     Thus, in one embodiment an enzymatic pathway for converting 2-PG into an intermediate compound of the CBBC, as described herein, is carbon-neutral. In another embodiment such a pathway is carbon-positive. 
     The conversion of 2-PG into an intermediate compound of the CBBC without releasing CO 2  in accordance with the invention may further enable/allow for a reduced ATP and/or NAD(P)H consumption (as compared to (an organism/tissue/cell/organelle with) normal/natural, i.e. non-alternative pathway of photorespiration). “Reduced . . . consumption” in this context means, for example, that at least 1, at least 2, at least 3, at least 4 or at least 5 less ATP molecule(s) and/or at least 1 molecule(s), at least 2, at least 3, at least 4, at least 5 less NAD(P)H molecule(s) is/are required/consumed per production of 1 triose phosphate via the CBBC. In principle, a lower ATP/NAD(P)H consumption are/is preferred. In this context, it is particularly envisaged that the pathway remains thermodynamically feasible and operates under strong thermodynamic motive force. 
     One particular advantage provided by the means and method of the present invention is that the alternative photorespiration pathway is short, i.e. comprises only a few enzymes (or enzymatic activities) and enzymatic conversions/reactions, respectively. In particular, 10 or less enzymatic conversions or reactions, respectively, are envisaged, wherein lower numbers are preferred. Particular, but non-limiting, examples of numbers of enzymes (or enzymatic activities) and enzymatic conversions or reactions, respectively, in accordance with the invention are 3, 4, 5, 6, 7, 8, 9 or 10. In principle, lower numbers are preferred. The different enzymatic routes provided by the present invention are described in more detail further below. 
     As a general feature, all pathways according to the present invention convert 2-PG into an intermediate compound of the CBBC. In principle any intermediate compound of the CBBC may be the resulting product/end-product of the conversion of 2-PG in accordance with the invention. The intermediate compounds of the CBBC are known in the art and are, for example, described in the FIGS. 2.1.33 and 2.1.35 of Strasburger, Lehrbuch der Botanik (33. Ed. 1991). Likewise, the intermediate compounds of the CBBC are described herein in  FIG. 5 . In particular, an intermediate compound of the CBBC resulting from the conversion of 2-PG to be employed in accordance with the invention is selected from the group consisting of: D-glycerate 3-phosphate, D-glycerate 1,3-bisphosphate, D-glyceraldehyde 3-phosphate, dihydroxyacetone phosphate (aka glycerone phosphate), D-fructose 1,6-bisphosphate, D-fructose 6-phosphate, D-sedoheptulose 7-phosphate, D-sedoheptulose 1,7-bisphosphate, D-erythrose 4-phosphate, D-xylulose 5-phosphate, D-ribose 5-phosphate, D-ribulose 5-phosphate, and D-ribulose 1,5-bisphosphate. Preferred intermediates are selected from the group consisting of: D-glycerate 3-phosphate; D-ribulose 5-phosphate; D-ribulose 1,5-bisphosphate; D-erythrose 4-phosphate; D-ribose 5-phosphate; D-xylulose 5-phosphate; D-fructose 6-phosphate; D-fructose 1,6-bisphosphate, D-sedoheptulose 1,7-bisphosphate and dihydroxyacetone phosphate. More preferred intermediate compounds are selected from the group consisting of: D-glycerate 3-phosphate, D-ribose 5-phosphate, D-ribulose 1,5-bisphosphate, D-ribulose 5-phosphate, D-xylulose 5-phosphate and D-erythrose 4-phosphate. 
     Examples of compounds which are not to be seen as intermediate compounds of the CBBC in accordance with the invention are, for example, intermediate compounds of the 3-hydroxypropionate cycle and intermediate compounds of the central metabolism. Examples of such non-envisaged compounds are 3-hydroxypropionate, malate, succinate, pyruvate, glycerate 2-phosphate and glucose 6-phosphate. Hence, in one aspect, it is envisaged that the conversion of 2-PG into an intermediate compound of the CBBC in accordance with the invention does not involve (parts of) and/or does not (considerably) overlap with the 3-hydroxypropionate bicycle. This means that (the) respective enzymes are not used in accordance with the invention (i.e. are not encompassed by the (cascade/series of) enzymes to be employed in accordance with the invention) and/or that no respective intermediate compounds occur. For example, it is envisaged that only 3 or less, preferably only 2 or less, more preferably only 1 and most preferably 0 enzyme(s) and/or intermediate compound(s) overlap with the 3-hydroxypropionate cycle. 
     It is in particular also envisaged that an organism, a tissue, a cell or an organelle may employ a pathway of the present invention, wherein said pathway does not involve any of the enzymes and/or metabolites of lower glycolysis (i.e. the pathways of the present invention do not overlap with the lower glycolysis). The term “lower glycolysis” refers to any conversions in glycolysis downstream of 2-phosphoglycerate. Possible end points of glycolysis are known in the art. Non-limiting examples for endpoints are lactate, ethanol or acetate. Enzymes that are involved in lower glycolysis but are not-envisaged in the pathways of the present invention are preferably selected from the group consisting of enolase; pyruvate kinase; pyruvate phosphate dikinase; and pyruvate water dikinase. Metabolites of lower glycolysis are known in the art. Preferably, metabolites that are involved in lower glycolysis but are not-envisaged in the pathways of the present invention are selected from phosphoenolpyruvate (PEP) and pyruvate. In other words, the enzymes expressed by an organism, a tissue, a cell or an organelle of the present invention that allow for conversion of 2-PG into an intermediate of the CBBC do not comprise any enzymes and/or metabolites of lower glycolysis. The enzyme(s) of the lower glycolysis are preferably selected from the group consisting of enolase; pyruvate kinase; pyruvate phosphate dikinase; and pyruvate water dikinase. The metabolites of the lower glycolysis are preferably selected from the group consisting of phosphoenolpyruvate (PEP) and pyruvate. 
     Similarly, it is in particular also envisaged that an organism, a tissue, a cell or an organelle may employ a pathway of the present invention, wherein said pathway does not involve any of the enzymes and/or metabolites of the citric acid/TCA cycle (i.e. the pathways of the present invention do not overlap with the citric acid/TCA cycle). Enzymes and metabolites of the citric acid/TCA cycle are known in the art. Preferably, metabolites that are involved in the citric acid/TCA cycle but are not-envisaged in the pathways of the present invention are selected from the group consisting of citrate, isocitrate, 2-keto-glutarate, succinyl-CoA, succinate, fimarate, malate and oxaloacetate. In other words the enzymes expressed by an organism, a tissue, a cell or an organelle of the present invention that allow for conversion of 2-PG into an intermediate of the CBBC do not comprise any enzymes and/or metabolites of the citric acid/TCA cycle. The metabolites of the citric assay/TCA cycle are preferably selected from the group consisting of citrate, isocitrate, 2-keto-glutarate, succinyl-CoA, succinate, fimarate, malate and oxaloacetate. 
     Furthermore, it is also envisaged that an organism, a tissue, a cell or an organelle may employ a pathway of the present invention, wherein said pathway does not involve any anaplerotic/cataplerotic enzymes and/or reaction. An anaplerotic enzyme is an enzyme that catalyzes an anaplerotic reaction. An anaplerotic reaction is a reaction in which a metabolite from lower glycolysis (preferably PEP or pyruvate) is converted into a metabolite of the citric acid/TCA cycle. A cataplerotic enzyme is an enzyme that catalyzes a cataplerotic reaction. A cataplerotic reaction is a reaction in which a metabolite from the TCA cycle is converted into a metabolite of lower glycolysis (preferably PEP or pyruvate). Anaplerotic/cataplerotic enzymes that are not-envisaged in the pathways of the present invention are preferably selected from the group consisting of PEP carboxylase, PEP carboxykinase, pyruvate carboxylase and malic enzyme. In other words the enzymes expressed by an organism, a tissue, a cell or an organelle of the present invention that allow for conversion of 2-PG into an intermediate of the CBBC do not comprise any anaplerotic/cataplerotic enzymes and/or reactions. Anaplerotic/cataplerotic enzymes may comprise or consist of PEP carboxylase, PEP carboxykinase, pyruvate carboxylase and malic enzyme. 
     The pathways according to the present invention as described in the following comprise enzymatic conversions which as such occur in nature and are part of the normal metabolism of certain organisms and for which corresponding enzymes have been described as being able to catalyze the reactions. Other enzymatic conversions which form part of the described pathways have as such not yet been described to occur in nature and, in particular, not in the context of a pathway as described herein. Such enzymatic reactions are sometimes referred herein as “non-native” (enzymatic) conversions or “non-native” reactions. In the appended Figures and elsewhere herein, these enzymatic conversions are indicated by hash keys or bold arrows. The present invention describes options for achieving these enzymatic conversions by using certain enzymes described in the prior art. Thus, in the context of the present invention, the term “non-native conversion” or “non-native reaction” means a chemical transformation for which no specific enzyme has been described so far, but which are expected to be promiscuously catalyzed, to some extent, by an existing enzyme or a variant thereof. Such existing enzyme is originally known to catalyze a different but chemically related reaction and is known or expected to also promiscuously accept the substrate of the non-native reaction. In particular, also mutant variants of one or more of the promiscuous existing enzymes for catalyzing one or more of the non-native reactions may be employed. Such mutant variants may, for example, be derived by the introduction of mutations or other alterations which, for example, alter or improve the enzymatic activity, so as to catalyze the non-native enzymatic conversion more efficiently. In particular, the person skilled in the art may thereby readily achieve higher rates of one or more non-native reaction(s) out of the promiscuous activity(ies). Methods for modifying and/or improving the enzymes or in other words enzyme evolution/engineering techniques are known by the person skilled in the art and are, for example, described herein elsewhere. By combining the different enzymatic conversions described herein, the present invention provides efficient photorespiration bypass pathways. 
     A pathway according to the present invention as described in the following is preferably characterized by the features that 2-PG is converted into an intermediate compound of the CBBC without releasing CO 2  and that this conversion involves as an intermediate
         glycolyl-CoA and/or glycolaldehyde; or   glycolaldehyde 2-phosphate;
 
or that this conversion consumes methylene-THF that results from enzymatic conversion of CO 2 /HCO 3   − .
       

     As mentioned above, one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-glycerate 3-phosphate. In the following, the possible pathways will be described which allow the conversion of 2-PG into D-glycerate 3-phosphate according to preferred embodiments of the present invention. The pathway which allows converting 2-PG into D-glycerate 3-phosphate will be referred to as option “A)” in the following. According to option A) the intermediate compound of the CBBC is D-glycerate 3-phosphate, and the conversion of 2-PG is preferably achieved by:
     a) enzymatic conversion of 2-PG into glycolyl-CoA, further enzymatic conversion of glycolyl-CoA into tartronyl-CoA, further enzymatic conversion of tartronyl-CoA into tartronate semialdehyde, further enzymatic conversion of tartronate semialdehyde into D-glycerate, and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (a respective illustrative example is provided by  FIG. 1A ); or
       enzymatic conversion of 2-PG into glycolyl-CoA, further enzymatic conversion of glycolyl-CoA into tartronyl-CoA, further enzymatic conversion of tartronyl-CoA into tartronate semialdehyde, further enzymatic conversion of tartronate semialdehyde into hydroxypyruvate, further enzymatic conversion of hydroxypyruvate into D-glycerate, and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (a respective illustrative example is provided by  FIG. 3A ; pathway: 2-PG conversion into glycolyl CoA as shown in  FIG. 2 +enzymes 3#, 4#, 25, 18, 6); or by   
       b) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glyoxylate, further enzymatic conversion of glyoxylate into glycine, further enzymatic conversion of glycine into serine, further enzymatic conversion of serine into hydroxypyruvate, further enzymatic conversion of hydroxypyruvate into D-glycerate, and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate,
       wherein said enzymatic conversion of glycine into serine consumes methylene-THF resulting from enzymatic conversion of CO 2  into formate, further enzymatic conversion of formate into formyl-THF, and further enzymatic conversion of formyl-THF into said methylene-THF (a respective illustrative example is provided by  FIG. 1D ); or by   
       c) enzymatic conversion of 2-PG into glycolyl-CoA, further enzymatic conversion of glycolyl-CoA into hydroxypyruvate, further enzymatic conversion of hydroxypyruvate into D-glycerate, and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (respective illustrative examples are provided by  FIG. 4 ; pathways: 2-PG conversion into glycolyl CoA as shown in  FIG. 2 +enzymes 55#, 18, 6; 2-PG conversion into glycolyl CoA as shown in  FIG. 2 +enzymes 55#, 25, 5, 6; 2-PG conversion into glycolyl CoA as shown in  FIG. 2 +enzymes 15, 54#, 18, 6; 2-PG conversion into glycolyl CoA as shown in  FIG. 2 +enzymes 15, 54#, 25, 5, 6).   

     The enzymatic conversions as described in A)a), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described in A)a), above, can be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolyl-CoA into tartronyl-CoA (reaction 3#) as described above in A)a) can, for example, be achieved by a biotin-dependent acyl-CoA carboxylase (EC 6.4.1.X) (this enzyme is an example of enzyme 3#, mentioned herein). In principle, any acyl-CoA carboxylase (EC 6.4.1.X) can be employed for such a conversion. In a preferred embodiment, a promiscuous biotin-dependent acyl-CoA carboxylase (e.g. see Tran T. H. et al., 2015 , Nature  518, 120-124) is used. In a particularly preferred embodiment, the acyl-CoA carboxylase (EC 6.4.1.X) is a propionyl-CoA carboxylase (EC 6.4.1.3) (Hügler M. et al., 2003 , Eur. J. Biochem.  270, 736-744). In one embodiment a propionyl-CoA carboxylase of  Methylobacterium extorquens  (the enzyme is herein also referred to as PCC Me ) may be employed. This enzyme comprises two subunits, generally referred to as propionyl-CoA carboxylase alpha and propionyl-CoA carboxylase beta, respectively, which are encoded by two separate genes. The amino acid sequence of propionyl-CoA carboxylase alpha (pccA) is known and available, e.g., under NCBI accession no.: WP_003599287.1 (nucleic acid sequence encoding the enzyme shown in SEQ ID NO: 1; amino acid sequence shown in SEQ ID NO: 2) The amino acid sequence of propionyl-CoA carboxylase beta (pccB) is known and available, e.g., under NCBI accession no.: WP_003597263.1 (nucleic acid sequence encoding the enzyme shown in SEQ ID NO: 3; amino acid sequence shown in SEQ ID NO: 4). It is of course not only possible to employ in the enzymatic conversion of glycolyl-CoA into tartronyl-CoA an enzyme having the subunits showing the amino acid sequences of SEQ ID NO: 2 and 4, respectively, but it is also possible to employ an enzyme, which has subunits showing related sequences, provided that the enzyme still shows the activity of converting glycolyl-CoA into tartronyl-CoA. 
     The term “related sequences” preferably means sequences showing at least 60%, preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 99% and most preferably at least 99.5% sequence identity to the amino acid sequences shown in SEQ ID NO: 2 or 4, respectively. 
     Those having skill in the art will know how to determine percent identity between/among sequences using, for example, algorithms such as those based on CLUSTALW computer program (Thompson (1994) Nucl. Acids Res. 2:4673-4680), CLUSTAL Omega (Sievers (2014) Curr. Protoc. Bioinformatics 48:3.13.1-3.13.16) or FASTDB (Brutlag (1990) Comp App Biosci 6: 237-245). Also available to those having skill in this art are the BLAST, which stands for Basic Local Alignment Search Tool, and BLAST 2.0 algorithms (Altschul, (1997) Nucl. Acids Res. 25:3389-3402; Altschul (1990) J. Mol. Biol. 215:403-410). The BLASTN program for nucleic acid sequences uses as defaults a word length (W) of 11, an expectation (E) of 10, M=5, N=4, and a comparison of both strands. The BLOSUM62 scoring matrix (Henikoff (1992) Proc. Natl. Acad. Sci. U.S.A. 89:10915-10919) uses alignments (B) of 50, expectation (E) of 10, M=5, N=4, and a comparison of both strands. 
     How to design assays for determining the enzymatic activity of converting glycolyl-CoA into tartronyl-CoA is known to the skilled person. It is for instance possible to use an in vitro assay as described in the appended examples for determining whether an enzyme has the activity of converting glycolyl-CoA into tartronyl-CoA. In one embodiment the assay as described in the example may also be modified with respect to concentration of any components used and/or modification of buffer compositions based on the common general knowledge of skilled person. 
     Such above-mentioned related sequences may, for example also comprise mutated variants showing improved properties. In a preferred embodiment a mutated version of a propionyl-CoA carboxylase of  Methylobacterium extorquens  is employed, which shows an improved activity catalyzing the conversion of glycolyl-CoA into tartronyl-CoA in comparison to the wild-type enzyme. The present invention provides for a non-limiting example of such mutant variant, which has surprisingly been found to have improved activity for catalyzing the conversion of glycolyl-CoA into tartronyl-CoA in comparison to the wild-type enzyme. This non-limiting example is a mutant variant of PCC Me  comprising a pccB mutant variant subunit that comprises the amino acid substitution from aspartate (D) to isoleucine (I) at a position corresponding to position 407 of the pccB amino acid sequence (see SEQ ID NO: 4) and/or the amino acid substitution from tyrosine (Y) to histidine (H) at a position corresponding to position 143 of the pccB amino acid sequence (see SEQ ID NO: 4). For example, a mutant variant of PCC Me  that comprises the two above-mentioned amino acid substitutions but otherwise corresponds to the wild-type sequences may be employed (also referred to herein as PCC Me _D407I_Y143H or pccB_D407I_Y143H_pccA, coding nucleic acid sequence is shown in SEQ ID NO: 5; amino acid sequence is shown in SEQ ID NO: 6) for converting glycolyl-CoA into tartronyl-CoA. The nucleic acid sequence encoding the pccB_D407I_Y143H subunit and the corresponding amino acid sequence are depicted in SEQ ID NO: 5 and 6, respectively. The improved activity of this mutant variant of PCC Me  provided herein to catalyze the enzymatic conversion of glycolyl-CoA into tartronyl-CoA (reaction 3#) is also illustrated in the appended examples. 
     In another embodiment also any other propionyl-CoA carboxylase (EC 6.4.1.3) may be employed which comprises an amino acid substitution at a position corresponding to position 143 of SEQ ID NO: 4 and/or a amino acid substitution at a position corresponding to position 407 of SEQ ID NO: 4. Preferably, the substitution results in an amino acid which is similar to the amino acid substitutions described above for positions 143 and 407 of SEQ ID NO: 4. “Similar” in this context means that the amino acid introduced has a related chemical structure and/or chemical properties. Amino acids with related chemical structures and/or chemical properties are well known in the art. The corresponding positions in the amino acid sequence can, for example be identified by alignments of the amino acid sequences and/or corresponding nucleic acid sequences with the amino acid sequence of pccB (SEQ ID NO: 4) or the nucleic acid sequence (SEQ ID NO: 3) encoding the pccB protein. 
     In order to determine whether a nucleotide residue/position or a amino acid residue/position in a given nucleotide sequence or amino acid sequence, respectively, corresponds to a certain position compared to another nucleotide sequence or amino acid sequence, respectively, the skilled person can use means and methods well known in the art, e.g., alignments, either manually or by using computer programs such as those mentioned herein. For example, BLAST 2.0 can be used to search for local sequence alignments. BLAST or BLAST 2.0, as discussed above, produces alignments of nucleotide sequences to determine sequence similarity. Because of the local nature of the alignments, BLAST or BLAST 2.0 is especially useful in determining exact matches or in identifying similar or identical sequences. Similarly, alignments may also be based on the CLUSTALW computer program (Thompson (1994) Nucl. Acids Res. 2:4673-4680) or CLUSTAL Omega (Sievers (2014) Curr. Protoc. Bioinformatics 48:3.13.1-3.13.16). 
     The further enzymatic conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) as described above in A)a) can, for example, be achieved by an acylating aldehyde dehydrogenase (EC 1.2.1.X) (this enzyme is an example of enzyme 4#, mentioned herein). In principle, any acylating aldehyde dehydrogenase (EC 1.2.1.X) can be employed for such a conversion, preferably a nonspecific acylating aldehyde dehydrogenase enzyme (e.g. see Baker P. et al., 2012 , Biochemistry  51, 4558-4567). In a preferred embodiment, the acylating aldehyde dehydrogenase is a malonyl-CoA reductase (EC 1.2.1.75) (Hügler M et al., 2002, Journal of Bacteriology May 2002, p. 2404-2410). In particular, the malonyl-CoA reductase may be a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase  Erythrobacter  sp. NAP1. The amino acid sequence of malonyl CoA reductase of  Chloroflexus aurantiacus  (MCR Ca ) is known and is available, e.g., under NCBI accession no. AAS20429.1 (nucleic acid sequence is shown in SEQ ID NO: 7; amino acid sequence is shown in SEQ ID NO: 8). The amino acid sequence of malonyl CoA reductase of  Erythrobacter  sp. NAP1 (MCR E ) is known and is available, e.g., under NCBI accession no. WP_007163680.1 (nucleic acid sequence is shown in SEQ ID NO: 9; amino acid sequence is shown in SEQ ID NO: 10). The capability of a MCR E  and MCR Ca  to catalyze the enzymatic conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) is also illustrated in the appended examples. It is of course not only possible to employ in the enzymatic conversion of tartronyl-CoA into tartronate semialdehyde an enzyme having the amino acid sequences of SEQ ID NO: 8 or 10, respectively, but it is also possible to employ an enzyme showing a related sequence, provided that the enzyme still shows the activity of converting tartronyl-CoA into tartronate semialdehyde. 
     The term “related sequences” preferably means sequences showing at least 60%, preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 99% and most preferably at least 99.5% sequence identity to the amino acid sequences shown in SEQ ID NO: 8 or 10, respectively. 
     As regards the determination of percent identity the same applies as has been described herein above. 
     Such above-mentioned related sequences may, for example also comprise mutated variants showing improved properties. In particular, also any mutant variants created by the evolution and optimization strategies described herein elsewhere are included in the related sequences. In a preferred embodiment a mutated version of a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase  Erythrobacter  sp. NAP1 is employed, which shows an improved activity catalyzing the conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) in comparison to the respective wild-type enzyme. 
     How to design assays for determining the enzymatic activity of converting tartronyl-CoA into tartronate semialdehyde is known to the skilled person. It is, for instance, possible to use an in vitro assay as described in the appended examples for determining whether an enzyme has the activity of converting tartronyl-CoA into glycerate with the exception that instead of detecting the formation of glycerate the formation of the product tartronate semialdehyde is detected. The formation of tatronate semialdehyde can, for example, be detected by an HPLC-MS based assay that uses phenylhydrazine. In such assays the tartronate semialdehyde can be covalently derivatized with phenylhydrazine to a phenylhydrazone, which can be detected by its absorbance at 324 nm and confirmed by its corresponding mass spectrum. Concentrations of any components used and/or buffer compositions can be selected analogous to the assay for detecting the activity to convert tartronyl-CoA into glycerate as described in the appended Examples or can also be based on the common general knowledge of a skilled person. Alternatively, the enzymatic activity of converting tartronyl-CoA into tartronate semialdehyde can, for example, also be detected by another assay. In the first step of such an assay the substrate tatronyl CoA is contacted with the respective enzyme (e.g. as described in the appended examples for the assay to measure the conversion from tartronyl-CoA into glycerate) and incubated for a defined time (e.g. as described in the appended examples for the assay to measure the conversion from tartronyl-CoA into glycerate). After the incubation the reaction is stopped, e.g. by heat inactivation, removal of the enzyme or any other means that do not interfere with the downstream analysis and are known to a skilled person. Subsequently, the formation of tatronate semialdehyde is detected by adding the enzyme tartronate semialdehyde reductase from  E. coli  (GarR) and NADH to the inactivated reaction mixture. After further incubation at 30° C. or 37° C. (e.g. for 1 min, 2 min, 3 min, 4 min, 5 min, 6 min, 7 min, 8 min, 9 min, 10 min, 15 min, 20 min, 30 min, 40 min) the decrease in absorbance at 340 nM is spectrophotometrically analyzed to indicate how much NADH was consumed. The measured NADH consumption is directly proportional to the level of tatronate semialdehyde in the initial solution (the reaction is basically irreversible). Further information can be found in THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 49, Issue of December 8, pp. 38780-38786, 2000 (Reuben K. Njau, Carter A. Herndon, and John W. Hawes, Novel b-Hydroxyacid Dehydrogenases in  Escherichia coli  and  Haemophilus influenzae ). In this article an assay, which detects the reverse, unfavorable direction, namely tatronate semialdehyde oxidation is described. 
     The further enzymatic conversion of tartronate semialdehyde into D-glycerate as described in A)a), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. According to one embodiment the conversion can be achieved by directly converting tartronate semialdehyde into D-glycerate (reaction 5). In addition to the enzymes listed in Table 2 also any acylating aldehyde dehydrogenase (EC 1.2.1.X) may be employed for such a conversion. In a preferred embodiment an acylating aldehyde dehydrogenase having alcohol dehydrogenase activity is used. Preferably a nonspecific acylating aldehyde dehydrogenase enzyme (e.g. see Baker P. et al., 2012 , Biochemistry  51, 4558-4567) is employed. In one embodiment, the acylating aldehyde dehydrogenase may be a malonyl-CoA reductase (EC 1.2.1.75 and/or 1.1.1.298) (Hügler M et al., 2002, Journal of Bacteriology May 2002, p. 2404-2410). In a preferred embodiment, the malonyl-CoA reductase may be a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase of  Erythrobacter  sp. NAP1. The amino acid sequence of malonyl-CoA reductase of  Chloroflexus aurantiacus  (MCR Ca ) is known and is available, e.g., under NCBI accession no. AAS20429.1 (nucleic acid sequence is shown in SEQ ID NO: 7; amino acid sequence is shown in SEQ ID NO: 8). The amino acid sequence of malonyl CoA reductase of  Erythrobacter  sp. NAP1 (MCR E ) is known and is available, e.g., under NCBI accession no. WP_007163680.1 (nucleic acid sequence is shown in SEQ ID NO: 9; amino acid sequence is shown in SEQ ID NO: 10). The general capability of both MCR E  and MCR Ca  to catalyze the enzymatic conversion of tatronate semialdehyde into glycerate (reaction 5) is also illustrated in the appended examples. It is of course not only possible to employ in the enzymatic conversion of tartronate semialdehyde into D-glycerate (reaction 5) an enzyme having the amino acid sequences of SEQ ID NO: 8 or 10, respectively, but it is also possible to employ an enzyme showing a related sequence, provided that the enzyme still shows the activity of converting tartronate semialdehyde into D-glycerate (reaction 5). 
     The term “related sequences” preferably means sequences showing at least 60%, preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 99% and most preferably at least 99.5% sequence identity to the amino acid sequences shown in SEQ ID NO: 8 or 10, respectively. 
     As regards the determination of percent identity the same applies as has been described herein above. 
     Such above-mentioned related sequences may, for example also comprise mutated variants showing improved properties. In particular, also any mutant variants created by the evolution and optimization strategies described herein elsewhere are included in the related sequences. In a preferred embodiment a mutated version of a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase  Erythrobacter  sp. NAP1 is employed, which shows an improved activity catalyzing the conversion of tatronate semialdehyde into D-glycerate in comparison to the respective wild-type enzyme. 
     How to design assays for determining the enzymatic activity of converting tatronate semialdehyde into D-glycerate is known to the skilled person. It is, for instance, possible to use an in vitro assay as described in the appended examples for determining whether an enzyme has the activity of converting tatronyl-CoA into D-glycerate (reaction 5) with the only exception that tatronate semialdehyde is employed as substrate instead of tatronyl-CoA. In one embodiment the assay as described in the example may also be modified with respect to concentration of any components used and/or modification of buffer compositions based on the common general knowledge of skilled person. In one embodiment the substrate tatronate semialdehyde may not be provided directly but rather be formed as the product of a second enzymatic reaction (e.g. coupled to the above assay). For instance, an assay in which tatronyl-CoA is provided as substrate and the reaction mixture further comprises a respective enzyme for converting tatronyl-CoA to tatronate semialdehyde (as described herein or known in the art) may be employed (see appended Examples). In principle also any other reaction known in the art resulting in tatronate semialdehyde could also be coupled in order to provide the tatronate semialdehyde substrate 
     In another embodiment, the enzymatic conversion can be achieved by first converting tartronate semialdehyde into hydroxypyruvate (reaction 25) and then further enzymatically converting hydroxypyruvate into D-glycerate (reaction 18). Also these conversions occur naturally (in particular enzymes for converting hydroxypyruvate into D-glycerate occur also in plants) and examples for the corresponding enzymes which can be employed are listed in Table 2. Preferably enzymes for converting hydroxypyruvate into D-glycerate derived from plants are employed. 
     In a preferred embodiment the enzymatic conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5) may also be achieved by a single enzyme or enzyme complex that is capable of accepting both tartronyl-CoA and tatronate semialdehyde as substrate for reduction. In principle, any acylating aldehyde dehydrogenase (EC 1.2.1.X) can be employed for such a conversion. Preferably, a nonspecific acylating aldehyde dehydrogenase enzyme (e.g. see Baker P. et al., 2012 , Biochemistry  51, 4558-4567) is employed. In particular, an acylating aldehyde dehydrogenase enzyme with alcohol dehydrogenase activity is used. In a preferred embodiment, the acylating aldehyde dehydrogenase is a malonyl-CoA reductase (EC 1.2.1.75 and/or EC 1.1.1.298) (Hügler M et al., 2002, Journal of Bacteriology May 2002, p. 2404-2410). In a preferred embodiment, the malonyl-CoA reductase may be a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase of  Erythrobacter  sp. NAP1. The amino acid sequence of malonyl CoA reductase of  Chloroflexus aurantiacus  (MCR Ca ) is known and is available, e.g., under NCBI accession no. AAS20429.1 (nucleic acid sequence is shown in SEQ ID NO: 7; amino acid sequence is shown in SEQ ID NO: 8). The amino acid sequence of malonyl CoA reductase of  Erythrobacter  sp. NAP1 (MCR E ) is known and is available, e.g., under NCBI accession no. WP_007163680.1 (nucleic acid sequence is shown in SEQ ID NO: 9; amino acid sequence is shown in SEQ ID NO: 10). The capability of both MCR E  and MCR Ca  to catalyze an enzymatic conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into glycerate (reaction 5) is also illustrated in the appended examples. 
     It is of course not only possible to employ in the enzymatic conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5) an enzyme having the amino acid sequences of SEQ ID NO: 8 or 10, respectively, but it is also possible to employ an enzyme showing a related sequence, provided that the enzyme still shows the activity of converting tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5). 
     The term “related sequences” preferably means sequences showing at least 60%, preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 99% and most preferably at least 99.5% sequence identity to the amino acid sequences shown in SEQ ID NO: 8 or 10, respectively. 
     As regards the determination of percent identity the same applies as has been described herein above. 
     Such above-mentioned related sequences may, for example also comprise mutated variants showing improved properties. In particular, also any mutant variants created by the evolution and optimization strategies described herein elsewhere are included in the related sequences. In a preferred embodiment a mutated version of a malonyl-CoA reductase of  Chloroflexus aurantiacus  or a malonyl-CoA reductase  Erythrobacter  sp. NAP1 is employed, which shows an improved activity catalyzing the conversion of tartronyl-CoA into tartronate semialdehyde (reaction 4#) and/or tatronate semialdehyde into D-glycerate (reaction 5) in comparison to the respective wild-type enzyme. 
     How to design assays for determining the enzymatic activity of converting tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5) is known to the skilled person. In principle the enzymatic activity of the enzyme can be tested by testing for the conversions of tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5) separately (as described above) or by testing for the capability of an enzyme to convert tartronyl-CoA into D-glycerate (reaction 4# and 5 combined). To test the enzymatic activity of converting tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5) it is, for instance, possible to use any of the in vitro assays as described in the appended examples for determining whether an enzyme has the activity of converting tartronyl-CoA into tartronate semialdehyde (reaction 4#) and tatronate semialdehyde into D-glycerate (reaction 5). In one embodiment the assay as described in the example may also be modified with respect to concentration of any components used and/or modification of buffer compositions based on the common general knowledge of skilled person. 
     Similarly, the enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (reaction 6) as described in A)a), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known, in particular also in plants. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes, preferably enzymes derived from plants, can be employed in the context of the present invention. 
     The enzymatic conversions as described in A)b), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate (reaction 1) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known, in particular also in plants. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes, preferably enzymes derived from plants, can be employed in the context of the present invention. 
     The further enzymatic conversion of glycolate into glyoxylate (reaction 12) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. 
     Similarly, the enzymatic conversion of glyoxylate into glycine (reaction 13) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. 
     The further enzymatic conversion of glycine into serine (reaction 14) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known, in particular also in plants. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes, preferably enzymes derived from plants, can be employed in the context of the present invention. The enzymatic conversion of glycine into serine (reaction 14) as described in A)b), above, is preferably a conversion which consumes methylene-THF resulting from the enzymatic conversion of CO 2  into formate (reaction 15#), further enzymatic conversion of formate into formyl-THF (reaction 16), and further enzymatic conversion of formyl-THF into said methylene-THF (reaction 17). 
     The enzymatic conversion of CO 2  into formate can, for example, be achieved by any type of formate dehydrogenase, preferably ferredoxin-dependent formate dehydrogenase (EC 1.1.99.X) (these enzymes are examples of enzyme 15# mentioned herein) (Hyunjun Choe et al., 2015 , Acta Cryst. D 71, 313-323; Schuchmann K. et al., 2014 , Nat. Rev. Microbiol.  12 (12), 809-21). In principle, any ferredoxin-dependent formate dehydrogenase (EC 1.1.99.X) can be employed for such a conversion. When a ferredoxin-dependent formate dehydrogenase is used, ferredoxin can be reduced by electrons donated directly from components of the electron transport chain, including one of the photosystems. The enzymatic conversions of formate into formyl-THF (reaction 16), of formyl-THF into said methylene-THF (reaction 17) occur naturally (in particular enzymes occur also in plants) and examples for the corresponding enzymes which can be employed are listed in Table 2. Preferably enzymes derived from plants are employed. 
     The further enzymatic conversion of serine into hydroxypyruvate (reaction 13) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. 
     The further enzymatic conversion of hydroxypyruvate into D-glycerate (reaction 18) as described in A)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known, in particular also in plants. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes, preferably enzymes derived from plants, can be employed in the context of the present invention. 
     The further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (reaction 6) as described in A)b) above, can be achieved as described in connection with A)a) above. 
     The enzymatic conversions as described in A)c), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described in A)c), above, can be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolyl-CoA into hydroxypyruvate as described in A)c) above can be achieved in different ways. Preferably, this enzymatic conversion is designed in a manner that it consumes directly or indirectly CO 2 . A direct consumption of CO 2  means that the enzymatic conversion of glycolyl-CoA into hydroxypyruvate involves the direct incorporation of (the carbon atom of) CO 2 . An indirect consumption of CO 2  means that (the carbon atom of) CO 2  is first converted (e.g. preferably reduced to formic acid) and/or incorporated into another compound and then incorporated into glycolyl-CoA. Examples for a direct or indirect consumption of CO 2  by the conversion of glycolyl-CoA into hydroxypyruvate will be described in the following and are represented by reactions 54# and 55#. For example, the conversion of glycolyl-CoA into hydroxypyruvate can be achieved by a (reversible) pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) (this enzyme is an example of enzyme 55#) resulting in a consumption of CO 2  due to a direct incorporation. Alternatively, the conversion of glycolyl-CoA into hydroxypyruvate can be achieved by a (fully reversible) pyruvate formate lyase enzyme (EC 2.3.1.54) (this enzyme is an example of enzyme 54#, mentioned herein). 
     Thus, in one embodiment the enzymatic conversion of glycolyl-CoA into hydroxypyruvate as described in A)c), above, can, for example, be achieved by a (reversible) pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) (this enzyme is an example of enzyme 55#, mentioned herein), also referred to as pyruvate synthase (EC 1.2.7.1) (Furdui C. et al., 2000 , J Biol Chem  275: 28494-28499). Some pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) variants are known to be promiscuous in the substrates that they can accept (e.g. Fukuda E. et al., 2002 , Biochim Biophys Acta  1597: 74-80). Accordingly, it is expected that glycolyl-CoA can also serve as a substrate for pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) or at least for some pyruvate:ferredoxin oxidoreductase variants. In principle, any pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) can be employed for such a conversion. In the context of the present invention, preferably pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) variants that accept glycolyl-CoA (at a high frequency) are employed. The enzymatic conversion of glycolyl-CoA into hydroxypyruvate achieved by a (reversible) pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) preferably (directly) consumes CO 2 . 
     While pyruvate:ferredoxin oxidoreductase enzymes (EC 1.2.7.1) are typically oxygen sensitive, several bacteria and archea exist that operate this enzyme under full microaerobic or aerobic conditions. For the enzymatic conversion of glycolyl-CoA into hydroxypyruvate in the context of the present invention, in particular, a pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) which is not or minimally oxygen sensitive and/or exhibits enzymatic activity under aerobic conditions (e.g. a pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) originating from  Hydrogenobacter thermophilus  TK-6,  Sulfolobus  sp. strain 7 or  Halobacterium halobium ) is employed. Several bacteria and archea, including but not limited to  Hydrogenobacter thermophilus  TK-6 (Yoon K. S. et al., 1997 , Arch Microbiol  167: 275-279),  Sulfolobus  sp. strain 7 (Fukuda E. et al., 2002, Biochim Biophys Acta 1597: 74-80) and  Halobacterium halobium  (Plaga W. et al., 1992, Eur J Biochem 205: 391-397), express pyruvate:ferredoxin oxidoreductase enzymes (EC 1.2.7.1) that operate under full microaerobic or aerobic conditions and are not or minimally oxygen sensitive. In another embodiment, a pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) originating from a host different from the organism, tissue thereof, cell thereof or organelle thereof of the current invention is employed for the enzymatic conversion of glycolyl-CoA into hydroxypyruvate. Multiple studies indicate that the maturation of a pyruvate:ferredoxin oxidoreductase enzyme can occur correctly under aerobic conditions when expressed in a foreign host (Fukuda E. et al., 2002, loc. cit.; Yamamoto M., 2003, Biochem Biophys Res Commun 312: 1297-1302). 
     The enzymatic conversion of glycolyl-CoA into hydroxypyruvate achieved, for example, by a pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1), can involve the oxidation of ferredoxin. In the context of this embodiment, preferably a pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1), capable of accepting the ferredoxin of the organism/tissue/cell/organelle used in the context of the present invention, is employed. For example, several studies indicate that plant-like ferredoxin can replace the native ferredoxin used by pyruvate:ferredoxin oxidoreductase enzymes (EC 1.2.7.1) with only a little effect on activity (Pieulle L. et al., 2004 , Biochemistry  43: 15480-15493). 
     In the context of a plant/plant tissue/plant cell/plant organelle according to the current invention, preferably a pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) accepting plant ferredoxin is employed. The pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) from  Desulfovibrio africanus  is for example known to accept e.g. algal ferredoxin, resulting in 60% of the original rate (Pieulle L. et al., 2004 , Biochemistry  43: 15480-15493). Alternatively, pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) variants that use NADPH as electron donor, instead of ferredoxin, are employed for the enzymatic conversion of glycolyl-CoA into hydroxypyruvate. An example for an NADPH-dependent pyruvate:ferredoxin oxidoreductase enzyme which is, however, non-limiting, is the pyruvate:ferredoxin oxidoreductase enzyme (EC 1.2.7.1) from  Euglena gracilis  (Inui H., 1987 , J Biol Chem  262: 9130-9135). Preferably, an NADPH-dependent pyruvate: ferredoxin oxidoreductase enzyme (EC 1.2.7.1) employed in the current invention is also capable of operating under (micro)aerobic conditions. 
     In another embodiment, the further enzymatic conversion of glycolyl-CoA into hydroxypyruvate as described in A)c), above, may, for example, be achieved by a (fully reversible) pyruvate formate lyase enzyme (EC 2.3.1.54) (this enzyme is an example of enzyme 54#, mentioned herein) (Buis J. M. et al., 2005 , Arch Biochem Biophys  433: 288-296). Some variants of pyruvate formate lyase (EC 2.3.1.54) are known to have broad substrate specificity (Hesslinger C. et al., 1998 , Mol Microbiol  27: 477-492; Sawers G. et al., 1998 , J Bacteriol  180: 3509-3516) and hence pyruvate formate lyase enzymes (EC 2.3.1.54) or at least some variants thereof are expected to accept glycolyl-CoA. In principle, any pyruvate formate lyase enzyme (EC 2.3.1.54) may be employed for the enzymatic conversion of glycolyl-CoA into hydroxypyruvate. Preferably, in the context of the current invention a pyruvate formate lyase enzyme variant (EC 2.3.1.54) that accepts glycolyl-CoA (at a high frequency) is employed. 
     The reaction catalyzed by pyruvate formate lyase (EC 2.3.1.54) takes place via a radical mechanism, which involves a glycyl radical (Becker A. et al., 1999 , Nat Struct Biol  6: 969-975; Plaga W. et al., 2000 , FEBS Lett  466: 45-48; Becker A. et al., 2002 , J Biol Chem  277: 40036-40042). In a preferred embodiment, a pyruvate formate lyase activating enzyme (PFL-AE) is employed to generate the stable and catalytically essential glycyl radical for the reaction catalyzed by pyruvate formate lyase (EC 2.3.1.54) (Buis J. M. et al., 2005, loc. cit.; Vey J. L. et al., 2008 , Proc Natl Acad Sci USA  105: 16137-16141). The glycyl radical is in principle susceptible to destruction by oxygen, which results in irreversible cleavage of the polypeptide and inactivation of pyruvate formate lyase (EC 2.3.1.54) (Sawers G. et al., 1998 , Mol Microbiol  29: 945-954; Zhang W. et al., 2001 , Biochemistry  40: 4123-4130). However, previous studies have shown that, for example,  E. coli  cells grown under microaerobic conditions produce a significant amount of formate, indicating that pyruvate formate lyase (EC 2.3.1.54) retains its activity in the presence of oxygen (Alexeeva S. et al., 2000 , J Bacteriol  182: 4934-4940; Levanon S. S. et al., 2005 , Biotechnol Bioeng  89: 556-564; Zhu J. et al., 2007 , Biotechnol Bioeng  97: 138-143). In the context of the current invention, preferably pyruvate formate lyase (EC 2.3.1.54) variants that have increased oxygen tolerance/enzymatic activity under aerobic conditions (e.g. evolved by methods as described elsewhere) are employed. In particular, for example, the product of the yfiD gene in  E. coli  may also be employed to increase the oxygen tolerance/enzymatic activity under aerobic conditions of pyruvate formate lyase (EC 2.3.1.54). The product of the yfiD gene in  E. coli  was shown to reactivate pyruvate formate lyase (EC 2.3.1.54) in the presence of oxygen by replacing its fragmented part (Zhu J. et al., 2007, loc. cit.; Wagner A F, 2001, Biochem Biophys Res Commun 285: 456-462). 
     The enzymatic conversion of glycolyl-CoA into hydroxypyruvate achieved by a (fully reversible) pyruvate formate lyase enzyme (EC 2.3.1.54) is preferably a conversion which consumes formic acid resulting from the enzymatic conversion of CO 2  into formate (reaction 15#). The enzymatic conversion of CO 2  into formate (reaction 15#) in this context, may be achieved by a ferredoxin-dependent formate dehydrogenase (EC 1.1.99.X) or another type of formate dehydrogenase as described in A)b) above. 
     The further enzymatic conversion of hydroxypyruvate into D-glycerate as described in A)c), above, is a conversion which does naturally occur and for which enzymes catalyzing this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes may be employed in the context of the present invention. 
     According to one embodiment the conversion of hydroxypyruvate into D-glycerate as described above in A)c) can be achieved by directly converting hydroxypyruvate into D-glycerate (reaction 18). Examples for corresponding enzymes which are known to catalyze this conversion occur naturally, in particular also in plants. Preferably enzymes for converting hydroxypyruvate into D-glycerate derived from plants are employed in the context of the current invention. 
     In another embodiment, the enzymatic conversion of hydroxypyruvate into D-glycerate as described in A)c), above, can be achieved by first enzymatically converting hydroxypyruvate into tartronate semialdehyde (reaction 25) and further enzymatically converting tartronate semialdehyde into D-glycerate (reaction 5). Both conversions occur naturally and enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes may be employed in the context of the present invention. 
     The further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (reaction 6) as described in A)c) above, can be achieved as described in connection with A)a) above. 
     As mentioned above, in another embodiment one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-ribulose 1,5-bisphosphate. In the following, the possible pathways will be described which allow the conversion of 2-PG into D-ribulose 1,5-bisphosphate according to preferred embodiments of the present invention. The pathway which allows converting 2-PG into D-ribulose 1,5-bisphosphate will be referred to as option “B)” in the following. According to option B) the intermediate compound of the CBBC is D-ribulose 1,5-bisphosphate, and the conversion of 2-PG is preferably achieved by:
     a) enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate, and further enzymatic conversion of D-ribulose 1-phosphate into D-ribulose 1,5-bisphosphate (a respective illustrative example is provided by  FIG. 1B ); or   b) enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate, further enzymatic conversion of D-ribulose 1-phosphate into D-ribose 1-phosphate, further enzymatic conversion of D-ribose 1-phosphate into D-ribose 1,5-bisphosphate, and further enzymatic conversion of D-ribose 1,5-bisphosphate into D-ribulose 1,5-bisphosphate (a respective illustrative example is provided by  FIG. 3B ; pathway: 2-PG conversion into glycolaldehyde as shown in  FIG. 2 +enzymes 8, 29#, 31, 32); or   c) enzymatic conversion of 2-PG into 2-phosphoglycolyl phosphate, further enzymatic conversion of 2-phosphoglycolyl phosphate into glycolaldehyde 2-phosphate, and further enzymatic conversion of glycolaldehyde 2-phosphate into D-ribulose 1,5-bisphosphate (a respective illustrative example is provided by  FIG. 3B ; pathway: 2-PG conversion into glycolaldehyde 2-phosphate as shown in  FIG. 2  (enzymes 23# and 24#)+enzyme 28#).   

     The enzymatic conversions as described in B)a), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in B)a), above, can be achieved by different pathways as will be described further below. 
     The enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate (reaction 8), which can be achieved, for example, by condensation of glycolaldehyde with dihydroxyacetone phosphate, as described in B)a), above, is a conversion which does naturally occur and for which enzymes catalyzing this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. 
     The enzymatic conversion of D-ribulose 1-phosphate into D-ribulose 1,5-bisphosphate (reaction 9#) as described in B)a), above, can for example be achieved by a 1-phosphofructokinase (EC 2.7.1.56) or a ribulokinase (EC 2.7.1.16) (these enzymes are examples for enzyme 9# mentioned herein). In principle any 1-phosphofructokinase (EC 2.7.1.56) or a ribulokinase (EC 2.7.1.16) can be employed for this purpose. 
     As regards 1-phosphofructokinase, it is known that several of these enzymes confuse D-ribulose and D-fructose—e.g., fructose 1,6-bisphosphatase can dephosphorylate ribulose 1,5-bisphosphate (Mizunuma H. et al., 1980 , Arch Biochem Biophys  201, 296-303; Donahue J. L. et al., 2000 , J Bacteriol  182, 5624-5627) and phosphoribulokinase can phosphorylate fructose 6-phosphate (Siebert K. et al., 1981 , Biochim Biophys Acta  658, 35-44). Thus, these enzymes are suitable for the described conversion of D-ribulose 1-phosphate into D-ribulose 1,5-bisphosphate. 
     As regards ribulokinase, it is preferred to employ in the present invention a promiscuous variant of D-ribulose 5-kinase (e.g. see Lee L. V. et al., 2001 , Arch Biochem Biophys  396, 219-224) which can accept D-ribulose 1-phosphate as an alternative substrate. 
     The enzymatic conversions as described in B)b), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in B)b), above, can be achieved by different pathways as will be described further below. 
     The enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate (reaction 8), for example by condensation of glycolaldehyde with dihydroxyacetone phosphate, as described in B)b) above, can be achieved as described in connection with B)a) above. 
     The enzymatic conversion of D-ribulose 1-phosphate into D-ribose 1-phosphate (reaction 29#) as described in B)b), above, can for example be achieved by a 5-methylthio-D-ribulose 1-phosphate 1,2-isomerase (this enzyme is an example for enzyme 29# mentioned herein). In principle any 5-methylthio-D-ribulose 1-phosphate 1,2-isomerase can be employed for this purpose, preferably a promiscuous 5-methylthio-D-ribulose 1-phosphate 1,2-isomerase. An example is the enzyme referred to as Rru_A0360 (Saito Y. et al., 2007 , Biochem  71, 2021-2028; Erb T. J. et al., 2012 , Nat Chem Biol  8, 926-932). 
     According to this embodiment, D-ribulose 1-phosphate can also be assimilated to the CBBC via its isomerisation to D-ribose 1-phosphate (reaction 29# in  FIG. 3 ). In a preliminary study it was found that this reaction can be catalyzed by the enzyme Rru_A0360 with measurable rate (k cat =0.03 s −1 , k cat /K M &lt;20 M −1 s −1 ). Preferably, such rate can even be evolutionary further optimized as described herein elsewhere. 
     The enzymatic conversion of D-ribose 1-phosphate into D-ribose 1,5-bisphosphate (reaction 31) as described in B)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. In particular, D-ribose 1-phosphate can be phosphorylated to D-ribose 1,5-bisphosphate (reaction 31) by an ADP-dependent ribose-1-phosphate kinase. 
     The enzymatic conversion of D-ribose 1,5-bisphosphate into D-ribulose 1,5-bisphosphate (reaction 32) as described in B)b), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. 
     Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. In particular, D-ribose 1,5-bisphosphate can be isomerised to D-ribulose 1,5-bisphosphate (reaction 32) by ribose-1,5-bisphosphate isomerase (Aono R. et al., 2015 , Nat Chem Biol  11, 355-360). 
     The enzymatic conversions as described in B)c), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into 2-phosphoglycolyl phosphate (reaction 23#) as described in B)c), above, can for example be achieved by transferring a phosphate group from another carboxylic acid or by utilizing a kinase enzyme such as 3-phosphoglycerate kinase: 2-PG was found to be a competitive inhibitor of this enzyme (Tompa P. et al., 1986 , Eur J Biochem  154, 643-649; Vas M., 1990 , Eur J Biochem  194, 639-645; Szilagyi A. N. et al., 1998 , Biochemistry  37, 8551-8563), indicating that it can also serve as a substrate for at least some enzyme variants. Accordingly, in a preferred embodiment the enzymatic conversion of 2-PG into 2-phosphoglycolyl phosphate as described in B)c), above, can for example be achieved by a 3-phosphoglycerate kinase (EC 2.7.2.3) (this enzyme is an example for enzyme 23# mentioned herein). In principle any 3-phosphoglycerate kinase (EC 2.7.2.3) can be employed for this conversion. 
     The enzymatic conversion of 2-phosphoglycolyl phosphate into glycolaldehyde 2-phosphate (reaction 24#) as described in B)c), above, can for example be achieved by a phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (this enzyme is an example for enzyme 24# mentioned herein). A phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) is known to catalyze the reduction of glycolyl phosphate (Fife T. H. et al., 1970 , Biochemistry  9, 4064-4067; Armstrong J. M. et al., 1976 , Biochem J  159, 513-527; Byers L. D., 1978 , Arch Biochem Biophys  186, 335-342) and the presence of a terminal phosphate moiety is known to enhance the reactivity (Byers L. D., 1978 loc. cit.). In principle, any phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) can be employed for this conversion. 
     The enzymatic conversion of glycolaldehyde 2-phosphate into D-ribulose 1,5-bisphosphate (reaction 28#) as described in B)c), above, can be achieved by a L-fuculose-phosphate aldolase (EC 4.1.2.17) (this enzyme is an example for enzyme 28# mentioned herein), an enzyme that can also condense glycolaldehyde and dihydroxyacetone phosphate (Ghalambor M. A. et al., 1962 , J Biol Chem  237, 2427-2433; Ghalambor, M. A. et al., 1966 , Methods Enzymol  9, 538-542). In principle, any L-fuculose-phosphate aldolase (EC 4.1.2.17) can be employed for this conversion. Preferably, an L-fuculose-phosphate aldolase (EC 4.1.2.17) derived from  E. coli  can be employed for this conversion. 
     As mentioned above, in another embodiment one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-erythrose 4-phosphate. In the following, the possible pathways will be described which allow the conversion of 2-PG into D-erythrose 4-phosphate according to preferred embodiments of the present invention. The pathway which allows converting 2-PG into D-erythrose 4-phosphate will be referred to as option “C)” in the following. According to option C) the intermediate compound of the CBBC is D-erythrose 4-phosphate, and the conversion of 2-PG is preferably achieved by:
     a) enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-erythrose, and further enzymatic conversion of D-erythrose into D-erythrose 4-phosphate (a respective illustrative example is provided by  FIG. 1C );   b) enzymatic conversion of 2-PG into glycolyl-CoA, further enzymatic conversion of glycolyl-CoA into 2,4-dihydroxy-3-oxo-butyryl-CoA, further enzymatic conversion of 2,4-dihydroxy-3-oxo-butyryl-CoA into 2,3,4-trihydroxy-3-oxo-butyryl-CoA, further enzymatic conversion of 2,3,4-trihydroxy-3-oxo-butyryl-CoA into a D-aldotetrose or a L-aldotetrose, and further enzymatic conversion of said D-aldotetrose or said L-aldotetrose into D-erythrose 4-phosphate, wherein said D-aldotetrose is D-erythrose or D-threose, and wherein said L-aldotetrose is L-erythrose or L-threose.   

     The enzymatic conversions as described in C)a), above, can, for example, be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in C)a), can be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolaldehyde into D-erythrose (reaction 10#) as described in C)a) can, for example, be achieved by an aldolase (EC 4.1.2.X) (this enzyme is an example for enzyme 10# mentioned herein). In principle, any aldolase (EC 4.1.2.X) can be employed for this conversion. Preferably, a nonspecific aldolase, which can accept unphosphorylated donor and acceptor, and catalyze a reaction with glycolaldehyde as an acceptor (e.g. see Schürmann M. et al., 2001 , J. Mol. Catal. B: Enzym.  19-20, 247-252; Chiu T. H. et al., 1969 , Biochemistry  8, 98-108) is employed in the context of the present invention. In a preferred embodiment the aldolase employed is a fructose 6-phosphate aldolase or a xylulose 1-phosphate aldolase (Schirmann M., 2002 , Journal of Molecular Catalysis B: Enzymatic  19-20, 247-252). 
     The further enzymatic conversion of D-erythrose into D-erythrose 4-phosphate (reaction 11#) as described in C)a) can, for example, be achieved by a dihydroxyacetone kinase (EC 2.7.1.29; Herz S. et al., 2002 , Phytochemistry  60, 3-11) (this enzyme is an example for enzyme 11# mentioned herein). In principle, any dihydroxyacetone kinase (EC 2.7.1.29) can be employed for this conversion. 
     The enzymatic conversions as described in C)b), above, can, for example, be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described in C)b), can be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolyl-CoA into 2,4-dihydroxy-3-oxo-butyryl-CoA (reaction 56#) as described in C)b) can, for example, be achieved by an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) (this enzyme is an example for enzyme 56# mentioned herein). In principle, any acetyl-CoA C-acetyltransferase (EC 2.3.1.9) can be employed for this conversion. Preferably, two molecules of glycolyl-CoA are enzymatically converted by an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) into 2,4-dihydroxy-3-oxo-butyryl-CoA. Preferably, an acetyl-CoA C-acetyltransferase (EC 2.3.1.9), which can accept glycolyl-CoA as donor and/or can accept glycolyl-CoA as an acceptor is employed in the context of the present invention. In a preferred embodiment the acetyl-CoA C-acetyltransferase (EC 2.3.1.9) bktB (UniProt accession code Q0KBP1; entry version 66 (9 Dec. 2015)) from  Cupriavidus necator  H16 (formerly known as  Ralstonia eutropha  H16) is employed. This acetyl-CoA C-acetyltransferase can substitute the donor acetyl-CoA with glycolyl-CoA and can further substitute the acceptor acetyl-CoA with glycolyl-CoA (Martin C H et al., 2013 , Nat Commun  4, 1414). Hence, this enzyme can catalyze the condensation of two glycolyl-CoA molecules to generate 2,4-dihydroxy-3-oxobutyryl-CoA. 
     The further enzymatic conversion of 2,4-dihydroxy-3-oxo-butyryl-CoA into 2,3,4-trihydroxy-3-oxo-butyryl-CoA (reaction 57#) as described in C)b) can, for example, be achieved by a 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) (this enzyme is an example for enzyme 57# mentioned herein). In principle, any 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) can be employed for this conversion. Preferably, a 3-hydroxybutyryl-CoA dehydrogenase, which has a high specificity for 2,4-dihydroxy-3-oxo-butyryl-CoA as a substrate is employed. 
     Moreover, the further enzymatic conversion of 2,3,4-trihydroxy-3-oxo-butyryl-CoA into a D-aldotetrose or a L-aldotetrose (reaction 125#) as described in C)b) can, for example, be achieved by an aldehyde dehydrogenase (acetylating, EC. 1.2.1.X). This enzyme is an example for enzyme 125# mentioned herein). A preferred D-aldotetrose is D-erythrose or D-threose. In principle, any aldehyde dehydrogenase (acetylating, EC. 1.2.1.X) can be employed for the enzymatic conversion of 2,3,4-trihydroxy-3-oxo-butyryl-CoA into a D-aldotetrose or a L-aldotetrose. Preferably, an aldehyde dehydrogenase (acetylating, EC. 1.2.1.X), which has a high specificity for 2,3,4-trihydroxy-3-oxo-butyryl-CoA as a substrate is employed. 
     The further enzymatic conversion of a D-aldotetrose or a L-aldotetrose into D-erythrose 4-phosphate as described in C)b) can, for example, be achieved by any of the interconversion pathways shown in  FIG. 3L  (lower panel; respective enzymes and further information as regards the reactions of these pathways are provided in Table 3). As mentioned above, a preferred D-aldotetrose is D-erythrose or D-threose. 
     In particular, the enzymatic conversion of D-erythrose (a preferred D-aldotetrose) into D-erythrose 4-phosphate (reaction Z44#; also referred to as 11# herein) can, for example, be achieved by a sugar kinase (EC 2.7.1.X) (this enzyme is an example for enzyme Z44# and enzyme 11# mentioned herein). In principle, any sugar kinase (EC 2.7.1.X) can be employed for this conversion. Preferably, a dihydroxyacetone kinase (EC 2.7.1.29; Herz S. et al., 2002 , Phytochemistry  60, 3-11) (this enzyme is an example for enzyme Z44# and enzyme 11# mentioned herein) is employed. In principle, any dihydroxyacetone kinase (EC 2.7.1.29) can be employed for this conversion. A respective example is described in Herz et al. 
     Furthermore, the enzymatic conversion of D-threose (a preferred D-aldotetrose) into D-erythrose 4-phosphate can, for example, be achieved by the enzymatic conversion of D-threose into D-erythrose (reaction Z31#), and the further enzymatic conversion of D-erythrose into D-erythrose 4-phosphate (reaction Z44#; also referred to as 11# herein). The enzymatic conversion of D-threose into D-erythrose (reaction Z31#) can, for example, be achieved by a sugar epimerase (EC 5.1.3.X) (this enzyme is an example for enzyme Z31# mentioned herein). In principle, any sugar epimerase (EC 5.1.3.X) can be employed for this conversion. Similarly, in principle also any sugar isomerase (EC 5.3.1.X) having sugar epimerase activity can be can be employed. Preferably, a xylose isomerase (EC 5.3.1.5; see, e.g., Vuolanto A et al., 2002 , Biocatalysis and Biotransformation  20, 235-240) and/or a L-rhamnose isomerase (5.3.1.14; see, e.g., Leang K et al., 2004 , Biochim Biophys Acta  1674, 68-77) is/are employed for this conversion. In principle any xylose isomerase and/or any L-rhamnose isomerase can be employed for this conversion. Preferably, an enzyme referred to in Vuolanto A et al. or Leang K et al. such as the xylose isomerase from  Streptomyces rubiginosus  (UniProt: P24300; entry version 119 (20 Jan. 2016)) is employed. The further enzymatic conversion of D-erythrose into D-erythrose 4-phosphate (reaction Z44#; also referred to as 11# herein) can, for example, be achieved as described further above. 
     Alternatively, the enzymatic conversion of D-threose (a preferred D-aldotetrose) into D-erythrose 4-phosphate can, for example, be achieved by the enzymatic conversion of D-threose into D-threose 4-phosphate (reaction Z45#), and further enzymatic conversion of D-threose 4-phosphate into D-erythrose 4-phosphate (reaction Z28#). 
     The enzymatic conversion of D-threose into D-threose 4-phosphate (reaction Z45#) can, for example, be achieved by a sugar kinase (EC 2.7.1.X) (this enzyme is an example for enzyme Z45# mentioned herein). In principle any sugar kinase (EC 2.7.1.X) can be employed for this conversion. Preferably, a sugar kinase (EC 2.7.1.X), which has a high specificity for D-threose as a substrate is employed. 
     The further enzymatic conversion of D-threose 4-phosphate into D-erythrose 4-phosphate (reaction Z28#) can, for example, be achieved by a sugar epimerase (EC 5.1.3.X) (this enzyme is an example for enzyme Z28# mentioned herein). In principle any sugar epimerase (EC 5.1.3.X) can be employed for this conversion. Preferably, a sugar epimerase (EC 5.1.3.X), which has a high specificity for D-threose 4-phosphate as a substrate is employed. 
     In an embodiment, in which an L-aldotetrose (L-threose or L-erythrose) is enzymatically converted to D-erythrose 4-phosphate, for example one of the enzymatic pathways shown in  FIG. 3L  (lower panel; respective enzymes and further information as regards the reactions of these pathways are provided in Table 3), which comprises the conversion of erythritol 4-phosphate to D-erythrose 4-phosphate (reaction Z34#) can be employed. This reaction can, for example, be achieved by an alcohol-sugar dehydrogenase (EC 1.1.1.X). 
     As mentioned above, in another embodiment one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-ribose 5-phosphate. In the following, the possible pathways will be described which allow the conversion of 2-PG into D-ribose 5-phosphate according to preferred embodiments of the present invention. The pathway which allows converting 2-PG into D-ribose 5-phosphate will be referred to as option “D)” in the following. According to option D) the intermediate compound of the CBBC is D-ribose 5-phosphate, and the conversion of 2-PG is preferably achieved by: 
     enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate, further enzymatic conversion of D-ribulose 1-phosphate into D-ribose 1-phosphate, and further conversion of D-ribose 1-phosphate into D-ribose 5-phosphate (a respective illustrative example is provided by  FIG. 3B ; pathway: 2-PG conversion into glycolaldehyde as shown in  FIG. 2 +enzymes 8, 29#, 30). 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in D) can, for example, be achieved by different pathways as will be described further below. 
     The enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate (reaction 8) as described in D), is a conversion which does naturally occur and can, for example, be achieved as described above for B)a) or B)b). 
     The further enzymatic conversion of D-ribulose 1-phosphate into D-ribose 1-phosphate (reaction 29#) as described in D) can, for example, be achieved by a 5-methylthio-D-ribulose 1-phosphate 1,2-isomerase as described in connection with B), above. 
     The further enzymatic conversion of D-ribose 1-phosphate into D-ribose 5-phosphate (reaction 30) as described in D) is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known (Hammer-Jespersen K. et al., 1970 , Eur J Biochem  17, 397-407). Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. 
     As mentioned above, in another embodiment one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-ribulose 5-phosphate. In the following, the possible pathways will be described which allow the conversion of 2-PG into D-ribulose 5-phosphate according to preferred embodiments of the present invention. The pathway which allows converting 2-PG into D-ribose 5-phosphate will be referred to as option “E)” in the following. According to option E) the intermediate compound of the CBBC is D-ribulose 5-phosphate, and the conversion of 2-PG is preferably achieved by: 
     enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-arabinose 5-phosphate, and further enzymatic conversion of D-arabinose 5-phosphate into D-ribulose 5-phosphate (a respective illustrative example is provided by  FIG. 1E ). 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in E) can, for example, be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolaldehyde into D-arabinose 5-phosphate (reaction 78#) as described in E) can, for example, be achieved by an aldolase (EC 4.1.2.X). Preferably, the enzymatic conversion of glycolaldehyde into D-arabinose 5-phosphate is achieved by the aldol condensation of glycolaldehyde (as a donor) with D-glyceraldehyde 3-phosphate (as an acceptor). In principle, any aldolase (EC 4.1.2.X) can be employed for the conversion of glycolaldehyde into D-arabinose 5-phosphate. Preferably, an aldolase, which is able to catalyze the aldol condensation of glycolaldehyde (as a donor) with D-glyceraldehyde 3-phosphate (as an acceptor), thus yielding D-arabinose 5-phosphate, is employed. An example for such an enzyme is a D-fructose 6-phosphate aldolase (an enzyme belonging to EC 4.1.2.X, which has not yet been assigned to a own EC number within this class of enzymes) (this enzyme is in particular a representative example for enzyme 78# mentioned herein). Even more preferably, an aldolase that has a substrate affinity that is characterized by a K M  below 1 mM towards glycolaldehyde (as a donor) and D-glyceraldehyde 3-phosphate (as an acceptor) and/or that achieves the condensation with 16.5&lt;k cat &lt;173 sec −1  is employed. Particularly preferred is an aldolase that is further characterized in that the affinity of the enzyme towards dihydroxyacetone (as a donor) is considerably worse/lower than for glycolaldehyde (as a donor). Preferred is a ratio of at least 5 times, preferably at least 10 times, even more preferably at least 15 times and most preferably at least 20 times between the respective affinities (defined by K M , wherein a higher K M  indicates a lower affinity). Similarly, a particularly preferred aldolase is characterized and/or further characterized in that the affinity of the enzyme towards D-fructose 6-phosphate as a substrate is considerably worse/lower than those for D-arabinose 5-phosphate as substrate. Preferred is a ratio of at least 5 times, preferably at least 10 times, even more preferably at least 15 times and most preferably at least 20 times between the respective affinities (as indicated by K M ). In other words, it is particularly preferred to employ an aldolase that catalyzes the conversion of glycolaldehyde and D-glyceraldehyde 3-phosphate into D-arabinose 5-phosphate (and/or the reverse reaction) more efficiently (as, e.g. characterized by a ratio of at least 5 times, preferably at least 10 times, even more preferably at least 15 times and most preferably at least 20 times between the k cat /K M  values of the respective reaction(s) than the conversion of dihydroxyaceton and D-glyceraldehyde 3-phosphate into D-fructose 6-phosphate (and/or the reverse reaction). 
     Most preferably, an enzyme that is encoded by the  E. coli  gene fsaA (UniProt accession code: P78055; entry version 138 (20 Jan. 2016)) or by the  E. coli  gene fsaB (UniProt accession code: P32669; Entry version 125 (20 Jan. 2016)) is employed. As previously shown, these enzymes are able to catalyze the aldol condensation of glycolaldehyde (as a donor) with D-glyceraldehyde 3-phosphate (as an acceptor) to yield D-arabinose 5-phosphate (Garrabou X et al., 2009 , Angew Chem Int Ed Engl  48(30), 5521-5525; Samland A K et al., 2011 , Chembiochem  12(10), 1454-1474; Sánchez-Moreno I et al., 2012 , J Mol Catal B: Enzym  2012 84; 9-14; Guérard-Hélaine C et al., 2015 , ChemCatChem  7(12), 1871-1879). The affinities of the enzymes encoded by fsaA and fsaB genes towards the substrates glycolaldehyde (as a donor) with D-glyceraldehyde 3-phosphate (as an acceptor) are characterized by a K M  below 1 mM and the condensation is expected to have 16.5&lt;k cat &lt;173 sec −1  (Garrabou X et al., 2009, loc. cit.; Sánchez-Moreno I et al., 2012, loc. cit.). It has further been reported that the affinities of these enzymes towards D-fructose 6-phosphate (K M &gt;6 mM (Garrabou X et al., 2009, loc. cit.; Sánchez-Moreno I et al., 2012, loc. cit.)) as a substrate and dihydroxyacetone phosphate (K M &gt;25 mM (Garrabou X et al., 2009, loc. cit.; Sánchez-Moreno I et al., 2012, loc. cit.)) as a substrate are considerably lower (as indicated by an increased K M ) than those for D-arabinose 5-phosphate (K M ≈0.5 mM (Garrabou X et al., 2009, loc. cit.)) and glycolaldehyde (K M ≈0.2 mM (Garrabou X et al., 2009, loc. cit.; Sánchez-Moreno I et al., 2012, loc. cit.)). Accordingly, an overexpressed enzyme encoded by the fsaA or fsaB gene will predominantly catalyze the reversible glycolaldehyde assimilation rather than the reversible D-fructose 6-phosphate cleavage. While the enzyme encoded by the fsaA or fsaB gene may in principle catalyzes the condensation of two glycolaldehyde molecules, the affinity towards glycolaldehyde as an acceptor is too low (K M &gt;60 mM (Garrabou X et al., 2009, loc. cit.; Sánchez-Moreno I et al., 2012, loc. cit.)) to compete with D-arabinose 5-phosphate synthesis in vivo. Thus, also this alternative reaction does not significantly compete with the conversion of glycolaldehyde into D-arabinose 5-phosphate. 
     The further enzymatic conversion of D-arabinose 5-phosphate into D-ribulose 5-phosphate (reaction 80) as described in E) is a conversion which does naturally occur and for which enzymes that catalyze this conversion are known (Meredith T C et al., 2005 , Journal of Bacteriology  187(20), 6936-6942; Smyth K M et al., 2013  Carbohyd Res  380, 70-75). In particular, such enzymes are known from  E. coli  and have also been suggested in planta. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. The enzymatic conversion of D-arabinose 5-phosphate into D-ribulose 5-phosphate (reaction 80) can for example be achieved by a D-arabinose 5-phosphate isomerase (EC 5.3.1.13). Variants of this isomerase are, for example, known from  E. coli  (Meredith T C et al., 2005, loc. cit.) and a corresponding candidate enzyme was also suggested in planta (Smyth K M et al., 2013, loc. cit.). 
     As mentioned above, in another embodiment one of the preferred intermediates of the CBBC into which 2-PG is converted according to the present invention is D-xylulose 5-phosphate. In the following, possible pathways will be described which allow the conversion of 2-PG into D-xylulose 5-phosphate according to preferred embodiments of the present invention. The pathways which allow converting 2-PG into D-xylulose 5-phosphate will be referred to as option “F)” in the following. According to option F) the intermediate compound of the CBBC is D-xylulose 5-phosphate, and the conversion of 2-PG is preferably achieved by:
     a) enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-xylulose, and further enzymatic conversion of D-xylulose into D-xylulose 5-phosphate (a respective illustrative example is provided by  FIG. 1F ); or   b) enzymatic conversion of 2-PG into glycolaldehyde, further enzymatic conversion of glycolaldehyde into D-xylulose 5-phosphate (a respective illustrative example is provided by  FIG. 1G ); or   c) enzymatic conversion of 2-PG into 2-phosphoglycolyl phosphate, further enzymatic conversion of 2-phosphoglycolyl phosphate into glycolaldehyde 2-phosphate, and further enzymatic conversion of glycolaldehyde 2-phosphate into D-xylulose 5-phosphate (respective illustrative examples are provided by  FIG. 3E : pathway 1: 2-PG conversion into glycolaldehyde 2-phosphate as shown in  FIG. 2 +enzyme/reaction 68#; pathway 2: 2-PG conversion into glycolaldehyde 2-phosphate as shown in  FIG. 2 +enzyme/reaction 71#).   

     The enzymatic conversions as described in F)a), above, can, for example, be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in F)a), above, can, for example, be achieved by different pathways as will be described, below. 
     The further enzymatic conversion of glycolaldehyde into D-xylulose as described in F)a) can, for example, be achieved by a transaldolase (EC 2.2.1.2). In principle, any transaldolase can be employed. Preferably, one or more of the transaldolases mentioned in the context of the two alternative reactions (reactions 67# and 70#), further below, is/are employed. 
     The enzymatic conversion of glycolaldehyde into D-xylulose can, for example be achieved by the transaldolase reaction between D-fructose 6-phosphate and glycolaldehyde (reaction 67#). For this conversion, preferably a transaldolase which accepts D-fructose 6-phosphate and glycolaldehyde as substrates is employed. Preferably, a transaldolase enzyme (EC 2.2.1.2) from  E. coli, B. subtilis  or  C. glutamicum  is employed. In particular, a transaldolase (EC 2.2.1.2) selected from the group consisting of the following enzymes can be employed: TalB from  E. coli  (UniProt accession code: P0A870; entry version 109 (20 Jan. 2016)); Tal from  B. subtilis  (UniProt accession code: P19669) and Tal from  C. glutamicum  (UniProt accession code: Q8NQ64; entry version 109 (9 Dec. 2015)) (Samland A K et al., 2012 , FEBS J  279(5), 766-778). These enzymes are known to catalyze the transaldolase reaction between D-fructose 6-phosphate and glycolaldehyde, in which the former transfers a dihydroxyacetone moiety to the latter, resulting in the formation of D-glyceraldehyde 3-phosphate and D-xylulose (reaction 67#) (Samland A K et al., 2012, loc. cit.). The V max  of this reaction is in reasonable scale (1.6-8.8 μmol/min/mg) if catalyzed by these enzyme(s). The affinity of the enzyme(s) towards glycolaldehyde has been reported to be characterized in a K M &gt;60 mM. Preferably, an enzyme, which is based on said enzymes but has been engineered and/or evolved to an even higher activity and/or affinity towards glycolaldehyde (characterized in a lower K M ) is employed. Methods for modifying and/or improving the desired enzymes are well-known to the person skilled in the art and are described elsewhere herein. Most preferably, a respective improved enzyme, which has a high affinity to glycolaldehyde, wherein the high affinity is reflected by a low K M  value (K M &lt;1 mM), is employed. Such enzyme allows for particularly efficient glycolaldehyde assimilation. 
     Alternatively, the enzymatic conversion of glycolaldehyde into D-xylulose as described in F)a) can also be achieved by the transaldolase reaction between D-sedoheptulose 7-phosphate and glycolaldehyde (reaction 70#). In such a case, preferably a transaldolase which accepts D-sedoheptulose 7-phosphate and glycolaldehyde as substrates is employed. 
     Finally, the further enzymatic conversion of D-xylulose into D-xylulose 5-phosphate (reaction 69) as described in F)a), above, is a conversion which does naturally occur and for which enzymes which catalyze this conversion are known. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes can be employed in the context of the present invention. In particular, the enzymatic conversion of D-xylulose into D-xylulose 5-phosphate (reaction 69) can, for example, be achieved by a D-xylulokinase enzyme (EC 2.7.1.17) (Di Luccio E et al., 2007 , J Mol Biol  365(3), 783-798; Hemmerlin A et al., 2006 , Plant Physiol  142(2), 441-457). 
     The enzymatic conversions as described in F)b), above, can, for example, be achieved as described in the following: The enzymatic conversion of 2-PG into glycolaldehyde as described in F)b), above, can, for example, be achieved by different pathways as will be described further below. 
     The enzymatic conversion of 2-PG into glycolaldehyde as described in F)b), above, can, for example, be achieved by different pathways as will be described further below. 
     The further enzymatic conversion of glycolaldehyde into D-xylulose 5-phosphate as described in F)b) can, for example, be achieved by a transketolase enzyme (EC 2.2.1.1). In principle, any transketolase can be employed. Preferably, one or more of the transketolases mentioned in the context of the two alternative reactions (reactions 97# and 98#), further below, is/are employed. 
     The enzymatic conversion of glycolaldehyde into D-xylulose 5-phosphate can, for example, be achieved by the (reversible) condensation of glycolaldehyde (as a donor) and D-glyceraldehyde 3-phosphate (as an acceptor) (reaction 97#). This conversion can, for example, be achieved with the transketolase (EC 2.2.1.1) TKL1 from  S. cerevisiae  (UniProt accession code: P23254; entry version 168 (20 Jan. 2016)), which was found to catalyze the reversible condensation of glycolaldehyde (as a donor) and D-glyceraldehyde 3-phosphate (as an acceptor), yielding the CBBC&#39;s intermediate D-xylulose 5-phosphate (Fiedler E et al., 2001 , J Biol Chem  276(19), 16051-16058). Preferably, a transketolase, which is, for example, based on the above mentioned enzyme, and which has been engineered and/or evolved to an even higher affinity towards its substrates, in particular glycolaldehyde as a donor (characterized in a lower K M ), is employed. Methods for modifying and/or improving the desired enzyme are well-known to the person skilled in the art and are described elsewhere herein. Most preferably, a respective improved enzyme, which has a high affinity of glycolaldehyde as a donor (K M &lt;1 mM), is employed. Even more preferably, since glycolaldehyde can also serve as an acceptor, which results in the formation of erythrulose (Fiedler E et al., 2001, loc. cit.; Sprenger G A et al., 1995 , Eur J Biochem  230(2), 525-532; Sevostyanova I A et al., 2004 , Biochem Biophys Res Commun  313(3), 771-774), a transketolase employed for the above mentioned conversion is preferably engineered and/or evolved to a high affinity of glycolaldehyde as a donor (K M &lt;1 mM) but low affinity for glycolaldehyde as an acceptor (K M &gt;10 mM). 
     Alternatively, the enzymatic conversion of glycolaldehyde into D-xylulose 5-phosphate can also be achieved by the enzymatic conversion of glycolaldehyde into D-xylulose and the subsequent enzymatic conversion of D-xylulose into D-xylulose 5-phosphate. The enzymatic conversion of glycolaldehyde into D-xylulose can, for example, be achieved by the condensation of glycolaldehyde (as a donor) and D-glyceraldehyde (as an acceptor) (reaction 98#). For such conversion, preferably a transketolase which accepts glycolaldehyde (as a donor) and D-glyceraldehyde (as an acceptor) is employed. The subsequent enzymatic conversion of D-xylulose into D-xylulose 5-phosphate (reaction 69) can, for example, be achieved as described in F)a), above. 
     The enzymatic conversions as described in F)c), above, can, for example, be achieved as described in the following: 
     The enzymatic conversion of 2-PG into 2-phosphoglycolyl phosphate (reaction 23#) as described in F)c) can, for example, be achieved as described in connection with B)c), above. 
     The further enzymatic conversion of 2-phosphoglycolyl phosphate into glycolaldehyde 2-phosphate (reaction 24#) as described in F)c) can, for example, be achieved as described in connection with B)c), above. 
     The enzymatic conversion of glycolaldehyde 2-phosphate into D-xylulose 5-phosphate as described in F)c) can, for example, be achieved by a transaldolase (EC 2.2.1.2). In principle, any transaldolase can be employed. Preferably, one of the transaldolase mentioned in the context of the two alternative reactions (reactions 68# and 71#), below, is/are employed. 
     The enzymatic conversion of glycolaldehyde 2-phosphate into D-xylulose 5-phosphate can, for example, be achieved by the condensation of D-fructose 6-phosphate (as a donor) and glycolaldehyde 2-phosphate (as an acceptor) (reaction 68#). In such a case, preferably a transaldolase which accepts D-fructose 6-phosphate (as a donor) and glycolaldehyde 2-phosphate (as an acceptor), is employed. 
     Alternatively, the enzymatic conversion of glycolaldehyde 2-phosphate into D-xylulose 5-phosphate can, for example, be achieved by the condensation of D-sedoheptulose 7-phosphate (as a donor) and glycolaldehyde 2-phosphate (as an acceptor) (reaction 71#). In such a case, preferably a transaldolase which accepts D-sedoheptulose 7-phosphate (as a donor) and glycolaldehyde 2-phosphate (as an acceptor) is employed. 
     Some of the pathways for the conversion of 2-PG into an intermediate compound of the CBBC of the present invention as described above comprise the enzymatic conversion of 2-PG into glycolyl-CoA. In the following, the possible pathways will be described which allow the conversion of 2-PG into glycolyl-CoA according to preferred embodiments of the present invention. The enzymatic conversion of 2-PG into glycolyl-CoA can, for example, be achieved by:
     a) enzymatic conversion of 2-PG into glycolate and further enzymatic conversion of glycolate into glycolyl-CoA (a respective illustrative example is provided by  FIG. 2 ; enzyme 1 and 2#); or   b) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolyl phosphate, and further enzymatic conversion of glycolyl phosphate into glycolyl-CoA (a respective illustrative example is provided by  FIG. 2 ; enzymes 1, 19# and 21#); or   c) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolyl phosphate, further enzymatic conversion of glycolyl phosphate into glycolaldehyde, and further enzymatic conversion of glycolaldehyde into glycolyl-CoA (a respective illustrative example is provided by  FIG. 2 ; enzymes 1, 19#, 20# and 7#); or   d) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolaldehyde, and further enzymatic conversion of glycolaldehyde into glycolyl-CoA (a respective illustrative example is provided by  FIG. 2 ; enzymes 1, 22# and 7#).   

     The enzymatic conversion of 2-PG into glycolyl-CoA as described in a), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate (reaction 1) as described in a), above, is a conversion which does naturally occur and for which enzymes catalyzing this conversion are known, in particular also in plants. Examples for corresponding enzymes which are known to catalyze this conversion are mentioned in Table 2 and corresponding enzymes, preferably enzymes derived from plants, can be employed in the context of the present invention. 
     The further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#) as described above in a) can, for example, be achieved by a CoA-transferase (EC 2.8.3.X) (Volodina E. et al., 2014 , Appl Microbiol Biotechnol  98, 3579-3589; Dhamankar H. et al., 2014 , Metab Eng  25 C,  72-81) or an ADP-forming or AMP-forming CoA ligase (EC 6.2.1.X) (Awano T. et al., 2014 , J Bacteriol  196, 140-147; US 2011/0118434 A1) (these enzymes are an example for enzyme 2# mentioned herein). In principle, any ADP-forming or AMP-forming CoA ligase (EC 6.2.1.X) or CoA-transferase (EC 2.8.3.X) can be employed for such a conversion. In a preferred embodiment, the ADP-forming or AMP-forming CoA ligase (EC 6.2.1.X) is a propionate-CoA ligase (EC 6.2.1.17) (Awano T. et al., 2014 , J Bacteriol  196, 140-147; US 2011/0118434 A1). In another preferred embodiment the CoA-transferase (EC 2.8.3.X) is a propionyl-CoA transferase (EC 2.8.3.1). In one embodiment a propionyl-CoA tranferase of  Ralstonia eutropha  or a propionyl-CoA tranferase of  Clostridium propionicum  is employed. The amino acid sequence of (the wild-type) propionyl-CoA tranferase of  Ralstonia eutropha  (PCT Re ) is known and is available, e.g., under NCBI accession no. CAJ93797.1 (encoding nucleic acid sequence is shown in SEQ ID NO: 11; amino acid sequence is shown in SEQ ID NO: 12). The amino acid sequence of (the wild-type) propionyl-CoA tranferase of  Clostridium propionicum  (PCT Cp ) is known and is available, e.g., under NCBI accession no. CAB77207.1 (encoding nucleic acid sequence is shown in SEQ ID NO: 13; amino acid sequence is shown in SEQ ID NO: 14). Notably, the capability of both enzymes to catalyze the conversion of glycolate into glycolyl-CoA (reaction 2#) is also shown in the appended examples. 
     It is of course not only possible to employ in the enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#) an enzyme having the amino acid sequences of SEQ ID NOs: 12 or 14, respectively, but it is also possible to employ an enzyme showing a related sequence, provided that the enzyme still shows the activity of converting glycolate into glycolyl-CoA (reaction 2#). 
     The term “related sequences” preferably means sequences showing at least 60%, preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 99% and most preferably at least 99.5% sequence identity to the amino acid sequences shown in SEQ ID NO: 12 or 14, respectively. 
     As regards the determination of percent identity the same applies as has been described herein above. 
     Such above-mentioned related sequences may, for example also comprise mutated variants showing improved properties. In particular, also any mutant variants created by the evolution and optimization strategies described herein elsewhere and showing improved properties are included in the related sequences. In a preferred embodiment a mutated version of a propionyl-CoA tranferase of  Ralstonia eutropha  or a propionyl-CoA tranferase of  Clostridium propionicum  is employed, which shows an improved activity catalyzing the conversion of glycolate into glycolyl-CoA (reaction 2#) in comparison to the respective wild-type enzyme. 
     How to design assays for determining the enzymatic activity of converting glycolate into glycolyl-CoA (reaction 2#) is well known in the art. It is, for instance, possible to use an in vitro assay as described in the appended examples for determining whether an enzyme has the activity of converting glycolate into glycolyl-CoA (reaction 2#). In one embodiment the assay as described in the example may also be modified with respect to concentration of any components used and/or modification of buffer compositions based on the common general knowledge of skilled person. 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described in b), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate (reaction 1) as described above in b) can, for example, be achieved as described in connection with a) above. 
     The further enzymatic conversion of glycolate into glycolyl phosphate (reaction 19#) as described above in b) can, for example, be achieved by a carboxyl kinase (EC 2.7.2.X) (this enzyme is an example for enzyme 19# mentioned herein). In principle, any carboxyl kinase (EC 2.7.2.X) can be employed for such a conversion. In a preferred embodiment, the carboxyl kinase (EC 2.7.2.X) is an acetate kinase (EC 2.7.2.1) (Lyer, P. et al., 2005 , Microbial Enzymes and Biotransformations  (Barredo, J. L., Ed.), pp 239-246, ISBN: 9781588292537) or, in another embodiment, a butyrate kinase (Hartmanis M. G., 1987 , J Biol Chem  262, 617-621) (EC 2.7.2.7). Even more preferably the carboxyl kinase (EC 2.7.2.X) is an acetate kinase (EC 2.7.2.1). 
     The further enzymatic conversion of glycolyl phosphate into glycolyl-CoA (reaction 21#) as described above in b) can, for example, be achieved by a phosphate acyltransferase (EC 2.3.1.X) (this enzyme is an example for enzyme 21# mentioned herein), as some glucosamine 6-phosphate acetyltransferase variants can accept glycolyl-CoA instead of acetyl-CoA (Macauley M. S., 2012 , J Biol Chem  287, 28882-28897). In principle, any phosphate acyltransferase (EC 2.3.1.X) can be employed for such a conversion. In a preferred embodiment, the phosphate acyltransferase (EC 2.3.1.X) is a phosphate acetyltransferase (EC 2.3.1.8). 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described in c), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate (reaction 1) as described above in c) can, for example, be achieved as described in connection with a) above. 
     The further enzymatic conversion of glycolate into glycolyl phosphate (reaction 19#) as described above in c) can, for example, be achieved as described in connection with b) above. 
     The further enzymatic conversion of glycolyl phosphate into glycolaldehyde (reaction 20#) as described above in c) can, for example, be achieved by a phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (this enzyme is an example for enzyme 20# mentioned herein) (Fife T. H. et al., 1970 , Biochemistry  9, 4064-4067; Armstrong J. M. et al., 1976 , Biochem J  159, 513-527; Byers L. D., 1978 , Arch Biochem Biophys  186, 335-342). In principle, any phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) can be employed for such a conversion. 
     The further enzymatic conversion of glycolaldehyde into glycolyl-CoA (reaction 7#) as described above in c) can, for example, be achieved by an acylating aldehyde dehydrogenase (EC 1.2.1.X) (this enzyme is an example for enzyme 7# mentioned herein) (Burton R. M. et al., 1953 , J Biol Chem  202, 873-890; Sohling B. et al., 1993 , Eur J Biochem  212, 121-127). In principle, any acylating aldehyde dehydrogenase (EC 1.2.1.X) can be employed for such a conversion. In a preferred embodiment, the acylating aldehyde dehydrogenase (EC 1.2.1.X) is an acetaldehyde dehydrogenase (acylating) (EC 1.2.1.10). 
     The enzymatic conversions for the enzymatic conversion of 2-PG into glycolyl-CoA as described in d), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate (reaction 1) as described above in d) can, for example, be achieved as described in connection with a) above. 
     The further enzymatic conversion of glycolate into glycolaldehyde (reaction 22#) as described above in d) can, for example, be achieved by an ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) (this enzyme is an example for enzyme 22# mentioned herein). Several ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) variants were shown to catalyze the reduction of acetate and lactate at high rate (Venkitasubramanian P., 2006 , Biocatalysis in the Pharmaceutical and Biotechnology Industries  (Patel, R. N., Ed.), ISBN: 9781588292537; Napora-Wijata K., 2014 , Biotechnol J  9, 822-843) strongly indicating that glycolate can also be accepted as substrate. In principle, any ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) can be employed for such a conversion. 
     The further enzymatic conversion of glycolaldehyde into glycolyl-CoA (reaction 7#) as described above in d) can, for example, be achieved as described in connection with c) above. 
     Some of the pathways for the conversion of 2-PG into an intermediate compound of the CBBC of the present invention as described above comprise the enzymatic conversion of 2-PG into glycolaldehyde. In the following, the possible pathways will be described which allow the conversion of 2-PG into glycolaldehyde according to preferred embodiments of the present invention. The enzymatic conversion of 2-PG into glycolaldehyde can, for example, be achieved by:
     i) enzymatic conversion of 2-PG into glycolyl-CoA (by any of the pathways for enzymatic conversion of 2-PG into glycolyl-CoA as described above) and further enzymatic conversion of glycolyl-CoA into glycolaldehyde (respective illustrative examples are provided by  FIG. 2 ; enzymes 1, 2# and 7#; or  FIG. 2 ; enzymes 1, 19#, 21# and 7#, respectively); or   ii) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolyl phosphate and further enzymatic conversion of glycolyl phosphate into glycolaldehyde (a respective illustrative example is provided by  FIG. 2 ; enzymes 1, 19# and 20#, respectively); or   iii) enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolaldehyde (a respective illustrative example is provided by  FIG. 2 ; enzymes 1 and 22#, respectively); or   iv) enzymatic conversion of 2-PG into glycolyl-CoA (by any of the pathways for enzymatic conversion of 2-PG into glycolyl-CoA as described above), further enzymatic conversion of glycolyl-CoA into glycolyl phosphate and further enzymatic conversion of glycolyl phosphate into glycolaldehyde (a respective illustrative example is provided by  FIG. 2 ; enzymes 1, 2#, 21# and 20#, respectively); or   

     The enzymatic conversions for the enzymatic conversion of 2-PG into glycolaldehyde as described in i), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described above in i) can, for example, be achieved as described above. In the context of i) the enzymatic conversion of 2-PG into glycolyl-CoA is preferably achieved by the pathways a) and b) as described above. 
     The further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#) as described above in i) can, for example, be achieved by an acylating aldehyde dehydrogenase (EC 1.2.1.X) (this enzyme is an example for enzyme 7# mentioned herein) (Burton R. M. et al., 1953 , J Biol Chem  202, 873-890; Sohling B. et al., 1993 , Eur J Biochem  212, 121-127). In principle, any acylating aldehyde dehydrogenase (EC 1.2.1.X) can be employed for such a conversion. In a preferred embodiment, the acylating aldehyde dehydrogenase (EC 1.2.1.X) is an acetaldehyde dehydrogenase (acylating) (EC 1.2.1.10). 
     The enzymatic conversions for the enzymatic conversion of 2-PG into glycolaldehyde as described in ii), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate as described above in ii) can, for example, be achieved as described above. 
     The further enzymatic conversion of glycolate into glycolyl phosphate (reaction 19#) as described above in ii) can, for example, be achieved by a carboxyl kinase (EC 2.7.2.X) (this enzyme is an example for enzyme 19# mentioned herein) as described above. In principle, any carboxyl kinase (EC 2.7.2.X) can be employed for such a conversion. In a preferred embodiment, the carboxyl kinase (EC 2.7.2.X) is an acetate kinase (EC 2.7.2.1.) (Lyer P. et al., 2005, loc. cit.) or, in another embodiment, a butyrate kinase (Hartmanis M. G., 1987, loc. cit.) (EC 2.7.2.7). Even more preferably the carboxyl kinase (EC 2.7.2.X) is an acetate kinase (EC 2.7.2.1.). 
     The further enzymatic conversion of glycolyl phosphate into glycolaldehyde (reaction 20#) as described above in ii) can, for example, be achieved by a phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) (this enzyme is an example for enzyme 20# mentioned herein) (Fife T. H. et al., 1970, loc. cit.; Armstrong J. M. et al., 1976, loc. cit.; Byers L. D., 1978, loc. cit.). In principle, any phosphorylating glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) can be employed for such a conversion. 
     The enzymatic conversions for the enzymatic conversion of 2-PG into glycolaldehyde as described in iii), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolate as described above in iii) can, for example, be achieved as described above. 
     The further enzymatic conversion of glycolate into glycolaldehyde (reaction 22#) as described above in iii) can, for example, be achieved by an ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) (this enzyme is an example for enzyme 22# mentioned herein). Several ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) variants were shown to catalyze the reduction of acetate and lactate at high rate (Venkitasubramanian P., 2006 , Biocatalysis in the Pharmaceutical and Biotechnology Industries  (Patel, R. N., Ed.), ISBN: 9781588292537; Napora-Wijata K., 2014 , Biotechnol J  9, 822-843) strongly indicating that glycolate can also be accepted as substrate. In principle, any ATP- and NAD(P)H-dependent carboxylic acid reductase (EC 1.2.1.X) can be employed for such a conversion. 
     The enzymatic conversions for the enzymatic conversion of 2-PG into glycolaldehyde as described in iii), above, can be achieved as described in the following: 
     The enzymatic conversion of 2-PG into glycolyl-CoA as described above in iv) can, for example, be achieved as described above. In the context of iv) the enzymatic conversion of 2-PG into glycolyl-CoA is preferably achieved by enzymatic conversion of 2-PG into glycolate, further enzymatic conversion of glycolate into glycolyl-CoA. These enzymatic conversions are achieved as described above. 
     The enzymatic conversion of glycolyl-CoA into glycolyl phosphate (reaction 21#) as described above in iv) can, for example, be achieved by a phosphate acyltransferase (EC 2.3.1.X) (this enzyme is an example for enzyme 21# mentioned herein). It has, for example, been shown that some glucosamine 6-phosphate acetyltransferase variants can accept glycolyl-CoA instead of acetyl-CoA (Macauley M. S., 2012, loc. cit.). In principle, any phosphate acyltransferase (EC 2.3.1.X) can be employed for such a conversion. In a preferred embodiment, the phosphate acyltransferase (EC 2.3.1.X) is a phosphate acetyltransferase (EC 2.3.1.8). 
     The further enzymatic conversion of glycolyl phosphate into glycolaldehyde as described above in iv) can, for example, be achieved as described above in b). 
     Preferred, but non-limiting examples of photorespiration bypass routes in accordance with the invention are those depicted in the appended  FIGS. 1 to 4 . The bypass routes shown in  FIG. 1  and mentioned above are particularly preferred. 
     Notably, there are multiple alternative implementation schemes of the pathways shown in  FIGS. 1A , B, C, and D as discussed above and/or further presented in, for example  FIG. 2  and  FIG. 3 . Furthermore, other types of bypass routes are shown in  FIG. 4 ; all these routes provide alternative approaches to support increased yield of photorespiration. All these pathways, and their possible combinations, are included in the current invention, but are non-limiting. Examples for enzymes that can, for example, achieve the enzymatic conversions of these pathways are given for each enzymatic conversion in Tables 2 and 3. The respective reactions/enzymes/enzymatic conversions are identified with the same Arabic numbers in the  FIGS. 1 to 4  and in the Tables 2 and 3. Of course, also respective organisms, tissues, cells, or organelles, in which one or more of said pathways for the conversion of 2-PG into an intermediate compound of the Calvin-Benson-Bassham Cycle (CBBC) are included in the present invention. 
     As indicated in the  FIGS. 1 to 4  and/or as described, above, some of the photorespiration bypass are listed in Tables 2 and 3). The invention, of course, also relates to corresponding organisms, tissues, cells, or organelles which express the corresponding enzyme(s). 
     Furthermore, some of the photorespiration bypass pathways (as shown in  FIGS. 1 to 4  and/or described above) of the present invention require tetrose rearrangement. Tetrose rearrangement can, for example, be achieved by one of the pathways and/or enzymes/enzymatic conversions/reactions shown in  FIG. 3L . Thus, the current invention also relates to one or more of the pathways and/or enzymes/enzymatic conversions/reactions for tetrose rearrangement, as shown in  FIG. 3L  (respective enzymes/enzymatic conversions/reactions are listed in Tables 2 and 3). The invention, of course, also relates to corresponding organisms, tissues, cells, or organelles which express the corresponding enzyme(s). 
     As it is evident from  FIGS. 1 to 4  and the description herein, the present invention provides pathways that achieve the conversion of 2-PG into an intermediate of the CBBC without releasing CO 2  by:
     a) the enzymatic conversion of 2-PG into glycolyl-CoA (e.g. by one of the pathways shown in  FIG. 2  and/or described above) and the further enzymatic conversion of glycolyl-CoA into an intermediate of the CBBC (e.g. by one or more of the pathways shown in  FIG. 1A, 3A ;  31 ,  3 J,  3 K or  4 ); or   b) the enzymatic conversion of 2-PG into glycolaldehyde (preferably by one of the pathways shown in  FIG. 2  and/or described above) and the further enzymatic conversion of glycolaldehyde into an intermediate of the CBBC (e.g. by one or more of the pathways shown in  FIG. 1B, 1C, 1E, 1F, 1G, 3A, 3B, 3C, 3E, 3F, 3G, 3H, 3J or 3K ); or   c) the enzymatic conversion of 2-PG into glycolaldehyde 2-phosphate (preferably by one of the pathways shown in  FIG. 2  and/or described above) and the further enzymatic conversion of glycolaldehyde 2-phosphate into an intermediate of the CBBC (e.g. by one or more of the pathways shown in  FIG. 3B, 3C, 3E, 3G, 3H, 3J or 3K ); or   d) the enzymatic conversion of 2-PG into an intermediate of the CBBC, wherein said conversion involves methylene-THF that results from enzymatic conversion of CO 2 /HCO 3   −  (e.g. by one or more of the pathways shown in  FIGS. 1D, 3D ).   

     The enzymes/reactions/enzymatic conversions are listed in Tables 2 and 3. Similarly, the present invention also provides respective organisms, tissues, cells, or organelles expressing enzymes which allow for the conversion of 2-PG into an intermediate compound of the CBBC by one or more of the pathways as listed, above, in a) to d). In particular said organisms, tissues, cells, or organelles can be genetically engineered so as to express the respective enzymes (as long as they are not already naturally expressed and/or expressed in a sufficient amount). 
     The present invention further provides pathways that allow for enzymatic conversion of 2-PG into glycolyl-CoA, 2-PG into glycolaldehyde and/or 2-PG into glycolaldehyde 2-phosphate (e.g. as shown in  FIG. 2  and/or described above). Similarly, the present invention also relates to a respective organisms, tissues, cells, or organelles expressing enzymes which allow for the conversion of 2-PG into glycolyl-CoA, 2-PG into glycolaldehyde and/or 2-PG into glycolaldehyde 2-phosphate. The respective pathways offer the possibility of converting 2-PG into glycolyl-CoA, 2-PG into glycolaldehyde and/or 2-PG into glycolaldehyde 2-phosphate. In particular, by the pathways of the present invention, the respective conversion can be achieved in a highly efficient manner (i.e. with low NAD(P)H consumption (less than 4 molecules, less than 3 molecules, preferably less than 2 molecules, most preferably less than 1 molecule) and/or ATP consumption (less than 4 molecules, less than 3 molecules, preferably less than 2 molecules, most preferably less than 1 molecule) and/or without releasing CO 2 ). In addition, the pathways allow for establishing photorespiration bypass pathways according to the current invention. 
     Furthermore the present invention also provides pathways that allow for enzymatic conversion of glycolyl-CoA into an intermediate of the CBBC, glycolaldehyde into an intermediate of the CBBC and/or glycolaldehyde 2-phosphate into an intermediate of the CBBC. Similarly, the present invention also relates to a respective organisms, tissues, cells, or organelles expressing enzymes which allow for the conversion of 2 glycolyl-CoA into an intermediate of the CBBC, glycolaldehyde into an intermediate of the CBBC and/or glycolaldehyde 2-phosphate into an intermediate of the CBBC. The respective pathways offer the possibility of converting glycolyl-CoA into an intermediate of the CBBC, glycolaldehyde into an intermediate of the CBBC and/or glycolaldehyde 2-phosphate into an intermediate of the CBBC. In particular, by the pathways of the current invention conversion can be achieved in a highly efficient manner (i.e. with low NAD(P)H consumption (less than 4 molecules, less than 3 molecules, preferably less than 2 molecules, most preferably less than 1 molecule) and/or ATP consumption (less than 4 molecules, less than 3 molecules, preferably less than 2 molecules, most preferably less than 1 molecule) and/or without releasing CO 2 ). In addition, the pathways allow for establishing photorespiration bypass pathways according to the current invention. 
     Similarly, as shown in  FIG. 1D , the present invention also relates to a pathway for enzymatically converting CO 2  (thereby fixing the same) to methylene-THF. The present invention further provides respective organisms, tissues, cells, or organelles expressing enzymes which allow for the conversion of CO 2  to methylene-THF The respective enzymatic conversions and enzymes are explained in the context of option A)b). This pathway has the advantage of fixing CO 2 . 
     In any of the above mentioned embodiments which employ one or more concrete enzymes for which the corresponding amino acid sequence(s) is/are identified herein or incorporated by reference to a prior art document or a database entry, it is also envisaged that any enzyme variant(s) (having the same activity as the concrete enzyme(s); as determined e.g. by in vitro conversion assays such as the assays as depicted in Example 6 (or analogous thereto)) having at least 60%, preferably at least 65%, preferably at least 70%, preferably at least 75%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95% and most preferably 99% identity in the amino acid sequence (compared to the respective wilde-type enzyme(s)) are employed. 
     Those having skill in the art will know how to determine percent identity between/among sequences using, for example, algorithms such as those based on CLUSTALW computer program (Thompson (1994) Nucl. Acids Res. 2:4673-4680), CLUSTAL Omega (Sievers (2014) Curr. Protoc. Bioinformatics 48:3.13.1-3.13.16) or FASTDB (Brutlag (1990) Comp App Biosci 6: 237-245). Also available to those having skill in this art are the BLAST, which stands for Basic Local Alignment Search Tool, and BLAST 2.0 algorithms (Altschul, (1997) Nucl. Acids Res. 25:3389-3402; Altschul (1990) J. Mol. Biol. 215:403-410). The BLASTN program for nucleic acid sequences uses as defaults a word length (W) of 11, an expectation (E) of 10, M=5, N=4, and a comparison of both strands. The BLOSUM62 scoring matrix (Henikoff (1992) Proc. Natl. Acad. Sci. U.S.A. 89:10915-10919) uses alignments (B) of 50, expectation (E) of 10, M=5, N=4, and a comparison of both strands. 
     The photorespiration bypasses of the current invention have the particular advantageous property of recycling 2-PG to an intermediate compound of the CBBC in a CO 2 -neutral (without releasing CO 2 ) or even a CO 2 -positive (supporting net carbon fixation) manner. This is achieved by avoiding a decarboxylation reaction and/or including a (at least one) carboxylation reaction. In particular, inorganic carbon (CO 2 ) will not be lost as described for natural or other synthetic photorespiration reactions. In particular, inorganic carbon (CO 2 ) will not be lost in the mitochondria as described for natural photorespiration. Accordingly, such pathways can increase the carbon fixation rate of the CBBC and thereby the photosynthetic rate and yield. In particular, this applies to organisms, which naturally exhibit the CBBC such as plants, algae, cyanobacteria or other bacteria (e.g.  Pseudomonas oxalaticus, Paracoccus denitrificans, Ralstonia eutropha, Rhizobium japonicum, Thiobacillus ferrooxidans ). By contrast, natural photorespiration, as well as photorespiration bypass routes known in the art have the major disadvantage of releasing CO 2  during enzymatic recycling of 2-PG, which decreases the effective carbon fixation rate of the CBBC and thereby limits photosynthetic rate and yield. 
     Another particular advantage of the 2-PG converting pathways of this invention is to combine the advantageous feature of avoiding CO 2  release with direct recycling of 2-PG in a CBBC intermediate. Moreover, the bypass routes of the current invention further combine the advantageous feature of avoiding CO 2  release with any other of the further advantageous features listed herein. 
     A further advantage of the photorespiration bypass routes of the current invention is that they are short, i.e. require only ten or less enzymatic conversions. Notably, high numbers of enzymes would increase the risk of interfering with the non-photorespiratory metabolism. Furthermore, implementing such longer pathways in organisms that do not naturally express the corresponding enzymes requires more steps of genetic engineering. 
     Notably, the photorespiration bypass pathways of the current invention have the advantage of minimally overlapping and interfering with non-photorespiratory central metabolism or the 3-hydroxypropionate bicycle. 
     As a further advantageous property, the photorespiration bypass pathways of the current invention allow recycling of 2-PG into an intermediate compound of the CBBC without releasing NH 3 . In contrast, natural photorespiration leads to the loss of NH 3 , which needs to be reassimilated at an energetic cost. 
     The current invention further reduces the energetic costs for recycling 2-PG into the CBBC compared to natural photorespiration and alternative photorespiration bypass pathways by decreasing the consumption of ATP and/or the consumption of reduction equivalents for recycling 2-PG into a CBBP intermediate. Thereby the current invention allows increasing not only the carbon fixation efficiency but also the energetic efficiency of the CBBC. 
     The exact fraction of Rubisco&#39;s oxygenation reaction is debated, however, multiple studies determined independently that, for C3 plants, this fraction is in the range of 20% to 30% (Zhu X. G., et al. (2010) Annu Rev Plant Biol 61, 235-261; Peterhansel C., et al. (2013) Plant Biol (Stuttg) 15, 754-758; Ogren W. L. (1984) Annu Rev Plant Physiol 35, 415-442; Sharkey T. D. (1988) Physiol. Plant. 73, 147-152; Cegelski L., et al. (2006) J Magn Reson 178, 1-10; Zhu X. G., et al. (2007) Plant Physiol 145, 513-526; Andersson I. (2008) J Exp Bot 59, 1555-1568; Sage R. F., et al. (2012) Annu Rev Plant Biol 63, 19-47; Busch F. A. (2013) Plant Biol (Stuttg) 15, 648-655; Szecowka M., et al. (2013) Plant Cell 25, 694-714; Ma F., et al. (2014) Proc Natl Acad Sci USA 111, 16967-16972; Misra J. B. (2014) J Plant Physiol 171, 319-328). For example, in C3 plants, assuming an average fraction of Rubisco&#39;s oxygenation reaction of 25%, the photorespiration bypass routes of this invention can support up to 10%, 15%, 20%, 25%, 30%, 40%, 50% or 60% increased CBBP efficiency, as regarding, in this context particularly, the iterations/cycles of the CBBC that are required to produce 1 triose phosphate via the CBBC. Moreover, they can increase the efficiency of ATP and consumption up to 10%, 15%, 20%, 25%, 30%, 35%, 39%, 45% or 49% and/or the efficiency of NAD(P)H consumption up to 5%, 10%, 15%, 20%, 25% or 28%. In other words, to produce one triose phosphate via the CBBC, the photorespiration bypass routes of this invention reduce the required iterations/cycles of the CBBC (e.g. to 3 or less or 4 or less, as compared to 4.8 for natural photorespiration), the ATP consumption (e.g. to 10.5 or less, 11 or less or 12 or less molecules as compared to 15.6 molecules for natural photorespiration) and/or the NAD(P)H consumption (e.g. to 7.5 or less or 8 or less molecules as compared to 9.6 molecules for natural photorespiration) as compared to C3 plants exhibiting natural photorespiration. Calculated per iteration/cycle of the CBBC, the bypass routes of the present invention support an up to 40%, 45%, 50%, 55% or 60% higher biomass yield and/or an up to 16%, 20%, 25%, 30%, 38%, or 49% higher yield per ATP. For comparison, the photorespiration bypass routes presented in the prior art support much lower decreases in ATP and/or NADPH consumption (≤8% and ≤14%, respectively) with no improvement in the productivity of the CBBC. 
     These calculations show that the CO 2 -neutral and CO 2 -positive photorespiration pathways of this invention have a significant advantage over their natural counterparts and previously suggested bypass routes. This applies to strong illumination, where growth is mainly limited by the activity of the CBBC, as well as to low light conditions, where growth is limited by the supply of ATP and NADPH (Xin C. et al., 2014 , Plant Physiol  dx.doi.org/10.1104/pp. 114.248013). The implementation of this bypass routes in CBBC-exhibiting/Rubico-using organisms/tissues/cells/organelles (e.g. C3 plants/tissues/cells/organelles) is thus expected to significantly increase photosynthetic efficiency, growth rate and/or biomass yield under various environmental conditions. This provides for example the basis for increasing photosynthetic efficiency and agricultural productivity of many cultivated crops such as rice, wheat, barley, oat, soybean, cotton and potato. Consequently, significantly higher agricultural yields are supported. Furthermore, the current invention can for example also establish increased growth rates of other organisms exhibiting the CBBC (e.g. algae, cyanobacteria and other bacteria). 
     In particular, because of the enhanced photosynthetic potential, an organism/tissue/cell/organelle having the photorespiration bypass pathways of the present invention achieves one or more of the following properties: elevated yield of harvestable parts (e.g. fruits, seeds, shoots, leaves, roots, etc. per dry weight of the whole organism, improved drought and heat resistance, enhanced nitrogen-use efficiency, and reduced requirements for fertilization. 
     The present invention further relates to an organism, tissue, cell or organelle expressing an improved photorespiration bypass route in accordance with the invention, for example an improved photorespiration bypass route as depicted in the enclosed Figures, preferably an improved photorespiration bypass route as depicted in  FIG. 1A , B, C or D. As mentioned, it is particularly envisaged that the bypass route according to the invention converts 2-PG into an intermediate compound of the CBBC without releasing CO 2 . The term “expressing an improved photorespiration bypass route in accordance with the invention” means that the organism, tissue, cell or organelle contains the respective enzymes which form part of such a pathway. 
     Thus, the present invention further relates to an organism, tissue, cell or organelle expressing (a cascade of/series of) enzymes which allow/which are required for an improved photorespiration bypass route in accordance with the invention. 
     In a specific aspect, in the organism/tissue/cell/organelle of the invention, the normal/natural photorespiration is inactivated, for example by inactivating/knock out/suppressing one or more of the respective enzymes like, for example, glycolate oxidase and/or enzymes of the glycine cleavage system. Respective means and methods for inactivating/knock out/suppressing certain enzymes in plants are known in the art. 
     However, the improved photorespiration bypass routes of the invention also operate alongside the natural one and still have a positive effect—without even interfering with the natural pathway. Respective embodiments are also covered by the invention. 
     In particular, the (cascade of/series of) enzymes to be employed in accordance with the invention (is) are meant to be (a cascade of/series of) enzymes which catalyze(s) the steps and conversions, respectively, which are required to convert 2-PG into an intermediate compound of the CBBC without releasing CO 2  as described herein. Respective enzymes are, for example, those enzymes which are marked by Arabic numerals in the appended Figures like, for example, in  FIG. 1A , B, C or D or in Tables 2 and 3. 
     In principle, the organism, tissue, cell or organelle of the present invention may be any organism, tissue, cell or organelle which exhibits and/or is capable of exhibiting an alternative photorespiration pathway as disclosed herein, i.e. which expresses the respective enzymes (the enzymes which allow/are required for the conversion 2-PG into an intermediate compound of the CBBC without releasing CO 2 ). 
     In particular, the organism, tissue, cell or organelle of the present invention is an organism, tissue, cell or organelle which exhibits the CBBC, in particular under aerobic conditions, i.e which comprises Rubisco that is active in the presence of O 2 , i.e. which, at least to some extent, also accept O 2  instead of CO 2 . The organism, tissue, cell or organelle of the present invention is also an organism, tissue, cell or organelle (the wild-type of) which exhibits (suffers from) photorespiration and, in particular, (the wild-type of) which suffers from (a) product(s)/intermediate(s) of photorespiration like, for example, 2-PG, and/or (the wild-type of) which requires to convert from (a) product(s)/intermediate(s) of photorespiration like, for example, 2-PG into an intermediate, like an intermediate of the CBBC. In a preferred embodiment, the organism/tissue/cell/organelle according to the present invention is a photosynthetically active organism/tissue/cell/organelle, i.e. an organism/tissue/cell/organelle which is capable of photosynthesis. 
     As mentioned above, the (wild-type) organism/tissue/cell/organelle in accordance with the invention may have an inactivated normal/natural photorespiration. 
     In another aspect, the invention relates to a cell of an organism comprising the organelle (e.g. the plastid) of the invention. 
     It is especially envisaged that the organism, tissue or cell of the present invention comprises (an) organelle(s) (e.g. (a) plastid such as (a) chloroplast(s)) of the invention or are itself of a organelle-like, plastid-like or chloroplast-like nature (like, for example, a cyanobacterium). 
     In principle, any step (sub-conversion) of, any subset of steps of, or all steps of the (entire) conversion of 2-PG into an intermediate of the CBBC, i.e. of the alternative photorespiratory pathways in accordance with the invention, may take place in any compartment of a cell/cell organelle. However, a particular compartmentation of one or more single step, one or more subset of steps, or all steps may be advantageous as can readily be comprehended by the skilled person. It is, for example, preferred that one or more single step, one or more subsets of steps, or all steps take place in the plastids (e.g. chloroplasts), in particular in the stroma (matrix) thereof. It is particularly preferred that all steps take place in the plastids (e.g. chloroplasts), in particular in the stroma (matrix) thereof. The person skilled in the art is readily able to choose for any step, any subset of steps, or all steps the respective most advantageous compartmentation. For example, the compartmentation may be chosen in a photorespiration-like a manner, i.e. the different steps and/or sub sets of steps may be split into the chloroplast, the peroxisome and the mitochondrion, as the case may be. The compartmentation may also be chosen according to the column “Natural plant localization” as referred to in Table 2. In particular, the compartmentation may be chosen so that the respective intermediates can easily be transported from and/or to (an)other relevant compartment(s). 
     For example, at least a first step, for example of converting 2-PG into glycolate, and a last step which eventually results in the intermediate compound of the CBBC (for example the step of converting D-gycerate into D-glycerate 3-phosphate or D-erythrose into D-erythrose 4-phosphate) may take place in the plastid (e.g. chloroplast). It is, however, preferred that all steps of the conversion, i.e. the entire conversion, of 2-PG, i.e. of the alternative photorespiratory pathway, in accordance with the invention take(s) place in the plastid (e.g. chloroplast), in particular in the plastid&#39;s stroma (matrix). Consequently, it is preferred that the plastid (e.g. chloroplast), in particular in its stroma (matrix), comprises (by way of expression or targeting) the enzymes which are required for the entire conversion of 2-PG, i.e. of the alternative photorespiratory pathway, in accordance with the invention. 
     The invention also relates to such (a) plastid(s). In addition, the invention relates to (a) plastid(s) comprising, in particular in the stroma (matrix), (by way of expression or targeting) a subset of, but at least one of, the enzymes which are required for the entire conversion of 2-PG, i.e. of the alternative photorespiratory pathway, in accordance with the invention. 
     In principle, any plastid is envisaged in the context of the invention i.e, any plastid may comprise (express) (an) enzyme(s) in accordance with the invention. However, a “green” plastid, i.e. a plastid which exhibits/is capable of exhibiting photosynthesis and, in particular, the CBBC and, more particular, the CBBC and photorespiration (the latter applies to the respective wild-type) is preferred. Hence, the most preferred plastid is a chloroplast. However, also other plastids are envisaged and may comprise (express) the enzyme(s) in accordance with the invention. Examples of such other plastids are plastids contained in the phloem (P-plastids), pro-plastids, chromoplasts, leucoplasts (e.g. amyloplasts, proteinoplasts, elaioplasts) and gerontoplasts. 
     The present invention also relates to a cell organelle comprising all, a subset of, but at least one of the enzymes which are required for the entire conversion of 2-PG, i.e. of the alternative photorespiration bypass pathway, in accordance with the present invention. In principle, any cell organelle is envisaged in this context (e.g. plastid, mitochondrium, peroxisome, ER, Golgi apparatus, nucleus, vacuole, cell wall, etc.). However, preferred organelles are those which are involved in natural photorespiration like, for example, chloroplasts, peroxisomes and mitochondria. As mentioned, plastids are the most preferred cell organelle. 
     The organism of the present invention may be a plant (including higher plants, ferns, mosses and algae), a cyanobacterium (e.g.  Synechocystis, Synechococcus ) or a bacterium of other bacterial lineages that utilizes the CBBC, such as  Pseudomonas oxalaticus, Paracoccus denitrificans, Ralstonia eutropha, Rhizobium japonicum, Thiobacillus ferrooxidans . As mentioned above a cyanobacterium is particularly envisaged as a bacterium that utilizes the CBBC. The tissue or cell of the present invention may origin from these organisms. A “green” organism, i.e. an organism which exhibits/is capable of exhibiting photosynthesis and, in particular, the CBBC and, more particular, the CBBC and photorespiration (the latter applies at least to the respective wild-type), is preferred. Respective organisms are known in the art and are, for example, plants (including higher plants, ferns, mosses and algae) and cyanobacteria. 
     A preferred “green” organism in accordance with the invention is a plant (including higher plants, ferns, mosses and algae), in particular a higher plant or a vascular plant. A preferred plant in accordance with the invention is a C3 plant, i.e. a plant which fixes CO 2  (directly) via Rubisco and which does not exhibit another upstream CO 2  fixation and/or concentrating mechanism (like the C4 mechanism). 
     The plant of the invention (for example genetically engineered, transgenic and/or transplastomic) may, for example, be any monocot or dicot plant, such as, but not limited to, plants of commercial or agricultural interest, such as crop plants (especially crop plants used for human food or animal feed), wood- or pulp-producing trees, vegetable plants, fruit plants, and ornamental plants. Non-limiting examples of plants of interest include grain crop plants (such as wheat, oat, barley, maize, rye, triticale, rice, millet, sorghum, quinoa, amaranth, and buckwheat); forage crop plants (such as forage grasses and forage dicots including alfalfa, vetch, clover, and the like); oilseed crop plants (such as cotton, safflower, sunflower, soybean, canola, rapeseed, flax, peanuts, and oil palm); tree nuts (such as walnut, cashew, hazelnut, pecan, almond, and the like); sugarcane, coconut, date palm, olive, sugarbeet, tea, and coffee; wood- or pulp-producing trees; vegetable crop plants such as legumes (for example, beans, peas, lentils, alfalfa, peanut), lettuce, asparagus, artichoke, celery, carrot, radish, the brassicas (for example, cabbages, kales, mustards, and other leafy brassicas, broccoli, cauliflower, Brussels sprouts, turnip, kohlrabi), edible cucurbits (for example, cucumbers, melons, summer squashes, winter squashes), edible alliums (for example, onions, garlic, leeks, shallots, chives), edible members of the Solanaceae (for example, tomatoes, eggplants, potatoes, peppers, groundcherries), and edible members of the Chenopodiaceae (for example, beet, chard, spinach, quinoa, amaranth); fruit crop plants such as apple, pear, citrus fruits (for example, orange, lime, lemon, grapefruit, and others), stone fruits (for example, apricot, peach, plum, nectarine), banana, pineapple, grape, kiwifruit, papaya, avocado, and berries; and ornamental plants including ornamental flowering plants, ornamental trees and shrubs, ornamental groundcovers, and ornamental grasses. Preferred dicot plants include, but are not limited to, canola, cotton, potato, quinoa, amaranth, buckwheat, safflower, soybean, sugarbeet, and sunflower, more preferably soybean, canola, and cotton. Preferred monocots include, but are not limited to, wheat, oat, barley, maize, rye, triticale, rice, ornamental and forage grasses, sorghum, millet, and sugarcane. However, as mentioned, C4 plants are less preferred (but not excluded). 
     Preferred but non-limiting examples of a plant of the invention are the highly cultivated C3 plants like, for example, rice, wheat, barley, oat, soybean, cotton and potato. 
     In principle, it is envisaged that the tissue or cell of the present invention originate from the organism of the invention, i.e from the organisms described herein. 
     The (transgenic) cell of the invention may be an isolated cell (e. g., individual (plant) cell or cell grown in or on an artificial culture medium), or can be a (plant) cell in undifferentiated tissue (e. g., callus or any aggregation of (plant) cells). The transgenic (plant) cell can be a (plant) cell in at least one differentiated tissue, e.g. selected from the group consisting of leaf (e. g., petiole and blade), root, stem (e. g., tuber, rhizome, stolon, bulb, and corm) stalk (e. g., xylem, phloem), wood, seed, fruit (e. g., nut, grain, fleshy fruits), and flower (e. g., stamen, filament, anther, pollen, carpel, pistil, ovary, ovules). The (transgenic) organism (e.g. plant) of the invention includes organisms (e.g. plants) of any developmental stage, and includes a regenerated organism (e.g. plant) prepared from the (transgenic) cells claimed herein, or a progeny organism (which can be an inbred or hybrid progeny organism) of the regenerated organism, or progeny (e.g. seed) of such a transgenic organism (e.g. plant). 
     Also provided and claimed is a (genetically engineered, transgenic and/or transplastomic) progeny (e.g. seed) of the organism (e.g. plant) of the invention. 
     The present invention further relates to an organism, tissue, cell or organelle, in particular an organism, tissue, cell or organelle as described herein, which expresses, preferably in its organelle(s) (e.g. plastid(s)), at least one of the enzymes as defined herein, preferably the cascade of/series of enzymes as defined herein (the photorespiratory bypass route). 
     Means and methods to confirm that the alternative photorespiration pathway and the involved (cascade of/series of) enzymes, respectively, is/are functional inside the organism, tissue, cell or organelle (e.g. in the plant chloroplast) are known in the art and, for example, include:
         Studying whether respective encoding genes are expressed and the respectively encoded proteins/enzymes occur/accumulate inside the organism, tissue, cell or organelle (e.g. the chloroplast).   Studying whether the respective metabolic intermediates of the pathway occur/accumulate in the organism, tissue, cell or organelle.   Studying any changes in the photosynthetic properties of the organism, tissue, cell or organelle by measurement of a photosynthetic property. This may include the determination of the CO 2  compensation point by gas exchange measurements and/or the ATP and/or NAD(P)H consumption rates.   Studying growth, biomass production and yield of the organism/tissue/cell/organelle under different growth conditions, such as under non-favourable conditions for C3-plants.       

     Examples of such methods are described herein elsewhere and in WO 2011/099006, WO 2003/100066, EP 2 093 283 and Shih (loc. cit.). 
     Subject-matter of the present invention also are organelles, cells, tissues or organisms (e.g. plant plastids, plant cells, plant tissues or plants) which comprise one or more nucleic acid(s) which encode (an) polypeptide(s) having the (cascade of/series of) enzymes/enzymatic activities in accordance with the invention, i.e. the enzymes/enzymatic activities as described herein. 
     The organism, tissue, cell or organelle of the invention may be a genetically engineered, transgenic, and/or transplastomic organism, tissue, cell or organelle (e.g. plastid), as the case may be. 
     In one aspect, the organism, tissue, cell or organelle may be genetically engineered transgenic and/or transplastomic so as to express an enzyme, or several or all of the (cascade of/series of) enzymes, by which an enzymatic conversion as defined herein is achieved, i.e. which allow for the photorespiration bypass route in accordance with the invention. 
     In a specific aspect, the organism, tissue, cell or organelle of the invention comprises, for example in its genome, one or more recombinant DNA constructs including DNA that can be transcribed into one or more mRNAs encoding the (cascade of/series of) enzyme(s) in accordance with the invention. 
     The present invention further relates to a method for producing an organism, a tissue, a cell or a organelle of the invention and as described herein. The method may comprise a step of genetically engineering an organism, a tissue, a cell or an organelle (e.g. a plant organelle (e.g. a plastid), plant cell, plant tissue or plant as defined herein). 
     The method of producing of the invention may, in particular, comprise the step of
     (i) genetically engineering an organism, tissue, cell or organelle so as to comprise (express) (an) enzyme(s) as described and defined herein, preferably the entire cascade of/series of enzymes (the entire alternative photorespiratory bypass route).   

     The method of producing of the invention may further comprise the step of
     (ii) (re)generating, for example, from said tissue, cell or organelle, the (transgenic and/or transplastomic) organism.   

     The invention further relates to the organism, tissue, cell or organelle as obtained or as obtainable by the method of producing of the invention. The invention further relates to the genetically engineered, transgenic and/or transplastomic organism, tissue, cell or organelle as obtained by or as obtainable by the method of producing of the invention. 
     In the context of the invention, genetically engineering an organism, tissue, cell and/or organelle so as to comprise/express (an) enzyme(s) as described and defined herein may be achieved by introducing into an organism, tissue, cell and/or organelle (for example as comprised or to be comprised in the organism, tissue, or cell) one or more nucleotide sequence(s) (e.g. (a) recombinant DNA construct(s)) encoding one or more of the enzymes to be employed in accordance with the invention. mRNA encoding the enzyme(s) may then be transcribed/expressed from said nucleotide sequence(s), preferably within said organelle, for example, where applicable, from the (organelle&#39;s) genome into which said nucleotide sequence(s) (e.g. (a) recombinant DNA construct(s)) has/have been integrated. 
     Further, the organism (e.g. plant) tissue or cell of the invention, and/or the organelle(s) (e.g. chloroplast(s)) comprised therein, may be genetically engineered so that (a) nucleotide sequence(s) (e.g. a recombinant DNA construct) encoding the enzyme(s) to be employed in accordance with the invention is comprised. mRNA encoding the enzyme(s) may then be transcribed/expressed from said nucleotide sequence. 
     When providing or producing the (genetically engineered, transgenic and/or transplastomic) organism, tissue, cell or organelle of the invention, the skilled person can readily rely on its common general knowledge and the teaching of the invention. In particular, respective means and methods for genetically engineering and transfecting/transforming, respectively are known in the art and are, for example, disclosed in WO 2011/099006, WO 03/100066, EP 2 093 283 and Shih et al., 2014 (loc. cit.). 
     Both, a transiently transformed/transfected and stably transformed/transfected organism, tissue, cell or organelle is encompassed by this invention. A stably transformed/transfected transgenic organism, tissue, cell or organelle is particularly preferred. In a preferred embodiment, the transgenic organism is a fertile transgenic plant from which seed can be harvested, and the invention further claims transgenic seeds of such a transgenic plant, wherein the seeds preferably also contain the enzymes and/or the respective recombinant construct(s) of this invention. 
     The transgenic tissue, cell or organelle or transgenic organism of the invention, e.g. comprising the (genetically engineered) organelle of the invention, can be obtained by use of any appropriate transient or stable, integrative or non-integrative transformation method known in the art or presently disclosed. The respective nucleotide sequences (e.g. recombinant DNA constructs) can in principle be transcribed in any cell, tissue or organelle or in a whole organism of any developmental stage. However, the herein elsewhere described compartimentation may be advantageous also in this context, 
     The nucleotide sequence(s) encoding the enzyme(s) in accordance with the invention may be introduced into the organism&#39;s, tissue&#39;s, cell&#39;s or organelle&#39;s genome (where the organelle has a genome). The enzyme(s) may be expressed from this genome, for example from the mentioned introduced nucleotide sequence(s). 
     For example, the organelle may be genetically engineered so as to produce/express the enzyme(s) (see Bock R., 2014 , Curr. Opin. Biotechnol.  26, 7-13 for genetical engineering of plastids). The enzyme(s) may be transcribed from the organelle&#39;s genome (where the organelle has a genome), for example from an encoding nucleotide sequence introduced therein (e.g. recombinant DNA construct). The organelle may comprise a nucleotide sequence which encodes and expresses the enzyme(s). 
     It is envisaged in the context of the invention that the enzymes may either be expressed directly in the organelle (e.g in the plastid and in particular in the plastid&#39;s stroma (matrix)) or may be targeted into the organelle (e.g in the plastid and in particular into the plastid&#39;s stroma (matrix)), e.g. after transcription/translation in the nucleus/cytosol. 
     As mentioned, in a preferred embodiment, the organelle to be comprised in the organism/tissue/cell of the invention, and the organelle of the invention, respectively, in particular the organelle which comprises (expresses) the enzyme(s) to be employed in accordance with the invention is a chloroplast. However, for example by choosing appropriate expression signals, it is also possible to express plastid transgenes encoding the enzyme(s) in non-green tissues, i.e. in other types of plastids (cf. Zhang, Plant J. 72 (2012) 115-128; Caroca, Plant J. 73 (2013) 368-379). Such other types of plastids are described herein elsewhere. For example, the enzyme(s) may be expressed from the mentioned nucleotide sequence(s) and/or from the plastids genome, respectively. 
     The skilled person is readily able to target (an) enzyme(s) in accordance with the invention into the relevant cell organelle/compartment. Thereby, the skilled person can, for example, rely on Emanuelsson ( Nature Protocols  2, 953-971 2007), WO 2011/099006, WO 03/100066, EP 2 093 283 and Shih (loc. cit.). In particular, targeting domains for the desired cell organelles may be used and may, hence, be comprised in the nucleotide sequences/constructs described herein. The respective enzyme may then be translated as a respective precursor with an amino (N)-terminal extension (the targeting domain). Usually, in case the enzymes are to be targeted into the plastid, mitochondria or peroxisome, transit peptides (TP), pre-sequences or peroxisomal targeting signals (e.g. PTS1 and PTS2) are used as targeting domains, respectively. 
     In particular, if the enzymes are to be targeted into the plastid, N-terminal extensions acting as the “zip code” (also called “transit peptides”) may be used. The targeting domains for plastids may be such which are recognized by Tocs (proteins of the outer membrane complex which shuttles the pre-protein through the outer membrane) and/or Tics (proteins of the inner membrane complex which shuttles the pre-protein through the inner membrane). The (pre-)proteins/enzymes may further be assembled with chaperons. In a preferred aspect the enzymes may be stroma (matrix)-targeted enzymes. Respective nucleic acid constructs may comprise stroma (matrix)-targeting domains. 
     The skilled person is further readily able to provide an organism (a plant) which comprises/expresses the enzyme(s) to be employed in accordance with the invention in certain plastids (e.g. in chloroplasts), and, optionally, not to comprise/express the enzyme(s) in other plastids (e.g. amyloplasts), as the case may be. For example, such a selective expression/production of the enzyme(s) in the respective plastids can readily be achieved by the choice of, for example, (a) respective suitable element(s) like (a) promoter(s) and/or (a) signaling sequence(s) (targeting domain(s)), and the like. 
     Means and methods to genetically engineer an organism, tissue, cell (e.g. a plant) and/or a plastid are well known in the art and are, for example, described in Valkov,  Transgenic Res.  20, 137 (2011) and Svab,  Proc. Natl. Acad. Sci. USA  90, 913 (1993), WO 2011/099006, WO 2003/100066, EP 2 093 283, Shih et al. 2014 (loc. cit.) and Bock R.,  Curr. Opin. Biotechnol.  26, 7-13 (2014). An example of such a method is biolistic transformation (particle bombardment), for example with gold particles coated with the nucleotide sequence (s) (e.g. recombinant DNA construct) encoding the enzyme(s) in accordance with the invention. The respective means may, for example be a PDS1000/He particle delivery system, for example equipped with a Hepta adaptor (BioRad, Hercules, Calif., USA). 
     Where a nucleotide sequence (e.g. recombinant DNA construct) is used to produce a (genetically engineered transgenic, e.g. transplastomic, organism (e.g. plant, or transgenic, e.g. transplastomic, tissue, cell or plastid thereof, of this invention), genetic engineering, transfection and transformation, respectively, can include any of the well-known and demonstrated methods and compositions. Suitable methods for, for example, plant transformation include virtually any method by which DNA can be introduced into a (plant) cell, in particular into a plastid, such as by direct delivery of DNA (e. g., by PEG-mediated transformation of protoplasts, by electroporation, by agitation with silicon carbide fibers, and by acceleration of DNA coated particles), by  Agrobacterium -mediated transformation, by viral or other vectors, etc. One preferred method of plant transformation is microprojectile bombardment, for example, as illustrated in U.S. Pat. No. 5,015,580 (soy), U.S. Pat. No. 5,550,318 (maize), U.S. Pat. No. 5,538,880 (maize), U.S. Pat. No. 6,153,812 (wheat), U.S. Pat. No. 6,160,208 (maize), U.S. Pat. No. 6,288,312 (rice) and U.S. Pat. No. 6,399,861 (maize), and U.S. Pat. No. 6,403,865 (maize). 
     In particular, the mRNA encoding the enzyme(s) may be expressed by transcription from a nucleotide sequence (for example DNA) following a promoter. 
     In various embodiments, the nucleotide sequence encoding the enzyme(s) (e.g. the recombinant DNA construct) as employed in the context of the invention include, in addition to the transcribable nucleotide sequence (coding for the enzyme(s)), one or more of the following elements:
     (a) a(n) (organelle (e.g. plastid)) promoter or a promoter from a heterologous source organism that is active (e.g. in organelles (e.g. plastids), cells, organisms, tissues of the invention) (e.g. from a bacterium or phage);   (b) a signal/targeting sequence capable of targeting (expression of) the enzyme(s) into the relevant compartment/organelle (e.g. plastid); and   (c) at least one gene expression element.   

     These elements are, for example, described in more detail herein elsewhere and in WO 2007/011479, WO 2011/099006, WO 03/100066, EP 2 093 283 and Shih (loc. cit.). 
     For the purpose of expressing the nucleic acids which encode the polypeptides having the enzymatic activities as required for the present invention in, for example, (plant) cells or organelles (e.g. plastids) any convenient regulatory sequences can be used. The regulatory sequences will provide transcriptional and translational initiation as well as termination regions, where the transcriptional initiation may be constitutive or inducible. The coding region is operably linked to such regulatory sequences. Suitable regulatory sequences, in particular for plants, are represented by the constitutive 35S promoter. This may, in particular, be used for dicotyledonous plants. For monocotyledonous plants the constitutive ubiquitin promoter may be used, in particular the maize ubiquitin promoter (GenBank: gil9700915). Examples for inducible promoters represent the light inducible promoters of the small subunit of Rubisco, in particular the tomato rbcS promoter (GenBank: gi22624), and the promoters of the “light harvesting complex binding protein (Ihcb)”, in particular the tobacco Ihcb promoter (GenBank: gil 890636). 
     Generally, a nucleotide sequence (e.g. a recombinant DNA construct) which encodes (an) enzyme(s) to be expressed in accordance with the invention may include a promoter operably linked to the transcribable nucleotide sequence. In various embodiments, the promoter may be selected from the group consisting of a constitutive promoter, a spatially specific promoter, a temporally specific promoter, a developmentally specific promoter, and an inducible promoter. Non-constitutive promoters suitable for use with the nucleotide sequence to be employed (e.g. recombinant DNA construct) of the invention include spatially specific promoters, temporally specific promoters, and inducible promoters. Spatially specific promoters can include cell-, tissue-, or organ-specific promoters. Temporally specific promoters can include promoters that tend to promote expression during certain developmental stages in an organism&#39;s (e.g. plant&#39;s) growth cycle, or during different times of day or night, or at different seasons in a year. Inducible promoters include promoters induced by chemicals or by environmental conditions such as, but not limited to, biotic or abiotic stress (e. g., water deficit or drought, heat, cold, high or low nutrient or salt levels, high or low light levels, or pest or pathogen infection). An expression-specific promoter can also include promoters that are generally constitutively expressed but at differing degrees or “strengths” of expression, including promoters commonly regarded as “strong promoters” or as “weak promoters”. 
     A particular but non-limiting example of a promoter which may be used to express (an) enzyme(s) to be expressed in accordance with the invention in the plastid (e.g. in the chloroplast) is the Prrn promoter. Other suitable promoters are, for example, the plastid psbA, psbD, rbcL and rp132 promoters (see, for example, Staub (1993) EMBO J. 12, 601-606; Allison (1995) EMBO J. 14, 3721-3730; Eibl (1999) Plant J. 19, 333-345). In principle, heterologous promoters from other organisms (e.g. bacteria and phages) may also be used (see, for example, Newell (2003) Transgenic Res. 12, 631-634). 
     This invention also provides a transgenic organism, tissue or cell thereof, having in its genome, in particular in the genome of its organelles (e.g. plastid(s)), a recombinant DNA construct (e.g. for (plant) cell transformation), including DNA that can be transcribed into an RNA encoding the enzyme(s) to be employed. In a preferred embodiment at least one of the enzymes of a pathway according to the present invention expressed in such a transgenic organism is heterologous with respect to the organism, i.e. it is not naturally expressed in said organism but is naturally expressed in a different organism. More preferably, at least 2, at least 3 or at least 5 of the enzymes of a pathway of the present invention present in such a transgenic plant are heterologous to the transgenic organism and are expressed from nucleic acid sequences which have been introduced into said organism by way of genetic engineering. 
     The polypeptides having the enzymatic activities as required for the present invention may comprise an amino acid sequence targeting them into organelles (e.g. a plastid (e.g. a chloroplast), preferably to the stroma (matrix) of the plastid (e.g. chloroplast)), but also to the organelle (e.g. plastid) membrane and/or the cytoplasm. Suitable targeting sequences are known in the art. Preferably, the chloroplast transit peptide derived from the ribulose-I,5-bisphosphate carboxylase gene (e.g. from  Solanum tuberosum  (GenBank: G68077, amino acids 1-58)) is used for targeting the polypeptides according to the present invention to the plastids. 
     Alternatively, the polypeptides are directly targeted to the plastid using transformation of the plastid genome by particle bombardment (for example of leaf sections) and integration by homologous recombination. Suitable vectors and selection systems are known in the art. The coding sequences for the polypeptides may either be transferred in individual vectors or in one construct, where the individual open reading frames may be fused to one or several polycistronic RNAs with ribosome binding sites added in front of each individual open reading frame in order to allow independent translation. 
     Some enzymes, for example enzymes of the CBBC and/or photorespiration, e.g., Rubisco, glyceraldehyde 3-phosphate dehydrogenase, glycolate 2-phosphatase, are abundant enzymes inside plant plastids/chloroplasts and thus do not have to be transferred to the organism, cell, tissue or plastids to enable function of the biochemical pathway of the invention. 
     The present invention further relates to an organism, tissue, cell or organelle expressing at least one of the enzymes as defined herein. The expression is particularly meant to be a heterologous expression. 
     The present invention further relates to a method of enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO 2  comprising the step of providing an organism, a tissue, a cell or a organelle of the invention. What has been said with respect to the features of this method herein elsewhere also applies here,  mutatis mutandis.    
     The present invention further relates to a use of an organism, a tissue, a cell or a organelle of the invention for enzymatically converting 2-PG into an intermediate compound of the CBBC without releasing CO 2 . What has been said with respect to the features of this use herein elsewhere also applies here, mutatis mutandis. 
     As described herein above, the pathways of the present invention may comprise so called “non-native conversion” or “non-native reactions” which can be catalyzed by enzymes as described above. Preferably, the non-native reactions of the photorespiration bypass pathways of the current invention (cf., for example, the bold arrows in the appended Figures) are catalyzed by the respective enzymes depicted in Table 3. It is of course also possible to employ enzymes, which are derived from any of the listed existing enzymes, e.g. by the introduction of mutations or other alterations which, for example, alter or improve the enzymatic activity so as to be more efficient in the desired enzymatic conversion. 
     Methods for modifying and/or improving the desired enzymes are well-known to the person skilled in the art and include, e.g., random mutagenesis or site-directed mutagenesis and subsequent selection of enzymes having the desired properties or approaches of the so-called “directed evolution”, DNA shuffling or in vivo evolution. 
     For example, for genetic engineering in prokaryotic cells, a nucleic acid molecule encoding a enzyme can be introduced into plasmids which permit mutagenesis or sequence modification by recombination of DNA sequences. Standard methods (see Sambrook and Russell (2001), Molecular Cloning: A Laboratory Manual, CSH Press, Cold Spring Harbor, N.Y., USA) allow base exchanges to be performed or natural or synthetic sequences to be added. DNA fragments can be connected to each other by applying adapters and linkers to the fragments. Moreover, engineering measures which provide suitable restriction sites or remove surplus DNA or restriction sites can be used. In those cases, in which insertions, deletions or substitutions are possible, in vitro mutagenesis, “primer repair”, restriction or ligation can be used. In general, a sequence analysis, restriction analysis and other methods of biochemistry and molecular biology are carried out as analysis methods. The resulting enzyme variants are then tested for their enzymatic activity. 
     In particular, in the current invention, modifying and/or improving the desired enzymes can be achieved by systematically screening orthologs and close paralogs of the respective enzymes for the highest activity in catalyzing the respective non-native reactions. To this end enzyme variants are recombinantly overexpressed in an expression host, preferably  E. coli  and are subsequently assessed for their promiscuous enzyme activity. For this purpose, the respective enzyme can be expressed in  E. coli  according to methods well-known in the art and the cells, cell extracts or purified protein can be assessed in corresponding enzymatic assays which are also well-known to the person skilled in the art for the desired enzymatic activity. 
     If the activity of an enzyme for a particular reaction is below the detection limit of the activity assay, directed evolution towards similar substrates that do show some promiscuity can be applied, thus obtaining ‘generalists’ that often show non-native activities (Rockah-Shmuel L. et al. (2012) Nucleic Acids Res 40, 11627-11637; Tokuriki N. et al. (2012) Nature communications 3, 1257). A similar strategy can also be applied if the substrate for a reaction can neither be purchased nor chemically synthesized. 
     Further, the activity of a promiscuous enzyme can be optimized towards catalyzing a desired non-native reaction by directed evolution the respective enzyme. To this end, recently developed strategies for the design and construction of enzyme libraries including phylogenetic (Goldsmith M. et al. (2013) Methods Enzymol 523, 257-283) and computational methods (Khersonsky O. et al. (2012) Proc Natl Acad Sci USA 109, 10358-10363) are used; such libraries deliver improved enzyme variants upon screening of ≤10 3  variants (Goldsmith M. et al. (2013), loc. cit.; Rockah-Shmuel L. et al. (2014) Methods Mol Biol 1179, 129-137). It has been previously demonstrated for a range of enzymes that are not related to this invention that k cat /K M  improvements in the order of 10 2 -10 5  could be achieved (Tokuriki N. et al. (2012), loc. cit.; Khersonsky O. et al. (2012), loc. cit.; Cherny I. et al. (2013)  ACS Chem Biol  8, 2394-2403) using these methods, even in cases in which the activity was below the detection limit in the starting enzyme (Rockah-Shmuel L. et al. (2012), loc. cit.). By applying libraries designed by using a consensus, phylogenetic approach (Goldsmith M. et al. (2013), loc. cit.; Khersonsky O. et al. (2009)  Biochemistry  48, 6644-6654) the enzyme structure can be further optimized for improved folding and stability (Khersonsky O. et al. (2012), loc. cit.; Aharoni A. et al. (2004)  Proc Natl Acad Sci USA  101, 482-487). 
     To drive the use of NADP(H) as the sole electron donor/acceptor, either enzymes that natively use NADPH are selected, or the cofactor specificity of NADH-dependent paralog enzymes are switched, as previously described for many oxidoreductases (e.g. see Watanabe S. et al. (2005) J Biol Chem 280, 10340-10349; Ehsani M. et al. (2009) Biotechnol Bioeng 104, 381-389). 
     To additionally improve pathway flux, co-localization of different enzymes can be enforced by fusion of two or more enzymes, into complexes that funnel intermediates between the different components. The folding of such constructs can be optimized by directed evolution as described above. Alternatively, scaffolding using engineered protein-protein interactions is implemented (Dueber J. E. et al. (2009) Nat Biotechnol 27, 753-759; Moon T. S. et al. (2010) Metab Eng 12, 298-305). The cellulosome provides a potential source of scaffolding proteins that can be grafted onto our metabolic systems (Smith S. P. et al. (2013)  Curr Opin Struct Biol  23, 686-694). 
     Thus, in one embodiment, the organism, tissue, cell or organelle of the present invention expresses at least one fusion protein comprising at least two of the enzymes of a pathway according to the present invention. 
     The enzymes capable of catalyzing the non-native reactions listed in the Table 3, highlighted in the Figures and/or mentioned herein elsewhere comprise existing enzymes having the promiscuous activity of catalyzing the respective non-native conversions. In addition, the enzymes if unmodified have affinity to their natural substrates. The enzymes capable of catalyzing the non-native reactions listed in the Table 3, highlighted in the Figures or mentioned elsewhere further comprise improved variants of these existing enzymes that have improved enzymatic activity for the non-native reactions and lowered affinity for their native substrates. Furthermore also enzyme variants that are only capable of catalyzing the non-native reactions, but no longer have affinity for their natural substrates are included. 
    
    
     
       The present invention is further described by reference to the following non-limiting figures and examples. 
       The Figures show: 
         FIG. 1  (A) shows a carbon-positive photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-glycerate 3-phosphate. The enzymatic conversion of 2-PG into D-glycerate 3-phosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into tartronytl-CoA (reaction 3#, as indicated in the Figure), further enzymatic conversion of tartronytl-CoA into tartronate semialdehyde (reaction 4#, as indicated in the Figure), further enzymatic conversion of tartronate semialdehyde into D-glycerate (reaction 5, as indicated in the Figure), and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (reaction 6, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (B) shows a carbon-neutral photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-ribulose 1,5-bisphosphate. The enzymatic conversion of 2-PG into D-ribulose 1,5-bisphosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#, as indicated in the Figure), further enzymatic conversion of glycolaldehyde into D-ribulose 1-phosphate (reaction 8, as indicated in the Figure), and further enzymatic conversion of D-ribulose 1-phosphate into D-ribulose 1,5-bisphosphate (reaction 9#, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (C) shows a carbon-neutral photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-erythrose 4-phosphate. The enzymatic conversion of 2-PG into D-ribulose 1,5-bisphosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#, as indicated in the Figure), further enzymatic conversion of glycolaldehyde into D-erythrose (reaction 10#, as indicated in the Figure), and further enzymatic conversion of D-erythrose into D-erythrose 4-phosphate (reaction 11#, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (D) shows a carbon-positive photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-glycerate 3-phosphate. The enzymatic conversion of 2-PG into D-glycerate 3-phosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glyoxylate (reaction 12, as indicated in the Figure), further enzymatic conversion glyoxylate into glycine (reaction 13, as indicated in the Figure), further enzymatic conversion of glycine into serine (reaction 14, as indicated in the Figure), further enzymatic conversion of serine into hydroxypyruvate (reaction 13, as indicated in the Figure), further enzymatic conversion of hydroxypyruvate to glycerate (reaction 18, as indicated in the Figure), and further enzymatic conversion of D-glycerate into D-glycerate 3-phosphate (reaction 6, as indicated in the Figure). The enzymatic conversion of glycine into serine is dependent on the enzymatic conversion of CO 2  into formate (reaction 15#, as indicated in the Figure), further enzymatic conversion of formate into formyl-tetrahydrofolate (reaction 16, as indicated in the Figure), and further enzymatic conversion of formyl-tetrahydrofolate into methylene-tetrahydrofolate (reaction 17, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (E) shows a carbon-neutral photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-ribulose 5-phosphate. The enzymatic conversion of 2-PG into D-ribulose 5-phosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#, as indicated in the Figure), further enzymatic conversion of glycolaldehyde into D-arabinose 5-phosphate (reaction 78# as indicated in the Figure), and further enzymatic conversion of D-arabinose 5-phosphate into D-ribulose 5-phosphate (reaction 80, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (F) shows a carbon-neutral photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-xylulose 5-phosphate. The enzymatic conversion of 2-PG into D-xylulose 5-phosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#, as indicated in the Figure), further enzymatic conversion of glycolaldehyde into D-xylulose (reaction 67#, as indicated in the Figure), and further enzymatic conversion of D-xylulose into D-xylulose 5-phosphate (reaction 69, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 1  (G) shows a carbon-neutral photorespiration bypass pathway in which 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) is enzymatically converted into the CBBC intermediate compound D-xylulose 5-phosphate. The enzymatic conversion of 2-PG into D-xylulose 5-phosphate involves the enzymatic conversion of 2-PG into glycolate (reaction 1, as indicated in the Figure), further enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#, as indicated in the Figure), further enzymatic conversion of glycolyl-CoA into glycolaldehyde (reaction 7#, as indicated in the Figure), and further enzymatic conversion of glycolaldehyde into D-xylulose 5-phosphate (reaction 97#, as indicated in the Figure). The reactions as indicated above and in the Figure can, for example, be catalyzed by the enzymes as listed in Tables 2 and 3 under the respective reaction number. 
         FIG. 2  shows multiple metabolic transformation that convert 2-PG (2-phosphoglycolate, here referred to as glycolate 2-phosphate) to glycolyl-CoA, glycolaldehyde and glycolaldehyde 2-phosphate (see Tables 2 and 3 for the identity of the reactions and for enzymes that can, for example catalyze these reactions). 
         FIG. 3  shows variants of the photorespiration bypass pathways shown in  FIG. 1 . (see Tables 2 and 3 for the identity of the reactions and for enzymes that can, for example catalyze these reactions) and additional photorespiration bypass pathways provided by the present application. 
       Specifically,  FIG. 3H  presents multiple ways to self-condense glycolaldehyde or to condense glycolaldehyde with glycolaldehyde phosphate to generate tetrose or tetrose phosphate, respectively, where tetrose can either be erythrose, erythrulose or threose. These tetroses can be interconverted one to another as shown in  FIG. 3L . 
       Specifically,  FIG. 3L  presents metabolic conversions that can lead to the conversion of an intermediate of the CBBC to dihydroxyacetone, glyceraldehyde and/or erythrose, which can further be used by some of the pathways shown in  FIG. 3A-K  to assimilate 2-PG to the CBBC.  FIG. 3L  (second page) further present interconversions of tetroses and tetroses phosphate, where tetrose can either be erythrose, erythrulose or threose. 
         FIG. 4  shows further alternative photorespiration bypass pathways that do not release CO 2 . (see Tables 2 and 3 for the identity of the reactions and for enzymes that can, for example, catalyze these reactions) 
         FIG. 5  shows the CBBC and all of its metabolic intermediates: D-glycerate 3-phosphate, D-glycerate 1,3-bisphosphate, D-glyceraldehyde 3-phosphate, dihydroxyacetone phosphate (also referred to as glycerone phosphate), D-fructose 1,6-bisphosphate, D-fructose 6-phosphate, D-sedoheptulose 7-phosphate, D-sedoheptulose 1,7-bisphosphate, D-erythrose 4-phosphate, D-xylulose 5-phosphate, D-ribose 5-phosphate, D-ribulose 5-phosphate, and D-ribulose 1,5-bisphosphate. 
         FIG. 6  shows a metabolic strategy to select for the activities of segments of the pathway shown in  FIG. 1B  in a heterotrophic host. Full line arrows show the natural D-arabionase degradation pathway. First selection step (semi-dashed arrows) involves deleting fucA, overexpressing the enzyme catalyzing reaction 9 (see Table 3) together with Rubisco, and feeding the cells with D-arabinose. In the second selection step (dashed arrows) the expression of fucA is reestablished, and the enzymes supporting glycoladehyde oxidation and growth on glycolate are deleted. This strain is fed with glycolaldehyde as sole carbon source. In the third and final selection step (dotted arrows), the enzymes catalyzing reactions 2 and 7 (see Table 3) are expressed in the above strain and glycolate is added as sole carbon source. 
         FIG. 7 : UPLC-hrMS analysis of glycolyl-CoA formed within reaction of PCT. A: Extracted ion chromatogram of glycolyl-CoA. B: Mass spectrum of glycolyl-CoA. 
         FIG. 8 : A: Reactions of the synthetic photorespiratory bypass with the corresponding enzymes. B: Michaelis-Menten kinetics for PCT Re . The corresponding K m  for glycolate is 51.7±9.6 mM, v max  is 1.3±0.07 U mg −1 . n=3. C: Michaelis-Menten kinetics for PCC double mutant (PCC Me _D407I_Y143H). The corresponding K m  is 1.0±0.15 mM, v max  is 1.5±0.09 U mg −1 . n=2. D: Michaelis-Menten kinetics for MCR Ca . The corresponding K m  for tartronyl-CoA is 0.03±0.003 mM, v max  is 0.6±0.01 U mg −1 . n=3. 
       The curves were fitted in Graph Pad Prism 6. 
         FIG. 9 : Michaelis-Menten kinetics for PCT Cp . The curve was fitted in Graph Pad Prism 6. The corresponding K m  for glycolate is 149±35 mM, v max  is 31.6±2.7 mU mg −1 . n=1 (preliminary result). 
         FIG. 10 : UPLC-hrMS analysis of tartronyl-CoA formed by PCC Me _D407I_Y143H. A: Extracted ion chromatogram of tartronyl-CoA. B: Mass spectrum of tartronyl-CoA. C: Mass spectrum of tartronyl-CoA. The reaction was performed with  13 C labeled bicarbonate. 
         FIG. 11 : UPLC-hrMS analysis of glycerate formed of glycolyl-CoA by PCC Me  and MCR Ca . A: Extracted ion chromatogram of glycerate. B: Mass spectrum of glycerate. C: Mass spectrum of glycerate. The reaction was performed with  13 C labeled bicarbonate. 
         FIG. 12 : Michaelis-Menten kinetics for MCR E . The curve was fitted in Graph Pad Prism 6. The corresponding K m  for tartronyl-CoA is 0.18±0.04 mM, v max  is 0.23±0.01 U mg −1  (n=2). 
     
    
    
     In this specification, a number of documents including patent applications are cited. The disclosure of these documents, while not considered relevant for the patentability of this invention, is herewith incorporated by reference in its entirety. More specifically, all referenced documents are incorporated by reference to the same extent as if each individual document was specifically and individually indicated to be incorporated by reference. 
     The invention will now be described by reference to the following examples which are merely illustrative and are not to be construed as a limitation of the scope of the present invention. 
     EXAMPLE 1: EXPLORATION OF SYNTHETIC PHOTORESPIRATION BYBASS ROUTES 
     Four highly advantageous photorespiration bypass pathways according to the present invention are shown in  FIG. 1 . They contain between one to four non-native reactions (as defined above) and are either CO 2 -neutral ( FIG. 1B , C) or CO 2 -positive (supporting net carbon fixation,  FIG. 1A , D). These pathways are all short, thermodynamically favourable, energetically efficient, and overlap only minimally with non-photorespiratory central metabolism. The enzymatic conversions employed in the pathways described herein are characterized in that they are thermodynamically feasible, i.e. they are thermodynamically feasible conversions, which can in principle be catalyzed by enzymes. Moreover, the enzymatic conversions, as described herein, shall have a high driving force and will therefore generally not limit the pathway flux, thereby leading to high pathway efficiency. 
     Notably, there are multiple alternative implementation schemes of the pathways shown in  FIGS. 1A , B, C, and D as discussed above and further presented in, for example  FIG. 2  and  FIG. 3 . Furthermore, other types of photorespiration bypass routes are shown in  FIG. 4 ; these all provide alternative approaches to support increased yield of photorespiration. 
     The non-native reactions of the pathways shown in  FIG. 1  and some alternatives thereof shown in the other Figures as well as exemplifying promiscuous enzymes capable of catalyzing these non-native reactions are described in more detail in the following: 
     Glycolate can be converted into Glycolyl-CoA (reaction 2#) by a range of enzymes, including a CoA-transferase (Volodina E. et al., 2014 , Appl Microbiol Biotechnol  98, 3579-3589; Dhamankar H. et al., 2014 , Metab Eng  25 C,  72-81), an ADP-forming CoA ligase (Awano T. et. al., 2014, loc. cit.), or an AMP-forming CoA ligase (Soucaille P. et al., 2012, loc. cit.). Glycolyl-CoA can be further reduced to glycolaldehyde (reaction 7#) by several acylating aldehyde dehydrogenases (Burton R. M. et al., 1953, loc. cit.; Sohling, B. et. al., 1993, loc. cit.).  FIG. 2  presents multiple alternative reaction sequences that can generate glycolyl-CoA and glycolaldehyde from glycolate. For example, glycolate can be converted to glycolyl phosphate (reaction 19#) by a promiscuous carboxyl kinase enzyme, such as acetate kinase (Lyer P. et al., 2005, loc. cit.) or butyrate kinase (Hartmanis M. G., 1987, loc. cit.), or by the transfer of a phosphate group from another carboxylic acid. Glycolyl phosphate can then be reduced to glycolaldehyde (reaction 20#) by a phosphorylating glyceraldehyde 3-phosphate dehydrogenase (Fife T. H. et al., 1970 , Biochemistry  9, 4064-4067; Armstrong J. M. et al., 1976 , Biochem J  159, 513-527; Byers L. D., 1978 , Arch Biochem Biophys  186, 335-342), or converted to glycolyl-CoA (reaction 21#) via a non-specific phosphate acetyltransferase enzyme (as some glucosamine 6-phosphate acetyltransferase variants can accept glycolyl-CoA instead of acetyl-CoA (Macauley M. S., 2012, loc. cit.). Another possibility is the direct reduction of glycolate to glycolaldehyde by an ATP- and NAD(P)H-dependent carboxylic acid reductase (CAR; reaction 22#). Several variants of this enzyme were shown to catalyze the reduction of acetate and lactate at high rate (Venkitasubramanian P., 2006, loc. cit.; Napora-Wijata K., 2014, loc. cit.), strongly indicating that glycolate can also be accepted as substrate. 
     Carboxylation of glycoyl-CoA to tartronyl-CoA (reaction 3#) can be catalyzed by a promiscuous biotin-dependent acyl-CoA carboxylase (e.g. see Tran T. H. et al., 2015, loc. cit.). Tartronyl-CoA can be reduced to tartronate semialdehyde (reaction 4#) by a nonspecific acylating aldehyde dehydrogenase enzyme (e.g. see Baker P. et al., 2012, loc. cit.). 
     The phosphorylation of D-ribulose 1-phosphate to D-ribulose 1,5-bisphosphate (reaction 9#) is expected to be catalyzed by two enzyme families: (i) Variants of 1-phosphofructokinase given that several enzymes confuse D-ribulose and D-fructose—e.g., fructose 1,6-bisphosphatase can dephosphorylate ribulose 1,5-bisphosphate (Mizunuma H. et al., 1980 , Arch Biochem Biophys  201, 296-303; Donahue J. L. et al., 2000 , J Bacteriol  182, 5624-5627) and phosphoribulokinase can phosphorylate fructose 6-phosphate (Siebert, K., 1981, loc cit.); (ii) Nonspecific variants of D-ribulose 5-kinase (e.g. see Lee L. V. et al., 2001, loc. cit.) which can accept D-ribulose 1-phosphate as an alternative substrate. 
     D-ribulose 1-phosphate can also be assimilated to the CBBC via its isomerisation to D-ribose 1-phosphate (reaction 29# in  FIG. 3 ), catalyzed promiscuously by a 5-methylthio-D-ribulose 1-phosphate 1,2-isomerase, such as Rru_A0360 (Saito Y. et al., 2007, loc. cit.; Erb T. J. et al., 2012, loc. cit.): in a preliminary study we found that this reaction occurs with measurable rate (k cat =0.03 s −1 , k cat /K M &lt;20 M −1 s −1 ). Preferably, such rate can even be evolutionary further optimized. D-ribose 1-phosphate can then be converted to the CBBC&#39;s intermediate D-ribose 5-phosphate (reaction 30) by D-ribose 1,5-phosphomutase (Hammer-Jespersen K. et al., 1970, loc. cit.). Alternatively, D-ribose 1-phosphate can be phosphorylated to D-ribose 1,5-bisphosphate (reaction 31) by ADP-dependent ribose-1-phosphate kinase and then isomerised to D-ribulose 1,5-bisphosphate (reaction 32) by ribose-1,5-bisphosphate isomerise (Aono R. et al., 2015, loc. cit.). 
     A notable variant of the pathway shown in  FIG. 1B  bypasses the initial dephosphorylation of 2-PG and instead reduce it to glycolaldehyde phosphate via 2-phospohglycolyl phosphate intermediate (reactions 23# and 24# in  FIG. 2 ). 2-PG conversion into 2-phospohglycolyl phosphate can proceed by transferring a phosphate group from another carboxylic acid or by utilizing a kinase enzyme such as 3-phosphoglycerate kinase: 2-PG was found to be a competitive inhibitor of this enzyme (Tompa P. et al., 1986, loc. cit.; Vas M., 1990, loc. cit.; Szilagyi A. N. et al., 1998, loc. cit.), indicating that it can also serve as a substrate for at least some enzyme variants. The reduction of 2-phosphoglycolyl phosphate can be catalyzed by a phosphorylating glyceraldehyde 3-phosphate dehydrogenase: this enzyme catalyzes the reduction of glycolyl phosphate (Fife T. H. et al., 1970, loc. cit.; Armstrong J. M. et al., 1976, loc. cit.; Byers L. D., 1978, loc. cit.) and the presence of a terminal phosphate moiety enhances the reactivity (Byers L. D., 1978, loc. cit.). Glycolaldehyde 2-phosphate can be then condensed with dihydroxyacetone phosphate to give the CBBC intermediate D-ribulose 1,5-bisphosphate (reaction 28#). This reaction is known to be catalyzed L-fuculose 1-phosphate aldolase, the same enzyme that can also condense glycolaldehyde and dihydroxyacetone phosphate (Ghalambor M. A. et al., 1962, loc. cit.; Ghalambor, M. A. et al., 1966, loc. cit.). 
     The condensation of glycolaldehyde molecules to form D-erythrose (reaction 10#) can be catalyzed by an aldolase enzyme. Nonspecific aldolases, which can accept unphosphorylated donor and acceptor, and catalyze a reaction with glycolaldehyde as an acceptor (e.g. see Schirmann M. et al., 2001, loc. cit.; Chiu T. H. et al., 1969, loc. cit.), are expected to catalyze this reaction. 
     The phosphorylation of D-erythrose to D-erythrose 4-phosphate (reaction 11#) can be catalyzed by dihydroxyacetone kinase (Herz S. et al., 2002, loc. cit.). 
     The reduction of CO 2  to formate (reaction 15#) can be supported by a ferredoxin-dependent formate dehydrogenase, where the ferredoxin is reduced by photosystem 1, or by electrons donated directly from components of the electron transport chain, including one of the photosystems. 
     Two other CO 2 -positive photorespiration bypass pathways can be established by the direct conversation of glycolyl-CoA to hydroxypyruvate (which is then reduced to D-glycerate, either directly or via initial isomerization to tartronate semialdehyde, and further phosphorylated to D-glycerate 3-phosphate). 
     In the first approach, glycolyl-CoA is converted to hydroxypyruvate via a (reversible) pyruvate:ferredoxin oxidoreductase enzyme (also referred to as pyruvate synthase, reaction 55#) (Furdui C. et al., 2000, loc. cit.). While this enzyme is generally oxygen sensitive, there exist several bacteria and archea that operate this enzyme under full microaerobic or aerobic conditions. These include  Hydrogenobacter thermophilus  TK-6 (Yoon K. S. et al., 1997, loc. cit.),  Sulfolobus  sp. strain 7 (Fukuda E. et al., 2002, loc. cit.), and  Halobacterium halobium  (Plaga W. et al., 1992, loc. cit.). Moreover, multiple studies indicate that enzyme maturation can occur correctly under aerobic condition when expressed in a foreign host (Fukuda E. et al., 2002, loc. cit.; Yamamoto M. et al., 2003, loc. cit.). Further, several studies indicates that plant-like ferredoxin can replace the native ferredoxin with only a little effect on activity. For example, pyruvate:ferredoxin oxidoreductase from  Desulfovibrio africanus  can accept algal ferredoxin, resulting in 60% of the original rate (Pieulle L. et al., 2004 , Biochemistry  43: 15480-15493). As some variants of pyruvate:ferredoxin oxidoreductase are known to by promiscuous in the substrates they can accept (e.g. Fukuda E. et al., 2002, loc. cit.), glycolyl-CoA is expected to serve as a substrate for at least some of the enzymes. Finally, some enzyme variants use NADPH as the electron acceptor, instead of ferredoxin, and can operate under (micro)aerobic conditions (e.g., the enzyme from  Euglena gracilis  (Inui H., 1987, loc. cit.)); these enzymes are also likely to support the conversion of glycolyl-CoA to hydroxypyruvate. 
     In the second approach, CO 2  is first reduced to formate (reaction 15#) by a ferredoxin-dependent formate dehydrogenase or by electrons donated directly from components of the electron transport chain, including one of the photosystems. Glycolyl-CoA is then converted to hydroxypyruvate via a (fully reversible) pyruvate formate lyase enzyme (reaction 54#) (Buis J. M. et al., 2005, loc. cit.). The reaction of pyruvate formate lyase (PFL) takes place via a radical mechanism, which involves a glycyl radical (Becker A. et al., 1999, loc. cit.; Plaga W. et al., 2000, loc. cit.; Becker A. et al., 2002, loc. cit.). Pyruvate formate lyase activating enzyme (PFL-AE) generates the stable and catalytically essential glycyl radical (Buis J. M. et al., 2005, loc. cit.; Vey J. L. et al., 2008, loc. cit.). The glycyl radical is susceptible to destruction by oxygen, which results in irreversible cleavage of the polypeptide and inactivation of PFL (Sawers G. et al., 1998, loc. cit.; Zhang W. et al., 2001, loc. cit.). However, previous studies have shown that  E. coli  cells grown under microaerobic conditions produce a significant amount of formate, indicating that PFL retains its activity in the presence of oxygen (Alexeeva S. et al., 2000 , J Bacteriol  182: 4934-4940; Levanon S. S. et al., 2005 , Biotechnol Bioeng  89: 556-564; Zhu J. et al., 2007 , Biotechnol Bioeng  97: 138-143) and could be further evolved to become more oxygen tolerant. The product of the yfiD gene in  E. coli  was shown to reactivate PFL in the presence of oxygen by replacing its fragmented part (Zhu J. et al., 2007, loc. cit.; Wagner A F, 2001, loc. cit.). Some variants of pyruvate formate lyase have broad substrate specificity (Hesslinger C. et al., 1998, loc. cit.; Sawers G. et al., 1998, loc. cit.) and hence are expected to accept glycolyl-CoA. 
     EXAMPLE 2: CALCULATED IMPROVEMENTS OF CBBC ACHIEVED BY THE PHOTORESPIRATION BYPASS PATHWAYS OF FIG.  1   
     The exact fraction of Rubisco&#39;s oxygenation reaction is debated; however, multiple studies determined independently that, for, for example, C3 plants, this fraction is in the range of 20% to 30% (Zhu X. G., et al. (2010) loc. cit.; Peterhansel C., et al. (2013) loc. cit.; Ogren W. L. (1984) loc. cit.; Sharkey T. D. (1988) loc. cit.; Cegelski L., et al. (2006) loc. cit.; Zhu X. G., et al. (2007) loc. cit.; Andersson I. (2008) loc. cit.; Sage R. F., et al. (2012) loc. cit.; Busch F. A. (2013) loc. cit.; Szecowka M., et al. (2013) loc. cit.; Ma F., et al. (2014) loc. cit.; Misra J. B. (2014) loc. cit.). Assuming an average oxygenation fraction of 25%, the photorespiration bypass routes shown in  FIG. 1  can support substantially higher carbon fixation and photosynthetic efficiency (Table 1). For comparison, the previously suggested photorespiration bypass routes support, at best, minimal decreases in ATP and NADPH consumption (≤8% and ≤14%, respectively) with no improvement in the productivity of the CBBC. 
     These calculations show that the CO 2 -neutral and CO 2 -positive photorespiration pathways of this invention (as, for example, in  FIG. 1 ) have a significant advantage over their natural counterparts, both under strong illumination, where growth is mainly limited by the activity of the CBBC, and under low light, where growth is limited by the supply of ATP and NADPH (Xin C. et al., 2014 , Plant Physiol  dx.doi.org/10.1104/pp. 114.248013). Accordingly, the calculations indicate that implementation of these novel bypass routes in e.g. C3 plants would significantly increase plant growth rate and biomass yield under various environmental conditions. 
     EXAMPLE 3: ENGINEERING OF INDIVIDUAL ENZYME COMPONENTS 
     Enzymes that promiscuously catalyze non-native reactions as described herein can be evolved so as to catalyzing the respective non-native reactions with higher efficiency in order to further increase the efficiency of the photorespiration bypass pathways of this invention. 
     Given that the level of promiscuity typically varies dramatically between homologues (Khersonsky O. et al. (2010)  Annu Rev Biochem  79, 471-505; Afriat L. et al. (2006)  Biochemistry  45, 13677-13686; Bar-Rogovsky H. et al. (2013)  J Biol Chem  288, 23914-23927), this is for example achieved by systematically screening orthologs and close paralogs of the respective enzymes for the highest activity in catalyzing the respective non-native reactions. To this end enzyme variants are recombinantly overexpressed in an expression host, preferably  E. coli  and are subsequently assessed for their promiscuous enzyme activity. If the activity of an enzyme for a particular reaction is below the detection limit of the activity assay, directed evolution towards similar substrates that do show some promiscuity can be applied, thus obtaining ‘generalists’ that show desired non-native activities (Rockah-Shmuel L. et al. (2012) loc. cit.; Tokuriki N. et al. (2012), loc. cit.). A similar strategy can also be applied if the substrate for a reaction can neither be purchased nor chemically synthesized. 
     Further, the activity of a promiscuous enzyme can be optimized towards catalyzing a desired non-native reaction by directed evolution of the respective enzyme. To this end, recently developed strategies for the design and construction of enzyme libraries including phylogenetic (Goldsmith, M., et al. (2013), loc. cit.) and computational methods (Khersonsky O. et al. (2012), loc. cit.) are used; such libraries deliver improved enzyme variants upon screening of ≤10 3  variants (Goldsmith, M., et al. (2013), loc. cit.; Rockah-Shmuel L. et al. (2014), loc. cit.). It has been previously demonstrated for a range of enzymes that are not related to this invention that k cat /K M  improvements in the order of 10 2 -10 5  could be achieved (Tokuriki N. et al. (2012), loc. cit.; Khersonsky O. et al. (2012), loc. cit.; Cherny I. et al. (2013), loc. cit.) using these methods, even in cases in which the activity was below the detection limit in the starting enzyme (Rockah-Shmuel L. et al. (2012) loc. cit.). By applying libraries designed by using a consensus, phylogenetic approach (Goldsmith, M., et al. (2013), loc. cit.; Khersonsky O. et al. (2009); loc. cit.) the enzyme structure can be further optimized for improved folding and stability (Khersonsky O. et al. (2012), loc. cit.; Aharoni, A., et al. (2004), loc. cit.). 
     The oxidoreductase enzymes employed in the context of the current invention are intended to preferably utilize NADP(H) and not other electron donor/acceptor. Unlike NAD + , NADP +  is directly reduced in photosynthesis, allowing photosynthetic electron flow to be directly coupled to an electron-consuming photorespiration bypass. Moreover, under illumination, the chloroplastic reduction potential of NADP(H) is considerably lower than that of NAD(H), which increases the driving force of electron-consuming reactions (Heineke D., et al., 1991 , Plant Physiol  95, 1131-1137). To drive the use of NADP(H) as the sole electron donor/acceptor, either enzymes that natively use NADP(H) are selected, or the cofactor specificity of NAD(H)-dependent paralog enzymes are switched, as previously described for many oxidoreductases (e.g. see Watanabe S. et al. (2005) loc. cit.; Ehsani M. et al. (2009) loc. cit.). 
     To additionally improve pathway flux, co-localization of different enzymes can be enforced by fusion of two, or more enzymes, into complexes that funnel intermediates between the different components. The folding of such constructs can be optimized by directed evolution as described above. Alternatively, scaffolding using engineered protein-protein interactions is implemented (Dueber J. E. et al. (2009), loc. cit.; Moon T. S. et al. (2010), loc. cit.). The cellulosome provides a potential source of scaffolding proteins that can be grafted onto our metabolic systems (Smith S. P. et al. (2013), loc. cit.). 
     In the context of this invention, an enzyme activity test is performed by providing the respective substrate to living host cells expressing the respective enzyme, to a crude extract comprising the respective enzyme or to the respective purified enzyme, and the turnover of said substrate is measured by detecting directly or indirectly the appearance of the desired product and/or the turnover of the respective substrate. Suitable detection methods are LC-MS (Bennett B. D. et al., 2009 , Nat. Chem. Biol.  5(8), 593-9) or spectrometric assays (e.g., formation of NAD(P)H results in increased fluorescence at a wavelength of 340 nm; Berrios-Rivera S J, 2002 , Metab Eng.  4(3), 217-29). Respective substrates and products are either purchased or synthesized. 
     EXAMPLE 4: ESTABLISHING PATHWAY ACTIVITY IN VITRO AND IN VIVO 
     In Vitro Reconstitution and Optimization of the Pathways 
     A dedicated in vitro platform is used to systematically test and further optimize the synthetic photorespiration bypass pathways of this invention. The in vitro platform is similar in design to already described systems (Bujara M. et al. (2011)  Nat Chem Biol  7, 271-277; Goh E. B. et al. (2014)  Metab Eng  26 C,  67-76). It consists of a small micro-reactor (1-20 ml in size), in which all purified enzymatic components, necessary cofactors (e.g., NAD(P)(H), ATP) and respective substrate(s) of the synthetic pathway are combined. The micro-reactor is directly coupled to a high resolution mass spectrometer (e.g., a QTOF-system) via an injection pump (operating at flow rates of 10-100 μl/min). The high resolution mass spectrometer allows identifying and quantifying the concentration of the metabolites of the synthetic pathway and their changes over time in the micro-reactor. With this setup, the rate(s) of product formation (i.e., pathway efficiency), as well as the pathway&#39;s boundary conditions can be tested systematically with changing parameters (different iso-enzymes, different enzyme concentrations, etc.) in a medium throughput approach. This allows to analyze enzymes and their optimal concentrations, thereby achieving highly efficient and robust operating pathways in vitro. 
     In Vivo Reconstitution and Optimization of the Pathways in  E. coli    
       E. coli  is easy to manipulate genetically and metabolically, and has a short doubling time, and can hence be used to evolutionary optimize the kinetics of the synthetic pathways. The pathways are incrementally established in  E. coli , at each step selecting for enhanced activity of one pathway segment. For example, the realization of the bypass route in  FIG. 1B  is performed as follows ( FIG. 6 ). Step 1: in a ΔglcDEF fuc+  E. coli  strain that can metabolize D-arabinose but not glycolate (LeBlanc D. J. et al. (1971)  J Bacteriol  106, 82-89; Zhu Y. et al. (1986)  J Mol Evol  23, 259-266), fucA is deleted and the enzymes catalyzing the reactions downstream of D-ribulose 1-phosphate are introduced. These include the enzyme catalyzing reaction 9# (see Table 3) and Rubisco. Growth of this strain on D-arabinose is dependent on the activity of the introduced pathway segment. Step 2: fucA is reintroduced and the strain is cultivated with glycolaldehyde as a sole carbon source (glycerone phosphate is recycled). Step 3: the segment reducing glycolate to glycolaldehyde completes the synthetic pathway to support growth on glycolate as sole carbon source. At each step, evolution optimization towards high flux is performed. 
     Dedicated expression of all pathway enzymes may optimize the activity of the non-native pathways. To optimize the regulation of native genes, a rapid and modular methodology can be employed, in which genes of interest are combinatorially paired with a small set of ribosome binding sites along a synthetically assembled operon, modulating the expression levels of the genes by several orders of magnitude (Zelcbuch L. et al. (2013)  Nucleic Acids Res  41, e98). Transformation methodologies as well as promoters, vectors and all other components required for a person skilled in the art to generate such bacteria are for example described in Zelcbuch L. et al. (2013)  Nucleic Acids Res  41, e98. 
     The experimental methodology described here do not just confirm pathway activity in vivo, but further enable to directly evolve enhanced activity: continuous cultivation of glycolate-consuming  E. coli  within a turbidostat can support the evolution of the bacterium to higher growth rate and hence higher pathway activity (Flegr J., 1997 , Journal of Theoretical Biology  188(1), 121-126). 
     In Vivo Reconstitution and Optimization of the Pathways in Cyanobacteria 
     The synthetic photorespiration bypass pathways in accordance with the invention are exemplary implemented in cyanobacteria, which are engineered to become highly dependent on photorespiration (e.g., DccmM  Synechocystis , a carboxysome-less strain that is dependent on high CO 2  concentrations (for example 5% CO 2  atmosphere, which is &gt;100 μM dissolved CO 2 ; Ogawa T. et al. (1994)  Photosynth Res  39, 183-190) and/or that cannot operate one or more of the native photorespiration pathways (e.g., Dtsr that abolishes the glycerate pathway (Eisenhut M. et al. (2008)  Proc Natl Acad Sci USA  105, 17199-17204)). This allows comparing the activity of the different synthetic pathways relative to natural photorespiration, and to directly selecting for high pathway activity in a photosynthetic organism that utilizes the CBBC. In particular. the growth rate, biomass yield, photosynthetic rate and flux via the CBBC in the cyanobacterial strains expressing the synthetic pathways are compared to those of wild-type strains. 
     EXAMPLE 5: ESTABLISHING PATHWAYS IN HIGHER PLANTS AND CHARACTERIZING THEIR PHENOTYPES 
     A high throughput in planta greenhouse screening platform is used to test different synthetic photorespiration pathways in parallel and in two different model species representing the two main classes of crop plants, monocots ( Brachypodium distachyon  (Brutnell T. P. et al. (2015)  Annu Rev Plant Biol.  66, 465-485)) and dicots ( Arabidopsis thaliana ). To express several genes from a single construct, the repetitive nature of the construct is reduced, thus avoiding unwanted gene silencing and recombination. To this end, each gene is expressed in the construct using different regulatory elements (promoters, terminators). To identify promoters that are induced as early as the seedling stage and in all photosynthetic tissues the EVO&#39;s database and mining capabilities are utilized. These promoters are further validated in planta using promoter′::gus fusions (Blume B. et al. (1997)  Plant J  12, 731-746). 
     Whole genome RNA sequencing is carried out to verify expression of the pathway genes in the plant. Where applicable, the chloroplast proteome is further analyzed to verify proper targeting of the expressed enzymes if desired. To comprehensively characterize the in planta responses to the synthetic pathways, changes in architecture, physiology and productivity of plants are measured. Furthermore, to demonstrate that the synthetic photorespiration bypass routes give rise to increased carbon fixation rates, growth rates or biomass yields, transgenic lines carrying the different synthetic pathways may be compared to plants carrying empty vectors. 
     EXAMPLE 6: IN VITRO ESTABLISHMENT OF THE SYNTHETIC PHOTORESPIRATORY BYPASS PATHWAY FROM GLYCOLATE TO GLYCERATE 
     The following example experimentally illustrates the implementation of the photorespiration pathways disclosed herein, in particular the photorespiration bypass pathway as shown in  FIG. 1A . In particular, the example experimentally illustrates that the non-native enzymatic conversions 2#, 3# and 4# as well as the enzymatic conversion 5 can be achieved by using the enzymes described herein. These four enzymatic conversions form part of the photorespiration bypass pathway shown in  FIG. 1A  but also other photorespiration bypass pathways disclosed herein. In particular, the present example also illustrates that the non-native enzymatic conversion of glycolate into glycolyl-CoA (reaction 2#) can be achieved by the enzymes listed herein. Thereby the present example also demonstrates experimentally that 2-PG can be enzymatically converted to glycolyl-CoA (via glycolate) by the proposed enzymatic conversions, using in particular the enzymes provided herein, because reaction 1, which converts 2-PG into glycolate, is a reaction well known with the enzymes disclosed herein (in particular also in plants as part of the natural photorespiration). As mentioned elsewhere herein, the enzymatic conversion of 2-PG into glycolyl-CoA is the first step of a number of photorespiration bypass pathways disclosed herein, which are therefore also experimentally illustrated and supported by the present example. 
     Specifically, in the present example the enzymes listed in Table 4, which are enzymes disclosed in the context of the present invention, were recombinantly expressed and subjected to in vitro activity assays to illustrate their capability of catalyzing the respective enzymatic conversions. The capability of catalyzing the respective enzymatic conversions (see, e.g.,  FIG. 8A  for which enzyme catalyzes which reaction) was assessed by different experimental means that are explained in more detail below. Furthermore, kinetic parameters for the respective reactions and enzymes were determined as described further below and are summarized in Table 5. 
     In the following the experimental analyses including the employed means and methods and results are explained in detail. 
     Construction of Expression Vectors for Heterologous Expression of the Enzymes PCT Re e PCT CP  PCC Me , PCC Me  D407I Y143H, MCR Ca  and MCR E    
     For the heterologous expression of the propionyl-CoA transferase from  Ralstonia eutropha  (PCT Re ; nucleic acid sequence shown in SEQ ID NO: 11; amino acid sequence shown in SEQ ID NO: 12), the previously described vector pET-19b::pct (Lindenkamp et al., 2013 , Applied Microbiology and Biotechnology,  97(17), 7699-7709) was employed. 
     For the heterologous expression of the propionyl-CoA transferase from  Clostridium propionicum  (PCT Cp ; nucleic acid sequence shown in SEQ ID NO: 13; amino acid sequence shown in SEQ ID NO: 14) a pET16b vector containing the gene encoding the PCT CP  was employed (SEQ ID NO: 26). 
     The propionyl-CoA carboxylase enzyme from  Methylobacterium extorquens  (PCC Me ) comprises two independent protein subunits that are expressed by two different genes, namely pccA (nucleic acid sequence is shown in SEQ ID NO: 1; encoded amino acid sequence is shown in SEQ ID NO:2) and pccB (SEQ ID NO: 3; encoded amino acid sequence is shown in SEQ ID NO:4). Thus, to express PCC Me  an expression vector for simultaneous heterologous expression of both the pccA gene and the pccB gene from the same vector with each gene under T7-lac promoter control, respectively was constructed. To this end, the pccA gene (SEQ ID NO: 1) was cloned from  Methylobacterium extorquens  genomic DNA into pTE100 (SEQ ID NO: 20) and the NcoI site within the pccA gene (SEQ ID NO: 1) at position 336 of SEQ ID NO: 1 was mutated by Quick Change PCR to remove a NcoI restriction site resulting in SEQ ID NO: 15. 
     For that, the following primers were used: 
     
       
         
           
               
               
            
               
                   
                 (SEQ ID NO: 16) 
               
               
                   
                 5′-GGTGCCATCGCCGCAATGGGCGACAAGATC-3′; 
               
               
                   
                 and 
               
               
                   
                   
               
               
                   
                 (SEQ ID NO: 17) 
               
               
                   
                 5′-GATCTTGTCGCCCATTGCGGCGATGGCACC-3′. 
               
            
           
         
       
     
     For amplification and introduction of NdeI and KpnI restriction sites of pccA with the modified NcoI site (SEQ ID NO:15) (for subsequent cloning into pCDFduet to construct the pCDFduet_pccB_pccA), the following primers were used: 
     
       
         
           
               
               
            
               
                   
                 (SEQ ID NO: 18) 
               
               
                   
                 5′-CGGCTGCCATATGTTCGATAAGATCCTGATTG-3′; 
               
               
                   
                 and 
               
               
                   
                   
               
               
                   
                 (SEQ ID NO: 19) 
               
               
                   
                 5′-CATGCGTGGTACCTCAGGCGAATTCCAGGATC-3′. 
               
            
           
         
       
     
     For amplification and introduction of NdeI and EcoR1 restriction sites of the pccB gene from  Methylobacterium extorquens  genomic DNA, the following primers were used: 
     
       
         
           
               
               
            
               
                   
                 (SEQ ID NO: 24) 
               
               
                   
                 5′-GACCGTGCATATGAAGGACATCCTCGAGAAGC-3′; 
               
               
                   
                 and 
               
               
                   
                   
               
               
                   
                 (SEQ ID NO: 25) 
               
               
                   
                 5′-GATACATGAATTCTCAGAGCGGGATGTTGTCGT-3′. 
               
            
           
         
       
     
     The pccA gene modified in the NcoI site (SEQ ID NO: 15) as well as the pccB gene (SEQ ID NO: 3) were cloned into the vector pCDFduet to yield the plasmid pCDFduet_pccB_pccA. This vector was employed for heterologous expression of the wilde-type PCC Me . 
     To construct an expression vector for heterologous expression of the mutant variant PCC Me _D407I_Y143H two point mutations (resulting in the amino acid exchanges D407I and Y143H) were introduced into the pccB gene of the above-mentioned pCDFduet_pccB_pccA vector. To this end single-oligo directed mutagenesis was performed (Shenoy and Visweswariah, 2003 , Analytical biochemistry,  319(2), 335-336). To introduce the nucleotide exchange resulting in the D407I amino acid exchange in the encoded pccB protein, the following primer was used: 
     
       
         
           
               
            
               
                 (SEQ ID NO: 21) 
               
               
                 5′-CAAGGCCTTCGGCGGCGCCTACATCGTCATGGCCTCCAAGCATG-3′. 
               
            
           
         
       
     
     After confirmation of the successful mutation via sequencing, another nucleic acid mutation was introduced in the mutated pccB gene resulting in the encoding of the second amino acid exchange, Y143H. For this second PCR the following primer was used: 
     
       
         
           
               
               
            
               
                   
                 (SEQ ID NO: 22) 
               
               
                   
                 5′-GCGCTCGGCGGCCACGGCGAGGTGTTCCGC-3′. 
               
            
           
         
       
     
     The final plasmid for the overexpression of the PCC Me _D407I_Y143H doublemutant protein variant (consisting of pccA with the amino acid sequence shown in SEQ ID NO: 2; and pccB_D407I_Y143H with the amino acid sequence shown in SEQ ID NO: 6) was named pCDFduetpccB_D407I_Y143H_pccA and comprised the modified pccA gene with SEQ ID NO: 15 and the pccB gene encoding the pccB_D407I_Y143H mutant variant with the nucleic acid sequence shown in SEQ ID NO: 5. 
     For the heterologous expression of the MCR Ca  protein (amino acid sequence is shown in SEQ ID NO: 8; corresponding nucleic acid sequence encoding the protein is depicted in SEQ ID NO: 7) the previously described pTRC-MCR Ca  plasmid (Kröger et al., 2011, Analytical biochemistry, 411(1), 100-105) was employed. 
     For the heterologous expression of the MCR E  protein (SEQ ID NO: 10; corresponding nucleic acid encoding the protein is depicted in SEQ ID NO: 9) an expression plasmid was cloned with the backbone pSEVA321 and an  E. coli  codon optimized insert that was provided by the Joint Genome Institute of the US Department of Energy (JGI-DOE), which synthesized the corresponding codon optimized insert comprising a codon optimized version of the gene encoding the MCR E  protein. The complete sequence of the expression plasmid with the insert is depicted in SEQ ID NO: 23) and comprises the codon optimized nucleotide sequence of the gene the MCR E  protein from nucleotide position 115 to 3827 of SEQ ID NO: 23. 
     Heterologous Expression and Purification of Recombinant Proteins 
     For the heterologous overexpression of the PCT Re , the PCT Cp , the PCC Me , the PCC Me _D407I_Y143H, the MCR Ca  and the MCR E  protein, respectively, the corresponding plasmid encoding the respective enzyme was first transformed into chemically competent  E. coli  BL21 (DE3) cells. The cells transformed with the respective plasmid encoding one of said enzymes were then grown on LB agar plates containing 100 μg mL −1  ampicillin (PCT Re , PCT Cp  and MCR Ca ), 34 μg mL −1  chloramphenicol (MCR E ) or 50 μg mL −1  spectinomycin (PCC Me , PCC Me _D407I_Y143H) at 37° C. over night. Subsequently, for expression of the PCC Me  and the PCC Me _D407I_Y143H 1 L selective TB medium was inoculated with the colonies obtained from the overnight culture and grown at 25° C. for 24 h without addition of IPTG, as the T7-lac promoter showed already constitutive expression in the absence of the inducer. For the overexpression of PCT Re , PCT Cp , MCR E  and MCR Ca , cells were cultivated in 1 L selective LB medium at 37° C. to an OD 600  of 0.4 to 0.6, induced with 0.5 mM IPTG and grown over night at 18° C. to 25° C. 
     Cells were harvested at 10 000×g for 10 min and cell pellets were stored at −80° C. until purification of enzymes. Cell pellets of MCR Ca  and MCR E  overexpressing cells were resuspended in two-fold volume of buffer A Strep  (50 mM Tris/HCl, 150 mM NaCl, pH 7.8) containing 0.1 mg mL −1  DNAse I. The cell suspension was passed through a French pressure cell twice at a pressure of 137 MPa and centrifuged at 100 000×g and 4° C. for 1 h. The supernatant was filtered through a 0.45 μm syringe filter and loaded at a flow rate of 1 mL min −1  onto a 1 mL StrepTrap™ HP column (GE healthcare) which had previously been equilibrated with 5 column volumes of buffer A Strep . The column was washed with 20 column volumes of buffer A Strep  and the protein was eluted with buffer A Strep  containing 3 mM desthiobiotin. The enzyme was stored in buffer A Strep  containing 20% glycerol. 
     PCT Re , PCT Cp , PCC Me  and PCC Me _D407I_Y143H overexpressing cells, respectively, were resuspended in two-fold volume of buffer A His  (50 mM Tris/HCl, 500 mM NaCl, pH 7.8) containing 0.1 mg mL −1  DNAse I. The cell suspension was passed through a French pressure cell twice at a pressure of 137 MPa and centrifuged at 100 000×g and 4° C. for 1 h. The supernatant was filtered through a 0.45 μm syringe filter and loaded at a flow rate of 1 mL min −1  onto a 1 mL HisTrap™ FF column (GE healthcare) which had previously been equilibrated with 5 column volumes of buffer A His . The column was washed with 20 column volumes of 90% buffer A His  and 10% buffer B His  (50 mM Tris/HCl, 500 mM NaCl, 500 mM imidazole, pH 7.8) and the respective protein was eluted with buffer B His . The fraction containing the respective eluted enzyme was desalted using two 5 mL HiTrap™ Desalting columns (GE healthcare) and buffer A Strep . The respective purified enzymes were stored at −20° C. in buffer A Strep  containing 20% glycerol. 
     Activity Assays 
     PCT Re  Activity for Catalyzing the Conversion of Glycolate into Glycolyl-CoA (Reaction 2#) 
     The activity of the purified PCT Re  protein to catalyze the conversion of glycolate into glycolyl-CoA (reaction 2#) was determined via analysis of the time dependent formation of glycolyl-CoA in an in vitro assay using ultra-high performance liquid chromatography coupled high resolution mass spectrometry (UPLC-hrMS, see  FIG. 7 ). 
     Specifically, the enzyme assay was performed at 37° C. in a total volume of 60 μL. The reaction mixture contained 200 mM MOPS/KOH, 2 mM acetyl-CoA, 97 μg enzyme and 10 mM to 800 mM glycolate (pH 7.5). 10 μL aliquots were taken at time points 0.5, 1.0, 1.5 and 2.0 minutes and the reaction was immediately stopped by HCl (1% total concentration). The samples were centrifuged at 17 000×g and the supernatant diluted 1:20 for MS analysis. The measurements were done using an Agilent 6550 iFunnel Q-TOF LC-MS system equipped with an electrospray ionization source set to positive ionization mode. 
     Compounds were separated on a RP-18 column (50 mm×2.1 mm, particle size 1.7 μm, Kinetex XB-C18, Phenomenex) using a mobile phase system comprised of 50 mM ammonium formate pH 8.1 and methanol. Chromatographic separation was carried out using the following gradient condition at a flow rate of 250 μl/min: 0 min 0% methanol; 1 min 0% methanol, 3 min 2.5% methanol; 9 min 23% methanol; 14 min 80% methanol; 16 min 80% methanol. Capillary voltage was set at 3.5 kV and nitrogen gas was used for nebulizing (20 psig), drying (13 l/min, 225° C.) and sheath gas (12 l/min, 400° C.). The TOF was calibrated using an ESI-L Low Concentration Tuning Mix (Agilent) before measurement (residuals less than 2 ppm for five reference ions) and was recalibrated during a run using 922 m/z as reference mass. MS data were acquired with a scan range of 500-1200 m/z. 
     LC-MS data were analyzed using MassHunter Qualitative Analysis software (Agilent). The velocity of the particular reactions was calculated within the linear range of the reaction via the concentration of the formed glycolyl-CoA, that had been determined via LC-MS using a standard curve (25 μM to 100 μM glycolyl-CoA). 
     The K m  for glycolate for the CoA transferase from  R. eutropha  (PCT Re ) was determined to 51.7±9.6 mM and the v max  to 1.4±0.1 U mg −1  using nonlinear regression (R 2 : 0.91, GraphPad Prism 6,  FIG. 8B ). 
     PCT Ca  Activity for Catalyzing the Conversion of Glycolate to Glycolyl-CoA (Reaction 2#) 
     As an alternative enzyme for catalyzing the conversion of glycolate to glycolyl-CoA (reaction 2#), the propionyl-CoA transferase of  Clostridium propionicum  (PCT Cp ) was tested. The activity assay using this enzyme was performed as described above for PCT Re  with the only difference that instead of the PCT Re  enzyme the PCT Cp  enzyme was employed. The detected K m  value of the PCT Ca  enzyme for glycolate was 149±35 mM and the v max  amounted to 31.6±2.7 mU mg −1  (see  FIG. 9 ). 
     PCC Me  and PCC Me  D407I Y143H Activity for Catalyzing the Conversion of Glycolyl-CoA into Tartonyl-CoA (Reaction 3#) 
     Next the activities of the purified PCC Me  protein and the mutant variant PCC Me _D407I_Y143H for catalyzing the conversion of glycolyl-CoA into tartonyl-CoA (reaction 2#) was analyzed. The PCC Me _D407I_Y143H is a mutant variant of PCC Me , which has been designed and tested for its activity to convert glycolyl-CoA into tartonyl-CoA for the first time in the context of the present invention. The amino acid substitutions D407I and Y143H were manually selected as potential target sited for mutagenesis in order to improve the catalytical activity for the conversion of glycolyl-CoA into tartonyl-CoA (reaction 2#). The selection of these amino acids was merely speculative and only supported by comparing existing structures of biotin-dependent propinyl-CoA-carboxylases and biotin-dependent methylmalonyl-CoA-decarboxylases. Specifically, these structures were evaluated in respect to residues potentially involved in binding propionyl-CoA. 
     As shown in the extracted ion chromatogram for tartronyl-CoA shown in  FIG. 10 , the purified PCC Me _D407I_Y143H protein indeed exhibited a glycolyl-CoA carboxylation activity. Similarly, as mentioned below, also the wilde-type PCC Me  exhibited a glycolyl-CoA carboxylation activity, although the activity was lower as the activity of the PCC Me _D407I_Y143H protein. Thus, the introduced mutations surprisingly indeed improved the activity for converting glycolyl-CoA into tartonyl-CoA. 
     The activity of the PCC Me _D407I_Y143H protein as well as the PCC Me  protein was determined spectrophotometrically at 37° C. The ATP hydrolysis reaction of the respective enzyme was coupled to ATP regeneration by pyruvate kinase (PK) with phosphoenolpyruvate (PEP) and subsequent reduction to lactate by lactate dehydrogenase (LDH). The oxidation of NADH by LDH was followed spectrophotometrically at 340 nm. The reaction mixture (300 μL) contained 200 mM NH 4 HCO 3  buffer, pH 7.7, 5 mM MgCl 2 , 1 mM ATP, 1 mM PEP, 4 U PK, 5.8 U LDH, 0.3 mM NADH and 48 μg of PCC Me _D407I_Y143H or PCC Me . The reaction was initiated by addition of 1 mM glycolyl-CoA. Samples for UPLC-hrMS were withdrawn and stopped by acidification (5% formic acid) after most of the NADH was consumed. Precipitated protein was removed by centrifugation at 4° C. and 17 000×g. The supernatants were analyzed by UPLC-hrMS as described above. Glycolyl-CoA-dependent ATP-hydrolyis of the PCC Me  wilde-type enzyme was detected at 0.4 U mg −1  protein, whereas the PCC Me _D407I_Y143H enzyme showed a glycoyly-CoA-dependent ATP hydrolysis rate of 1.0 U mg −1  protein. As mentioned above, and shown in  FIG. 10 , the glycolyl-CoA carboxylation activity of the PCC Me _D407I_Y143H enzyme was confirmed by direct detection of the product tartronyl-CoA by UPLC-hrMS. 
     In a second assay, the reaction mixture was slightly modified for a  13 C labeling experiment. Here, the reaction mixture contained 50 mM NH 4 HCO 3  buffer, pH 7.7 and 150 mM [ 13 C]NaHCO 3 , pH 7.7 (otherwise as above-mentioned). The incorporation of the  13 C label into the carboxylation product tartronyl-CoA is depicted by a shift in the mass spectrum (see  FIG. 10C ). 
     A similar assay was used to determine the K m  value of the PCC Me _D407I_Y143H enzyme for the substrate glycolyl-CoA. The reaction mixture (300 μL) contained 200 mM NH 4 HCO 3  buffer, pH 7.7, 8.3 mM MgCl 2 , 1.7 mM ATP, 1.7 mM PEP, 4 U PK, 5.8 U LDH, 0.3 mM NADH and 24 μg of PCC Me _D407I_Y143H. The reaction was started by addition of varying amounts of glycolyl-CoA (0.125-3 mM). For the PCC Me _D407I_Y143H double mutant, the K m  for glycolyl-CoA was determined to be 1.0±0.15 mM with a v max  1.5±0.09 U mg −1  (see  FIG. 8C ). 
     MCR Ca  Activity for Catalyzing the Conversion of Tartonyl-CoA into Tartronate Semialdehyde (Reaction 4#) and the Subsequent Conversion of Tartronate Semialdehyde (Also Referred to as Tartronic Semialdehyde) into Glycerate (Reaction 5) 
     The kinetics of the MCR Ca  enzyme for enzymatically converting the substrate tartonyl-CoA into glycerate (via reactions 4# and 5 both catalyzed by MCR Ca ) were determined spectrophotometrically at 365 nm following the oxidation of NADPH. Per molecule tartronyl-CoA, two molecules of NADPH are oxidized by MCR Ca  (a first in reaction 4# and a second in reaction 5) The measurements were carried out at 37° C. in a total reaction volume of 200 μL containing 100 mM MOPS buffer (with 5 mM MgCl 2 , pH 7.5) with an initial NADPH concentration of 0.4 mM NADPH and 23 μg MCR Ca . 
     With its physiological substrate, malonyl-CoA, the enzyme exhibits a specific activity of approximately 7 U mg −1  at 37° C. (0.3 mM substrate, Kröger et al. 2011, loc. cit.). With tartronyl-CoA (0.25 mM), the specific activity at 37° C. was 0.6 U mg −1 . 
     The determined kinetic values for tartronyl-CoA are (n=3, nonlinear regression with GraphPad Prism 6): K m : 25.7±2.6 μM and v max : 635±14 mU/mg (R 2 : 0.96,  FIG. 8D ). The K m  value for tartronyl-CoA is comparable to the apparent K m  value for malonyl-CoA (30 μM, Hügler et al., 2002, Journal of Bacteriology, p. 2404-2410) and indicates in line with the usage of this enzyme in the present invention a high affinity for tartronyl-CoA. It is envisaged that the substrate specificity for tartronyl-CoA versus malonyl-CoA, can be further increased by enzyme engineering and evolution (as described elsewhere herein). 
     MCR E  Activity for Catalyzing the Conversion of Tartonyl-CoA into Tartronate Semialdehyde (Reaction 4#) and the Subsequent Conversion of Tartronate Semialdehyde into Glycerate (Reaction 5) 
     An alternative enzyme for catalyzing the conversion of tartonyl-CoA into glycerate (via reactions 4# and 5) is the MCR from  Erythrobacter  sp. NAP1 (MCR E ). It was tested for its activity with malonyl-CoA and for tartronyl-CoA with the assay described above for MCR Ca . The specific activity of MCR E  for tartronyl-CoA is 6 times lower than that of MCR Ca  (0.1 U mg −1  with 0.25 mM tartronyl-CoA, see  FIG. 12 ), but it also exhibits a 100 times lower specific activity for malonyl-CoA than MCR Ca  (0.1 U mg −1  with 0.25 mM malonyl-CoA). Thus, MCR E  exhibits lower rates of catalysis than MCR Ca , its substrate specificity is higher which could be advantageous for the in vivo application of the pathway. 
     Coupling of the Conversion of Glycolyl-CoA into Tartronyl-CoA (Reaction 3#) by PCC Me  D407I Y143H with the Conversions of Tartronyl-CoA into Tartronate Semialdehyde (Reaction 4#) and of Tartronate Semialdehyde into Glycerate (Reaction 5) by MCR Ca    
     In addition to the above mentioned assays also another assay was performed in which the formation of tartronyl-CoA from glycolyl-CoA (reaction 3#) by the PCC Me _D407I_Y143H enzyme was directly coupled to its subsequent two step reduction via tartronate-semialdehyde (reaction 4#) to glycerate (reaction 5) by use of the purified MCR Ca  (Kröger et al., 2011, loc. cit.). The reaction mixture (300 μL) contained 200 mM NH 4 HCO 3  buffer, pH 7.7, 5 mM MgCl 2 , 1 mM ATP, 0.4 mM NADPH, 43 μg PCC Me _D407I_Y143H, and 184 μg of MCR Ca . 
     To determine whether MCR Ca  was able to catalyze the two step reduction of tartonyl-CoA to glycerate (via tartronic semialdehyde), samples of the reaction mixture were withdrawn after all of the NADPH was consumed. The samples were stopped with formic acid (5% final concentration). The acidified samples were centrifuged at 4° C. and 17 000×g and the supernatants were analyzed by HPLC-hrMS. 
     The formation of glycerate was analyzed using an Agilent 6550 iFunnel Q-TOF LC-MS system equipped with an electrospray ionization source set to negative ionization mode. Compounds were separated on a Luna-NH2 column (100 mm×2.0 mm, particle size 3 μm, Phenomenex) using a mobile phase system comprised of 20 mM ammonium acetate, 20 mM NH 4 OH, 95:5 H 2 O/acetonitrile, pH 9.8 and acetonitrile. Chromatographic separation was carried out using the following gradient condition at a flow rate of 250 μl/min: 0 min 85% acetonitrile; 7 min 0% acetonitrile; 14 min 0% acetonitrile; 15 min 85% acetonitrile; 17.5 min 85% acetonitrile. Capillary voltage was set at 3.5 kV and nitrogen gas was used for nebulizing (20 psig), drying (13 l/min, 225° C.) and sheath gas (12 l/min, 400° C.). The TOF was calibrated using an ESI-L Low Concentration Tuning Mix (Agilent) before measurement (residuals less than 2 ppm for five reference ions) and was recalibrated during a run using 113 m/z as reference mass. MS data were acquired with a scan range of 50-200 m/z. 
     LC-MS data were analyzed using MassHunter Qualitative Analysis software (Agilent). MCR Ca  was indeed able to reduce the tartronyl-CoA, produced by PCC Me _D407I_Y143H, to glycerate (see  FIG. 11 ). This indirectly also confirmed that MCR Ca  reduced tartronyl-CoA to tatronate semialdehayde. To detect tatronate semialdehyde an HPLC-MS based assay can be employed that uses phenylhydrazine. In such assays the tartronate semialdehyde can be covalently derivatized with phenylhydrazine to a phenylhydrazone, which can be detected by its absorbance at 324 nm and confirmed by its corresponding mass spectrum. 
     The reaction mixture was slightly modified for an additional  13 C labeling assay. For that the mixture contained 50 mM NH 4 HCO 3  buffer, pH 7.7 and 150 mM [ 13 C]NaHCO 3 , pH 7.7. A shift in the mass spectrum after incubation in the presence of  13 C labeled bicarbonate ( FIG. 11C ) proves that the glycerate was formed from  13 C labeled tartronyl-CoA, resulting from the carboxylation of glycolyl-CoA. 
     Notably, the results with respect to the enzyme kinetics of the PCC Me _D407I_Y143H from the ATP hydrolysis assay for PCC Me _D407I_Y143H and the MCR Ca  coupled assay showed an ˜10 fold discrepancy in the calculated specific activities of PCC Me _D407I_Y143H, which was further investigated. 
     First, the option that this difference in the determined values resulted from an additional ATP hydrolysis during glycolyl-CoA carboxylation that is not directly related to the glycolyl-CoA carboxylation was assessed. The assay used for this analysis was performed in a reaction volume of 300 μL that contained 200 mM MOPS/KOH (pH 7.5), 1.6 mM MgCl 2 , 50 mM KHCO 3 , 0.33 mM ATP, 0.533 mM NADPH, 24 μg PCC Me _D407I_Y143H, 138 μg MCR Ca , 16 μg epimerase. The assay was started by the addition of 2 mM glycolyl-CoA. The amount of formed tartronyl-CoA was calculated based on the absorption difference of NADPH from start to end of the reaction. From 333 μM ATP applied to the reaction, 46 μM were used for actual carboxylation. This implies, that only 14% of the ATP hydrolysis lead to tartronyl-CoA formation, which would in turn explain the difference in the determined values. However, anyhow irrespective of the exact values of the enzyme kinetics it is clear from both experiments that PCC Me _D407I_Y143H has glycolyl-CoA carboxylation activity and can convert glycolyl-CoA tartonyl-CoA. 
     The activity of the wildtype PCC Me  with glycolyl-CoA, measured with ATP hydrolysis assay was 0.4 U mg −1 , whereas with the MCR Ca  coupled assay, no activity could be measured. However, given the results of the PCC Me _D407I_Y143H, the failure to detect activity of the wildtype PCC Me  with glycolyl-CoA in the MCR Ca  coupled assay probably results from the fact that the activity is below the detection limit of this assay. Thus, the PCC Me _D407I_Y143H was indeed much more efficient in glycolyl-CoA carboxylation than the wild type enzyme. It may be advantageous to construct mutant variants of PCC Me _D407I_Y143H (by enzyme evolution) which reduces the amount of hydrolyzed ATP independent of glycolyl-CoA conversion. Such efforts could focus on increasing interaction of the enzyme with the hydroxy group of glycolyl-CoA. 
     Summary of Activity Assays 
     In summary, the above mention activity assays illustrated that the respective reactions of the proposed pathway can be performed by the enzymes used and disclosed herein. In particular,  FIG. 11  shows that the in vitro conversion of glycolyl-CoA to glycerate by the combined function of PCC Me _D407I_Y143H and MCR Ca  is possible and that the formed glycerate is  13 C labeled if the reaction is performed in the presence of  13 C labeled bicarbonate. 
       FIG. 8  gives an overview of the investigated enzymes and their Michaelis-Menten kinetics. The enzymes and their corresponding kinetic values are listed in Table 5. 
     The present invention refers to the following tables: 
                     TABLE 1                  Estimated efficiency advantages of the synthetic photorespiration bypass       routes shown in FIG. 1 over the natural photorespiration pathway.                         Requirements for the production of 1 triose           phosphate via the CBBC                                 cycles/                   iterations       NAD(P)H           of the CBBC   ATP molecules   molecules                                                 relative       relative       relative       Pathway   #   efficiency   #   efficiency   #   efficiency                                                 Native   4.8   100%   15.6   100%   9.6   100%       FIG. 1A   3   160%   11.3-12 †     130-138%   7.5   128%       FIG. 1B   4   120%   12-13 †     120-130%   8   120%       FIG. 1C   4   120%   12.5-13.5 †     116-125%   8   120%       FIG. 1D   3   160%   10.5   149%   7.5 ††     128%                 † formation of glycolyl-CoA can consume either one or two ATP equivalents         †† assuming that glycolate oxidation is NAD(P)-dependent       #: signifies numbers of iterations/cycles of the CBBC or molecules consumed, respectively            
Table 2 and Table 3.
 
     Table 2 and Table 3 summarize all reactions as shown in the  FIGS. 1 to 4 . In particular, Table 2 lists the non-native reactions/enzymes/enzymatic conversions and Table 3 lists all other reactions/enzymes/enzymatic conversions The first column of these Tables indicate the number of the reactions/enzymatic conversions/enzymes as shown in the Figures. In particular, the individual enzymatic reactions/enzymatic conversions are depicted with numbers in the Figures (e.g. the enzymatic conversion of 2-PG (2-phosphoglycolate, also known as glycolate 2-phosphate) into glycolate is depicted as “1”). In the context of this application, this number “X” is depicted as “reaction X” or “enzymatic conversion X”, where it refers to the enzymatic conversion. Moreover, this number “X” is depicted as “enzyme X”, where it refers to the respective enzyme catalysing the respective reaction. 
     In Tables 2 and 3, possible cofactors are indicated in brackets. 
     
       
         
           
               
               
               
               
               
               
               
               
               
             
               
                 TABLE 2 
               
               
                   
               
               
                 Reac- 
                   
                   
                   
                   
                   
                   
                   
                   
               
               
                 tion/ 
                 EC no. of 
                   
                   
                   
                   
                   
                 Enzymatic activity 
                   
               
               
                 En 
                 enzyme to 
                   
                   
                   
                   
                   
                 within the 
               
               
                 zyme 
                 be 
                 Enzyme to be 
                 Examples for 
                 Natural plant 
                   
                   
                 photorespiration 
               
               
                 no. 
                 employed 
                 employed 
                 organisms 
                 localization 
                 Substrate(s) 
                 Product(s) 
                 bypass pathways 
                 Ref. 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
               
               
               
               
               
               
            
               
                 1 
                 3.1.3.18 
                 phosphoglycolate 
                 ubiquitous 
                 chloroplast 
                 2-PG, H 2 O 
                 glycolate, 
                 phosphoglycolate 
                  [1] 
               
               
                   
                   
                 phosphatase 
                   
                   
                   
                 phosphate 
                 phosphatase 
               
               
                 5 
                 1.1.1.60 
                 tartronate- 
                 
                   Escherichia coli 
                 
                   
                 tartronate- 
                 glycerate 
                 tartronate- 
                  [2] 
               
               
                   
                   
                 semialdehyde 
                   
                   
                 semialdehyde 
                 (NAD(P)) 
                 semialdehyde 
               
               
                   
                   
                 reductase 
                   
                   
                 (NAD(P)H) 
                   
                 reductase 
               
               
                 6 
                 2.7.1.31 
                 glycerate kinase 
                 ubiquitous 
                 chloroplast 
                 D-glycerate (ATP) 
                 D-glycerate 
                 glycerate kinase 
                  [3] 
               
               
                   
                   
                   
                   
                   
                   
                 (ADP) 
               
               
                 8 
                 4.1.2.17 
                 L-fuculose- 
                 
                   Escherichia coli 
                 
                   
                 dihydroxyacetone 
                 D-ribulose 1- 
                 D-ribulose 1- 
                  [4] 
               
               
                   
                   
                 phosphate 
                   
                   
                 phosphate, 
                 phosphate 
                 phosphate 
               
               
                   
                   
                 aldolase 
                   
                   
                 glycolaldehyde 
                   
                 aldolase 
               
               
                 12 
                 1.1.1.26 
                 glyoxylate 
                 
                   Arabidopsis 
                 
                 chloroplast 
                 glycolate (NAD(P)) 
                 glyoxylate 
                 glycolate 
                  [5] 
               
               
                   
                   
                 reductase 
                 
                   thaliana 
                 
                   
                   
                 (NAD(P)H) 
                 dehydrogenase 
               
               
                 13 
                 2.6.1.45 
                 serine-glyoxylate 
                 
                   Arabidopsis 
                 
                 peroxisome 
                 L-serine, glyoxylate 
                 Hydroxypyruvate, 
                 serine-glyoxylate 
                  [6] 
               
               
                   
                   
                 transaminase 
                 
                   thaliana 
                 
                   
                   
                 glycine 
                 transaminase 
               
               
                 14 
                 2.1.2.1 
                 serine hydroxyl- 
                 ubiquitous 
                 mitochondria 
                 methylene-THF, 
                 L-serine 
                 serine 
                  [7] 
               
               
                   
                   
                 methyltransferase 
                   
                   
                 glycine 
                   
                 hydroxymethyl- 
               
               
                   
                   
                   
                   
                   
                   
                   
                 transferase 
               
               
                 16 
                 6.3.4.3 
                 formate 
                 ubiquitous 
                 chloroplast 
                 formate, THF 
                 formyl-THF (ADP, 
                 formate 
                  [8] 
               
               
                   
                   
                 tetrahydrofolate 
                   
                   
                 (ATP) 
                 phosphate) 
                 tetrahydrofolate 
               
               
                   
                   
                 ligase 
                   
                   
                   
                   
                 ligase 
               
               
                 17 
                 3.5.4.9 + 
                 methylene- 
                 ubiquitous 
                 chloroplast 
                 formyl-THF 
                 methylene-THF, 
                 methylene- 
                  [8] 
               
               
                   
                 1.5.1.5 
                 tetrahydrofolate 
                   
                   
                 (NAD(P)H) 
                 H 2 O (NAD(P)) 
                 tetrahydrofolate 
               
               
                   
                   
                 dehydrogenase &amp; 
                   
                   
                   
                   
                 dehydrogenase &amp; 
               
               
                   
                   
                 cyclohydrolase 
                   
                   
                   
                   
                 cyclohydrolase 
               
               
                 18 
                 1.1.1.81 
                 hydroxypyruvate 
                 ubiquitous 
                 peroxisome 
                 hydroxypyruvate 
                 glycerate 
                 hydroxypyruvate 
                  [9] 
               
               
                   
                   
                 reductase 
                   
                   
                 (NAD(P)H) 
                 (NAD(P)) 
                 reductase 
               
               
                 25 
                 5.3.1.22 
                 hydroxypyruvate 
                 
                   Escherichia coli 
                 
                   
                 hydroxypyruvate 
                 tartronate- 
                 hydroxypyruvate 
                 [10] 
               
               
                   
                   
                 isomerase 
                   
                   
                   
                 semialdehyde 
                 isomerase 
               
               
                 30 
                 5.4.2.7 
                 phosphopento- 
                 
                   Escherichia coli 
                 
                   
                 D-ribose 1- 
                 D-ribose 5- 
                 D-ribose 1- 
                 [11] 
               
               
                   
                   
                 mutase 
                   
                   
                 phosphate 
                 phosphate 
                 phosphate 
               
               
                   
                   
                   
                   
                   
                   
                   
                 mutase 
               
               
                 31 
                 2.7.1.X 
                 ADP-dependent 
                 
                   Thermococcus 
                 
                   
                 D-ribose 1- 
                 D-ribose 1,5- 
                 ADP-dependent 
                 [12] 
               
               
                   
                   
                 #ribose-1- 
                 
                   kodakarensis 
                 
                   
                 phosphate 
                 bisphosphate 
                 ribose-1- 
               
               
                   
                   
                 phosphate kinase 
                   
                   
                 (ATP) 
                 (ADP) 
                 phosphate kinase 
               
               
                 32 
                 5.3.1.X 
                 ribose-1,5- 
                 
                   Thermococcus 
                 
                   
                 D-ribose 1,5- 
                 D-ribulose 1,5- 
                 ribose-1,5- 
                 [12] 
               
               
                   
                   
                 bisphosphate 
                 
                   kodakarensis 
                 
                   
                 bisphosphate 
                 bisphosphate 
                 bisphosphate 
               
               
                   
                   
                 isomerase 
                   
                   
                   
                   
                 isomerase 
               
               
                 38 
                 2.7.1.2 
                 glucokinase 
                 ubiquitous 
                 cytosol 
                 D-glucose (ATP) 
                 D-glucose 6- 
                 D-glucose 6- 
                 [13] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate (ADP) 
                 kinase 
               
               
                 39 
                 5.3.1.9 
                 glucose-6- 
                 ubiquitous 
                 cytosol 
                 D-glucose 6- 
                 D-fructose 6- 
                 glucose-6- 
                 [14] 
               
               
                   
                   
                 phosphate 
                   
                   
                 phosphate 
                 phosphate 
                 phosphate 
               
               
                   
                   
                 isomerase 
                   
                   
                   
                   
                 isomerase 
               
               
                 46 
                 2.7.1.4 
                 fructokinase 
                 ubiquitous 
                 cytosol 
                 D-fructose (ATP) 
                 D-fructose 6- 
                 D-fructose 6- 
                 [15] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate (ADP) 
                 kinase 
               
               
                 48 
                 1.1.99.14 
                 glycolate oxidase 
                 ubiquitous 
                 peroxisome 
                 glycolate, O 2   
                 glyoxylate, H 2 O 2   
                 glycolate oxidase 
                 [16] 
               
               
                 49 
                 1.4.1.10 
                 glycine 
                 
                   Myco- 
                 
                   
                 glyoxylate, NH 3 , 
                 glycine, H 2 O, 
                 glycine 
                 [17] 
               
               
                   
                   
                 dehydrogenase 
                   bacterium  sp. 
                   
                 (NAD(P)H) 
                 (NAD(P)) 
                 dehydrogenase 
               
               
                 50 
                 4.3.1.17 
                 L-serine 
                 
                   Escherichia coli 
                 
                   
                 L-serine 
                 pyruvate, NH 3   
                 L-serine 
                 [18] 
               
               
                   
                   
                 ammonia-lyase 
                   
                   
                   
                   
                 ammonia-lyase 
               
               
                 51 
                 2.7.9.2 
                 pyruvate, water 
                 
                   Escherichia coli 
                 
                   
                 pyruvate, H 2 O 
                 PEP, phosphate, 
                 PEP synthetase 
                 [19] 
               
               
                   
                   
                 dikinase 
                   
                   
                 (ATP) 
                 (AMP) 
               
               
                 52 
                 4.2.1.11 
                 enolase 
                 ubiquitous 
                 plastid 
                 PEP, H 2 O 
                 D-glycerate 2- 
                 PEP hydratase 
                 [20] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate 
               
               
                 53 
                 5.4.2.12 
                 phosphoglycerate 
                 ubiquitous 
                   
                 D-glycerate 2- 
                 D-glycerate 3- 
                 phosphoglycerate 
                 [21] 
               
               
                   
                   
                 mutase 
                   
                   
                 phosphate 
                 phosphate 
                 mutase 
               
               
                 61 
                 1.1.1.X 
                 D-gluconate 5- 
                 
                   Gluconobacter 
                 
                   
                 D-gluconate 
                 5-keto D- 
                 D-gluconate 5- 
                 [22] 
               
               
                   
                   
                 dehydrogenase 
                   oxydans  621H 
                   
                   
                 gluconate 
                 dehydrogenase 
               
               
                 69 
                 2.7.1.17 
                 D-xylulokinase 
                 
                   Escherichia coli 
                 
                   
                 D-xylulose (ATP) 
                 D-xylulose 5- 
                 xylulokinase 
                 [100]  
               
               
                   
                   
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 80 
                 5.3.1.13 
                 D-arabinose 5- 
                 ubiquitous 
                 cytosol 
                 D-arabinose 5- 
                 D-ribulose 5- 
                 Arabinose 5- 
                 [23, 24] 
               
               
                   
                   
                 phosphate 
                   
                   
                 phosphate 
                 phosphate 
                 phosphate 
               
               
                   
                   
                 isomerase 
                   
                   
                   
                   
                 isomerase 
               
               
                 81 
                 2.7.1.54 
                 D-arabinokinase 
                 
                   Propionibacterium 
                 
                   
                 D-arabinose 
                 D-arabinose 5- 
                 D-arabinokinase 
                 [25] 
               
               
                   
                   
                   
                 
                   acidipropionici 
                 
                   
                   
                 phosphate 
               
               
                 82 
                 5.3.1.3 
                 D-arabinose 
                 
                   Aeribacillus 
                 
                   
                 D-arabinose 
                 D-ribulose 
                 arabinose 
                 [26] 
               
               
                   
                   
                 isomerase 
                 
                   pallidus 
                 
                   
                   
                   
                 isomerase 
               
               
                 83 
                 2.7.1.47 
                 D-ribulokinase 
                 
                   Escherichia coli 
                 
                   
                 D-ribulose 
                 D-ribulose 5- 
                 D-ribulokinase 
                 [27] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate 
               
               
                 94 
                 2.7.1.4 
                 D-fructokinase 
                 ubiquitous 
                 chloroplast 
                 D-fructose (ATP) 
                 D-fructose 6- 
                 6-fructokinase 
                 [28] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 95 
                 2.7.1.3 
                 ketohexokinase 
                 
                   Homo sapiens 
                 
                   
                 D-fructose (ATP) 
                 D-fructose 1- 
                 1-fructokinase 
                 [29] 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 96 
                 2.7.1.56 
                 1- 
                 
                   Escherichia coli 
                 
                   
                 D-fructose 1- 
                 D-fructose 1,6- 
                 1- 
                 [30] 
               
               
                   
                   
                 phosphofructokinase 
                   
                   
                 phosphate (ATP) 
                 bisphosphate 
                 phosphofructokinase 
               
               
                   
                   
                   
                   
                   
                   
                 (ADP) 
               
               
                 108 
                 2.7.1.14 
                 D- 
                 
                   Mus musculus 
                 
                   
                 D-sedoheptulose 
                 D-sedoheptulose 
                 D- 
                 [31] 
               
               
                   
                   
                 sedoheptulokinase 
                   
                   
                 (ATP) 
                 7-phosphate 
                 sedoheptulokinase 
               
               
                   
                   
                   
                   
                   
                   
                 (ADP) 
               
               
                 Z10 
                 1.1.1.177 
                 glycerol-3- 
                 
                   Archaeoglobus 
                 
                   
                 D-glyceraldehyde 
                 glycerol-1- 
                 glycerol-3- 
                 [32] 
               
               
                   
                   
                 phosphate 1- 
                 
                   fulgidus 
                 
                   
                 3-phosphate 
                 phosphate 
                 phosphate 1- 
               
               
                   
                   
                 dehydrogenase 
                   
                   
                   
                   
                 dehydrogenase 
               
               
                 Z11 
                 5.3.1.1 
                 triose-phosphate 
                 ubiquitous 
                 chloroplast 
                 D-glyceraldehyde 
                 dihydroxyacetone 
                 triose-phosphate 
                 [33] 
               
               
                   
                   
                 isomerase 
                   
                   
                 3-phosphate 
                 phosphate 
                 isomerase 
               
               
                 Z12 
                 1.1.1.8/94 
                 glycerol-3- 
                 ubiquitous 
                 cytosol 
                 dihydroxyacetone 
                 glycerol-1- 
                 glycerol-3- 
                 [34] 
               
               
                   
                   
                 phosphate 
                   
                   
                 phosphate 
                 phosphate 
                 phosphate 2- 
               
               
                   
                   
                 dehydrogenase 
                   
                   
                   
                   
                 dehydrogenase 
               
               
                 Z13 
                 3.1.3.21 
                 glycerol-1- 
                 ubiquitous 
                 cytosol 
                 glycerol-1- 
                 glycerol, 
                 glycerol-1- 
                 [35] 
               
               
                   
                   
                 phosphatase 
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z14 
                 1.1.1.6/ 
                 glycerol 
                 
                   Escherichia coli 
                 
                   
                 glycerol 
                 dihydroxyacetone 
                 glycerol 2- 
                 [36] 
               
               
                   
                 156 
                 dehydrogenase 
                   
                   
                   
                   
                 dehydrogenase 
               
               
                 Z15 
                 1.1.1.21/ 
                 glycerol 
                 rabbit muscle 
                   
                 glycerol 
                 D-glyceraldehyde 
                 glycerol 3- 
                 [36] 
               
               
                   
                 72 
                 dehydrogenase 
                   
                   
                   
                   
                 dehydrogenase 
               
               
                 Z19 
                 4.1.2.13 
                 fructose- 
                 ubiquitous 
                 chloroplast 
                 D-sedoheptulose 
                 D-erythrose 4- 
                 sedoheptulose- 
                 [37] 
               
               
                   
                   
                 bisphosphate 
                   
                   
                 1,7-bisphosphate 
                 phosphate, 
                 bisphosphate 
               
               
                   
                   
                 aldolase 
                   
                   
                   
                 dihydroxyacetone 
                 aldolase 
               
               
                   
                   
                   
                   
                   
                   
                 phosphate 
               
               
                 Z20 
                 3.1.3.37 
                 D-sedoheptulose 
                 ubiquitous 
                 chloroplast 
                 D-sedoheptulose 
                 D-sedoheptulose 
                 D-sedoheptulose 
                 [38] 
               
               
                   
                   
                 1,7- 
                   
                   
                 1,7-bisphosphate 
                 7-phosphate, 
                 1,7-bisphosphate 
               
               
                   
                   
                 bisphosphatase 
                   
                   
                   
                 phosphate 
                 1-phosphatase 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
               
               
               
               
               
               
             
               
                 TABLE 3 
               
               
                   
               
               
                 Reaction/ 
                 EC no. of 
                   
                   
                   
                 Enzymatic activity within the 
                   
               
               
                 Enzyme 
                 enzyme to 
                   
                   
                   
                 photorespiration bypass 
               
               
                 no. 
                 be employed 
                 Enzyme to be employed 
                 Substrate(s) 
                 Product(s) 
                 pathways 
                 Ref. 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
               
               
               
               
            
               
                 2# 
                 6.2.1.17 
                 propionate-CoA ligase 
                 glycolate, CoA (ATP)) 
                 glycolyl-CoA (AMP, 
                 glycolate-CoA ligase 
                 [39] 
               
               
                   
                   
                   
                   
                 PP i ) 
               
               
                 3# 
                 6.4.1.3 
                 propionyl-CoA carboxylase or 
                 glycolyl-CoA, CO 2  in 
                 tartronyl-CoA (ADP, 
                 glycolyl-CoA carboxylase 
                 [40] 
               
               
                   
                   
                 acyl-CoA carboxylase 
                 form of bicarbonate 
                 phosphate) 
               
               
                   
                   
                   
                 (ATP) 
               
               
                 4# 
                 1.2.1.75 
                 malonyl-CoA reductase 
                 tartronyl-CoA 
                 tartronate 
                 tartronyl-CoA reductase 
                 [41] 
               
               
                   
                   
                   
                 (NAD(P)H) 
                 semialdehyde 
               
               
                   
                   
                   
                   
                 (NAD(P)) 
               
               
                 7# 
                 1.2.1.10 
                 acetaldehyde dehydrogenase 
                 glycolyl-CoA 
                 glycolaldehyde, CoA 
                 glycolaldehyde 
                 [42, 
               
               
                   
                   
                 (acylating) 
                 (NAD(P)H) 
                 (NAD(P)) 
                 dehydrogenase (acylating) 
                 43] 
               
               
                 9# 
                 2.7.1.56/ 
                 1-phosphofructokinase or 
                 D-ribulose 1- 
                 D-ribulose 1,5- 
                 1-phosphoribulokinase 
                 [30, 
               
               
                   
                 2.7.1.16 
                 ribulokinase 
                 phosphate 
                 bisphosphate (ADP) 
                   
                 44] 
               
               
                   
                   
                   
                 (ATP) 
               
               
                 10# 
                 4.1.2.X 
                 various aldolases (e.g., 
                 2 glycolaldehyde 
                 D-erythrose 
                 D-erythrose aldolase 
                 [45] 
               
               
                   
                   
                 fructose 6-phosphate 
               
               
                   
                   
                 aldolase and/or xylulose 1- 
               
               
                   
                   
                 phosphate aldolase) 
               
               
                 11# 
                 2.7.1.29 
                 dihydroxyacetone kinase 
                 D-erythrose (ATP) 
                 D-erythrose 4- 
                 D-erythrose kinase 
                 [46] 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 15# 
                 1.1.99.33 
                 formate dehydrogenase 
                 CO 2  (NAD(P)H) 
                 formate (NAD(P)) 
                 carbon dioxide reductase 
                 [47] 
               
               
                 19# 
                 2.7.2.1 
                 acetate kinase 
                 glycolate (ATP) 
                 glycolyl-phosphate 
                 glycolate 1-kinase 
                 [48] 
               
               
                   
                   
                   
                   
                 (ADP) 
               
               
                 20# 
                 1.2.1.12 
                 phosphorylating 
                 glycolyl-phosphate 
                 glycolaldehyde, 
                 glycolaldehyde 
                 [49-51] 
               
               
                   
                   
                 glyceraldehyde 3-phosphate 
                 (NAD(P)H) 
                 phosphate (NAD(P)) 
                 dehydrogenase 
               
               
                   
                   
                 dehydrogenase 
                   
                   
                 (phosphorylating) 
               
               
                 21# 
                 2.3.1.8 
                 phosphate acetyltransferase 
                 glycolyl-phosphate, 
                 glycolyl-CoA, 
                 phosphate 
                 [52] 
               
               
                   
                   
                   
                 CoA 
                 phosphate 
                 glycolyltransferase 
               
               
                 22# 
                 1.2.1.X 
                 ATP- and NAD(P)H- 
                 glycolate (ATP, 
                 glycolaldehyde (AMP, 
                 glycolate reductase 
                 [53] 
               
               
                   
                   
                 dependent carboxylic acid 
                 NAD(P)H) 
                 PPi, NAD(P)) 
               
               
                   
                   
                 reductase 
               
               
                 23# 
                 2.7.2.3 
                 3-phosphoglycerate kinase 
                 2-PG (ATP) 
                 glycolate 1,2- 
                 phosphoglycolate kinase 
                 [54-56] 
               
               
                   
                   
                   
                   
                 bisphosphate (ADP) 
               
               
                 24# 
                 1.2.1.12 
                 phosphorylating 
                 glycolate 1,2- 
                 glycolaldehyde 2- 
                 phosphoglycolaldehyde 
                 [49-51] 
               
               
                   
                   
                 glyceraldehyde 3-phosphate 
                 bisphosphate 
                 phosphate, phosphate 
                 dehydrogenase 
               
               
                   
                   
                 dehydrogenase 
                 (NAD(P)H) 
                 (NAD(P)) 
                 (phosphorylating) 
               
               
                 26# 
                 6.4.1.1 
                 pyruvate carboxylase 
                 glycolaldehyde, CO 2   
                 tartronate 
                 glycolaldehyde carboxylase 
                 [57] 
               
               
                   
                   
                   
                 in form of bicarbonate 
                 semialdehyde (ADP, 
               
               
                   
                   
                   
                 (ATP) 
                 phosphate) 
               
               
                 27# 
                 1.1.1.39 
                 malate dehydrogenase 
                 glycolaldehyde, CO 2   
                 glycerate (NADP) 
                 glycerate dehydrogenase 
                 [58] 
               
               
                   
                   
                 (decarboxylating) 
                 (NAD(P)H) 
                   
                 (decarboxylating) 
               
               
                 28# 
                 4.1.2.17 
                 L-fuculose-phosphate 
                 glycolaldehyde 2- 
                 D-ribulose 1,5- 
                 D-ribuolse bisphosphate 
                 [4, 59] 
               
               
                   
                   
                 aldolase 
                 phosphate, 
                 bisphosphate 
                 aldolase 
               
               
                   
                   
                   
                 dihydroxyacetone 
               
               
                   
                   
                   
                 phosphate 
               
               
                 29# 
                 — 
                 5-methylthio-D-ribulose 1- 
                 D-ribulose 1- 
                 D-ribose 1-phosphate 
                 D-ribulose 1-phosphate 1,2- 
                 [60] 
               
               
                   
                   
                 phosphate 1,2-isomerase 
                 phosphate 
                   
                 isomerase 
               
               
                 33# 
                 — 
                 5-methylthio-D-ribulose 1- 
                 D-ribulose 1- 
                 D-xylulose 5- 
                 D-ribulose 1-phosphate 1,3- 
                 [61, 
               
               
                   
                   
                 phosphate 1,3-isomerase 
                 phosphate 
                 phosphate 
                 isomerase 
                 62] 
               
               
                 34# 
                 4.1.2.X 
                 various aldolases 
                 glycolaldehyde, D- 
                 D-ribose 
                 D-ribose 5-phosphate 
                 [63] 
               
               
                   
                   
                   
                 glyceraldehyde 
                 5-phosphate 
                 aldolase 
               
               
                   
                   
                   
                 3-phosphate 
               
               
                 35# 
                 4.1.2.X 
                 various aldolases 
                 glycolaldehyde, 
                 D-erythrose 
                 D-erythrose 4-phosphate 
                 [45] 
               
               
                   
                   
                   
                 glycolaldehyde 
                 4-phosphate 
                 aldolase 
               
               
                   
                   
                   
                 2-phosphate 
               
               
                 36# 
                 4.1.2.X 
                 various aldolases 
                 D-erythrose, 
                 D-glucose 
                 D-glucose aldolase 
                 [45] 
               
               
                   
                   
                   
                 glycolaldehyde 
               
               
                 37# 
                 4.1.2.X 
                 various aldolases 
                 D-erythrose 
                 D-glucose 
                 D-glucose 6-phosphate 
                 [45] 
               
               
                   
                   
                   
                 4-phosphate, D- 
                 6-phosphate 
                 aldolase 
               
               
                   
                   
                   
                 erythrose 
               
               
                   
                   
                   
                 4-phosphate 
               
               
                 40# 
                 4.1.1.X 
                 transketolase, pyruvate 
                 2 glycolaldehyde 
                 D-erythrulose 
                 D-erythrulose synthetase 
                 [64-66] 
               
               
                   
                   
                 decarboxylase or other 
               
               
                   
                   
                 thiamine dependent enzymes 
               
               
                 41# 
                 5.3.1.X 
                 Various sugar isomerases; 
                 D-erythrulose 
                 D-erythrose 
                 D-erythrose isomerase 
                 [67] 
               
               
                   
                   
                 e.g. glucose isomerase 
               
               
                 42# 
                 2.7.1.X 
                 Various sugar kinases 
                 D-erythrulose 
                 D-erythrulose 4- 
                 D-erythrulose kinase 
                 [68] 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 43# 
                 4.1.1.X 
                 pyruvate decartboxylase and 
                 glycolaldehyde 2- 
                 D-erythrulose 4- 
                 D-erythrulose 4-phosphate 
                 [64-66] 
               
               
                   
                   
                 other thiamine dependent 
                 phosphate, 
                 phosphate 
                 synthetase 
               
               
                   
                   
                 enzymes 
                 glycolaldehyde 
               
               
                 44# 
                 5.3.1.X 
                 Various sugar isomerases 
                 D-erythrulose 4- 
                 D-erythrose 4- 
                 D-erythrose 4-phosphate 
                 [69] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 isomerase 
               
               
                 45# 
                 4.1.1.X 
                 transketolase, pyruvate 
                 D-erythrose, 
                 D-fructose 
                 D-fructose synthetase 
                 [64-66] 
               
               
                   
                   
                 decarboxylase or other 
                 glycolaldehyde 
               
               
                   
                   
                 thiamine dependent enzymes 
               
               
                 47# 
                 4.1.1.X 
                 transketolase, pyruvate 
                 D-erythrose 4- 
                 D-fructose 
                 D-fructose 6-phosphate 
                 [64-66] 
               
               
                   
                   
                 decarboxylase or other 
                 phosphate, 
                 6-phosphate 
                 synthetase 
               
               
                   
                   
                 thiamine dependent enzymes 
                 glycolaldehyde 
               
               
                 54# 
                 2.3.1.54 
                 pyruvate formate lyase 
                 glycolyl-CoA, formate 
                 hydroxypyruvate 
                 hydroxypyruvate formate 
                 [70, 
               
               
                   
                   
                   
                   
                   
                 lyase 
                 71] 
               
               
                 55# 
                 1.2.7.1 
                 pyruvate synthase 
                 glycolyl-CoA, CO 2  (2 
                 Hydroxypyruvate (2 
                 hydroxypyruvate synthase 
                 [72] 
               
               
                   
                   
                   
                 reduced ferredoxin) 
                 oxidized ferredoxin) 
               
               
                 56# 
                 2.3.1.9 
                 acetyl-CoA C- 
                 2 glycolyl-CoA 
                 2,4-dihydroxy-3-oxo 
                 glycolyl-CoA C- 
                 [73] 
               
               
                   
                   
                 acetyltransferase 
                   
                 butyryl-CoA 
                 glycolyltransferase 
               
               
                 57# 
                 1.1.1.X 
                 various secondary-alcohol 
                 2,4-dihydroxy-3-oxo 
                 2,3,4-trihydroxy 
                 2,3,4-trihydroxybutyryl-CoA 
                 [74] 
               
               
                   
                   
                 dehydrogenases 
                 butyryl-CoA 
                 butyryl-CoA 
                 dehydrogenase 
               
               
                 58# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4-trihydroxy 
                 D-erythrose 
                 D-erythrose dehydrogenase 
                 [42, 
               
               
                   
                   
                 dehydrogenases (acylating) 
                 butyryl-CoA 
                   
                   
                 43] 
               
               
                 59# 
                 4.1.2.X 
                 various aldolases 
                 glycolyl-CoA, D- 
                 gluconyl-CoA 
                 gluconyl-CoA aldolase 
                 [45] 
               
               
                   
                   
                   
                 erythrose 
               
               
                   
                   
                   
                 4-phosphate 
               
               
                 60# 
                 3.1.2.X 
                 various acyl-CoA hydrolases 
                 gluconyl-CoA 
                 Gluconate, CoA 
                 gluconyl-CoA hydrolase 
                 [75] 
               
               
                 62# 
                 4.1.2.X 
                 various aldolases 
                 Gluconate (NAD(P)) 
                 5-dehydrogluconate, 
                 5-dehydro-gluconate 
                 [45] 
               
               
                   
                   
                   
                   
                 (NAD(P)H) 
                 aldolase 
               
               
                 63# 
                 1.1.1.X 
                 various secondary-alcohol 
                 gluconyl-CoA 
                 5-dehydro gluconyl- 
                 gluconyl-CoA 5- 
                 [74] 
               
               
                   
                   
                 and sugar dehydrogenases 
                 (NAD(P)) 
                 CoA (NAD(P)H) 
                 dehydrogenase 
               
               
                 64# 
                 3.1.2.X 
                 various acyl-CoA hydrolases 
                 5-dehydro gluconyl- 
                 5-dehydrogluconate, 
                 5-dehydro-gluconyl-CoA 
                 [75] 
               
               
                   
                   
                   
                 CoA 
                 CoA 
                 hydrolase 
               
               
                 65# 
                 2.3.1.9 
                 acetyl-CoA C- 
                 2,4-dihydroxy-3-oxo 
                 2,4,6-trihydroxy-3,5- 
                 2,4-dihydroxy-3-oxo butyryl- 
                 [73] 
               
               
                   
                   
                 acetyltransferase 
                 butyryl-CoA, glycolyl- 
                 oxo hexanoyl-CoA 
                 CoA C-glycolyltransferase 
               
               
                   
                   
                   
                 CoA 
               
               
                 66# 
                 1.1.1.X 
                 various secondary-alcohol 
                 2,4,6-trihydroxy-3,5- 
                 5-dehydro 
                 5-dehydro gluconyl-CoA 
                 [74] 
               
               
                   
                   
                 and sugar dehydrogenases 
                 oxo hexanoyl-CoA 
                 gluconyl-CoA, (NADP) 
                 dehydrogenase 
               
               
                   
                   
                   
                 (NAD(P)H) 
               
               
                 67# 
                 2.2.1.2 
                 transaldolase 
                 glycolaldehyde, D- 
                 D-xylulose, D- 
                 transaldolase with 
                 [76] 
               
               
                   
                   
                   
                 fructose 6-phosphate 
                 glyceraldehyde 3- 
                 glycolaldehyde (acceptor) 
               
               
                   
                   
                   
                   
                 phosphate 
                 and D-fructose 6-phosphate 
               
               
                   
                   
                   
                   
                   
                 (donor) 
               
               
                 68# 
                 2.2.1.2 
                 transaldolase 
                 glycolaldehyde 
                 D-xylulose 5- 
                 transaldolase with 
                 [76] 
               
               
                   
                   
                   
                 phosphate, D-fructose 
                 phosphate, D- 
                 glycolaldehyde phosphate 
               
               
                   
                   
                   
                 6-phosphate 
                 glyceraldehyde 3- 
                 (acceptor) and D-fructose 6- 
               
               
                   
                   
                   
                   
                 phosphate 
                 phosphate (donor) 
               
               
                 70# 
                 2.2.1.2 
                 transaldolase 
                 glycolaldehyde, D- 
                 D-xylulose, D- 
                 transaldolase with 
                 [76] 
               
               
                   
                   
                   
                 sedoheptulose 7- 
                 erythrose 4-phosphate 
                 glycolaldehyde (acceptor) 
               
               
                   
                   
                   
                 phosphate 
                   
                 and D-sedoheptulose 7- 
               
               
                   
                   
                   
                   
                   
                 phosphate (donor) 
               
               
                 71# 
                 2.2.1.2 
                 transaldolase 
                 glycolaldehyde 
                 D-xylulose 5- 
                 transaldolase with 
                 [76] 
               
               
                   
                   
                   
                 phosphate, D- 
                 phosphate, D- 
                 glycolaldehyde phosphate 
               
               
                   
                   
                   
                 sedoheptulose 7- 
                 erythrose 4-phosphate 
                 (acceptor) and D- 
               
               
                   
                   
                   
                 phosphate 
                   
                 sedoheptulose 7-phosphate 
               
               
                   
                   
                   
                   
                   
                 (donor) 
               
               
                 72# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde, D- 
                 D-erythrulose or L- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 xylulose 5-phosphate 
                 erythrulose, D- 
                 glycolaldehyde (acceptor) 
               
               
                   
                   
                   
                   
                 glyceraldehyde 3- 
                 and D-xylulose 5-phosphate 
               
               
                   
                   
                   
                   
                 phosphate 
                 (donor) 
               
               
                 73# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde, D- 
                 D-erythrulose or L- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 fructose 6-phosphate 
                 erythrulose, D- 
                 glycolaldehyde (acceptor) 
               
               
                   
                   
                   
                   
                 erythrose 4-phosphate 
                 and D-fructose 6-phosphate 
               
               
                   
                   
                   
                   
                   
                 (donor) 
               
               
                 74# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde, D- 
                 D-erythrulose or L- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 sedoheptulose 7- 
                 erythrulose, D-ribose 
                 glycolaldehyde (acceptor) 
               
               
                   
                   
                   
                 phosphate 
                 5-phosphate 
                 and D-fructose 6-phosphate 
               
               
                   
                   
                   
                   
                   
                 (donor) 
               
               
                 75# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde, D- 
                 D-erythrulose 4- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 xylulose 5-phosphate 
                 phosphate or L- 
                 glycolaldehyde phosphate 
               
               
                   
                   
                   
                   
                 erythrulose 4- 
                 (acceptor) and D-xylulose 5- 
               
               
                   
                   
                   
                   
                 phosphate, D- 
                 phosphate (donor) 
               
               
                   
                   
                   
                   
                 glyceraldehyde 3- 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 76# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde 
                 D-erythrulose 4- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 phosphate, D-fructose 
                 phosphate or L- 
                 glycolaldehyde phosphate 
               
               
                   
                   
                   
                 6-phosphate 
                 erythrulose 4- 
                 (acceptor) and D-fructose 6- 
               
               
                   
                   
                   
                   
                 phosphate, D- 
                 phosphate (donor) 
               
               
                   
                   
                   
                   
                 erythrose 4-phosphate 
               
               
                 77# 
                 2.2.1.1 
                 transketolase 
                 glycolaldehyde 
                 D-erythrulose 4- 
                 transketolase with 
                 [77] 
               
               
                   
                   
                   
                 phosphate, D- 
                 phosphate or L- 
                 glycolaldehyde phosphate 
               
               
                   
                   
                   
                 sedoheptulose 7- 
                 erythrulose 4- 
                 (acceptor) and D-fructose 6- 
               
               
                   
                   
                   
                 phosphate 
                 phosphate, D-ribose 
                 phosphate (donor) 
               
               
                   
                   
                   
                   
                 5-phosphate 
               
               
                 78# 
                 4.1.2.X 
                 D-fructose 6-phosphate 
                 glycolaldehyde, D- 
                 D-arabinose 5- 
                 D-arabinose 5-phosphate 
                 [78, 
               
               
                   
                   
                 aldolase 
                 glyceraldehyde 3- 
                 phosphate 
                 aldolase 
                 79] 
               
               
                   
                   
                   
                 phosphate 
               
               
                 79# 
                 4.1.2.X 
                 D-fructose 6-phosphate 
                 glycolaldehyde, D- 
                 D-arabinose 
                 D-arabinose aldolase 
                 [79, 
               
               
                   
                   
                 aldolase 
                 glyceraldehyde 
                   
                   
                 80] 
               
               
                 84# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldopentose 5- 
                 D-aldopentose 5-phosphate 
                 [78, 
               
               
                   
                   
                 fructose 6-phosphate 
                 glyceraldehyde 3- 
                 phosphate 
                 aldolase 
                 79] 
               
               
                   
                   
                 aldolase) 
                 phosphate 
               
               
                 85# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldopentose 
                 D-aldopentose aldolase 
                 [79, 
               
               
                   
                   
                 fructose 6-phosphate 
                 glyceraldehyde 
                   
                   
                 80] 
               
               
                   
                   
                 aldolase) 
               
               
                 86# 
                 5.3.1.X/ 
                 Various phosphosugars 
                 D-aldopentose 5- 
                 D-ribulose 5- 
                 D-aldopentose 5-phosphate 
                 [81, 
               
               
                   
                 5.1.3.X 
                 isomerases and epimerases 
                 phosphate 
                 phosphate/D- 
                 isomerase/epimerase 
                 82] 
               
               
                   
                   
                   
                   
                 xylulose 5-phosphate/ 
               
               
                   
                   
                   
                   
                 D-ribose 5-phosphate 
               
               
                 87# 
                 2.7.1.X 
                 Various sugar kinases 
                 D-aldopentose (ATP) 
                 D-aldopentose 5- 
                 D-aldopentose kinase 
                 [68] 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 88# 
                 5.3.1.X/ 
                 Various sugars isomerases 
                 D-aldopentose 
                 D-ribulose/D-xylulose/ 
                 D-aldopentose 
                 [81, 
               
               
                   
                 5.1.3.X 
                 and epimerases 
                   
                 D-ribose 
                 isomerase/epimerase 
                 82] 
               
               
                 89# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldohexose 6- 
                 D-aldohexose 6-phosphate 
                 [78, 
               
               
                   
                   
                 fructose 6-phosphate 
                 aldotetrose 4- 
                 phosphate 
                 aldolase 
                 79] 
               
               
                   
                   
                 aldolase) 
                 phosphate 
               
               
                 90# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldohexose 
                 D-aldohexose aldolase 
                 [79, 
               
               
                   
                   
                 fructose 6-phosphate 
                 aldotetrose 
                   
                   
                 80] 
               
               
                   
                   
                 aldolase) 
               
               
                 91# 
                 5.3.1.X 
                 Various phosphosugars 
                 D-aldohexose 6- 
                 D-fructose 6- 
                 D-aldohexose 6-phosphate 
                 [81, 
               
               
                   
                   
                 isomerases 
                 phosphate 
                 phosphate 
                 isomerase 
                 82] 
               
               
                 92# 
                 2.7.1.X 
                 Various sugar kinases 
                 D-aldohexose (ATP) 
                 D-aldohexose 6- 
                 D-aldohexose kinase 
                 [68] 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 93# 
                 5.3.1.X 
                 Various sugars isomerases 
                 D-aldohexose 
                 D-fructose 
                 D-aldohexose isomerase 
                 [81, 
               
               
                   
                   
                   
                   
                   
                   
                 82] 
               
               
                 97# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-xylulose 5- 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 glyceraldehyde 3- 
                 phosphate 
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                 phosphate 
                   
                 D-glyceraldehyde 3- 
               
               
                   
                   
                   
                   
                   
                 phosphate (acceptor) 
               
               
                 98# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-xylulose 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 glyceraldehyde 
                   
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                   
                   
                 D-glyceraldehyde (acceptor) 
               
               
                 99# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-ribulose 5- 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 glyceraldehyde 3- 
                 phosphate 
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                 phosphate 
                   
                 D-glyceraldehyde 3- 
               
               
                   
                   
                   
                   
                   
                 phosphate (acceptor) 
               
               
                 100# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-ribulose 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 glyceraldehyde 
                   
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                   
                   
                 D-glyceraldehyde (acceptor) 
               
               
                 101# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-ketohexose 6- 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 aldotetrose 4- 
                 phosphate 
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                 phosphate 
                   
                 D-aldotetrose 4-phosphate 
               
               
                   
                   
                   
                   
                   
                 (acceptor) 
               
               
                 102# 
                 2.2.1.2 
                 transketolase 
                 glycolaldehyde, D- 
                 D-ketohexose 
                 transketolase with 
                 [64] 
               
               
                   
                   
                   
                 aldotetrose 
                   
                 glycolaldehyde (donor) and 
               
               
                   
                   
                   
                   
                   
                 D-aldotetrose (acceptor) 
               
               
                 103# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldohexose 6- 
                 D-aldoheptose 7-phosphate 
                 [78, 
               
               
                   
                   
                 fructose 6-phosphate 
                 aldopentose 4- 
                 phosphate 
                 aldolase 
                 79] 
               
               
                   
                   
                 aldolase) 
                 phosphate 
               
               
                 104# 
                 4.1.2.X 
                 Various aldolases (e.g., D- 
                 glycolaldehyde, D- 
                 D-aldohexose 
                 D-aldoheptose aldolase 
                 [79, 
               
               
                   
                   
                 fructose 6-phosphate 
                 tetrose 
                   
                   
                 80] 
               
               
                   
                   
                 aldolase) 
               
               
                 105# 
                 5.3.1.X 
                 Various phosphosugars 
                 D-aldoheptose 7- 
                 D-sedoheptulose 7- 
                 D-aldoheptose 7-phosphate 
                 [81, 
               
               
                   
                   
                 isomerases and epimerases 
                 phosphate 
                 phosphate 
                 isomerase 
                 82] 
               
               
                 106# 
                 2.7.1.X 
                 Various sugar kinases 
                 D-aldoheptose (ATP) 
                 D-aldoheptose 7- 
                 D-aldoheptose kinase 
                 [68] 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 107# 
                 5.3.1.X 
                 Various sugars isomerases 
                 D-aldoheptose 
                 D-sedoheptulose 
                 D-aldoheptose isomerase 
                 [81, 
               
               
                   
                   
                 and epimerases 
                   
                   
                   
                 82] 
               
               
                 109# 
                 4.1.2.X 
                 Various aldolases 
                 dihydroxyacetone 
                 D-xylulose 1- 
                 D-xylulose 1-phosphate 
                 [45] 
               
               
                   
                   
                   
                 phosphate, 
                 phosphate 
                 aldolase 
               
               
                   
                   
                   
                 glycolaldehyde 
               
               
                 110# 
                 4.1.2.X 
                 Various aldolases 
                 dihydroxyacetone, 
                 D-xylulose 
                 D-xylulose aldolase 
                 [45] 
               
               
                   
                   
                   
                 glycolaldehyde 
               
               
                 111# 
                 4.1.2.X 
                 Various aldolases 
                 dihydroxyacetone, 
                 D-ribulose 
                 D-ribulose aldolase 
                 [4, 
               
               
                   
                   
                   
                   
                   
                   
                 59] 
               
               
                 112# 
                 4.1.2.43 
                 3-hexulose-6-phosphate 
                 glycolaldehyde, D- 
                 4-heptulose 7- 
                 4-heptulose 7-phosphate 
                 [83] 
               
               
                   
                   
                 synthase 
                 ribulose 5-phosphate 
                 phosphate 
                 synthase 
               
               
                 113# 
                 3.1.3.X 
                 Various phosphatases 
                 D-ribulose 1- 
                 D-ribulose, phosphate 
                 D-ribulose 1-phosphatase 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
               
               
                 114# 
                 5.1.3.X 
                 Various epimerases 
                 D-xylulose-1- 
                 D-ribulose-1- 
                 D-ribulose-1-phosphate 3- 
                 [85] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 epimerase 
               
               
                 115# 
                 3.1.3.X 
                 Various phosphatases 
                 D-xylulose 1- 
                 D-xylulose 
                 D-xylulose 1-phosphatase 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 (phosphate) 
               
               
                 116# 
                 5.3.1.X 
                 Various isomerases (e.g., 3- 
                 4-heptulose 7- 
                 D-Sedoheptulose 7- 
                 4-heptulose 7-phosphate 
                 [86] 
               
               
                   
                   
                 hexulose-6-phosphate 
                 phosphate 
                 phosphate 
                 isomerases 
               
               
                   
                   
                 isomerase) 
               
               
                 117# 
                 4.1.2.17 
                 L-fuculose-phosphate 
                 glycolaldehyde 2- 
                 D-ribulose 5- 
                 D-ribuolse 5-phosphate 
                 [4, 59] 
               
               
                   
                   
                 aldolase 
                 phosphate, 
                 phosphate 
                 aldolase 
               
               
                   
                   
                   
                 dihydroxyacetone 
               
               
                 118# 
                 4.1.2.X 
                 Various aldolases 
                 glycolaldehyde 2- 
                 D-xylulose 5- 
                 D-xylulose 5-phosphate 
                 [45] 
               
               
                   
                   
                   
                 phosphate, 
                 phosphate 
                 aldolase 
               
               
                   
                   
                   
                 dihydroxyacetone 
               
               
                 119# 
                 4.1.2.X 
                 various aldolases 
                 2 glycolaldehyde 
                 D-erythrose or L- 
                 (D-erythrose or L-erythrose) 
                 [45] 
               
               
                   
                   
                   
                   
                 erythrose 
                 aldolase 
               
               
                 120# 
                 4.1.2.X 
                 various aldolases (e.g., D- 
                 2 glycolaldehyde 
                 D-threose or L-threose 
                 (D-threose or L-threose) 
                 [45, 
               
               
                   
                   
                 fructose 6-phosphate 
                   
                   
                 aldolase 
                 78] 
               
               
                   
                   
                 aldolase) 
               
               
                 121# 
                 4.1.1.X 
                 transketolase, pyruvate 
                 2 glycolaldehyde 
                 D-erythrulose or L- 
                 (D-erythrulose or L- 
                 [64-66] 
               
               
                   
                   
                 decarboxylase or other 
                   
                 erythrulose 
                 erythrulose) synthetase 
               
               
                   
                   
                 thiamine dependent enzymes 
               
               
                 122# 
                 4.1.2.X 
                 various aldolases 
                 2 glycolaldehyde 
                 D-erythrose 4- 
                 (D-erythrose 4-phosphate or 
                 [45] 
               
               
                   
                   
                   
                   
                 phosphate or L- 
                 L-erythrose 4-phosphate) 
               
               
                   
                   
                   
                   
                 erythrose 4-phosphate 
                 aldolase 
               
               
                 123# 
                 4.1.2.X 
                 various aldolases (e.g., D- 
                 2 glycolaldehyde 
                 D-threose 4- 
                 (D-threose 4-phosphate or 
                 [45, 
               
               
                   
                   
                 fructose 6-phosphate 
                   
                 phosphate or L- 
                 L-threose 4-phosphate) 
                 78] 
               
               
                   
                   
                 aldolase) 
                   
                 threose 4-phosphate 
                 aldolase 
               
               
                 124# 
                 4.1.1.X 
                 transketolase, pyruvate 
                 2 molecules 
                 D-erythrulose 4- 
                 (D-erythrulose 4-phosphate 
                 [64-66] 
               
               
                   
                   
                 decarboxylase or other 
                 glycolaldehyde 
                 phosphate or L- 
                 or L-erythrulose 4- 
               
               
                   
                   
                 thiamine dependent enzymes 
                   
                 erythrulose 4- 
                 phosphate) synthetase 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 125# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4-trihydroxy 
                 D-erythrose or L- 
                 (D-erythrose or L-erythrose 
                 [42, 
               
               
                   
                   
                 dehydrogenases (acylating) 
                 butyryl-CoA 
                 erythrose or D-threose 
                 or D-threose or L-threose) 
                 43] 
               
               
                   
                   
                   
                   
                 or L-threose 
                 dehydrogenase 
               
               
                 126# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, D- 
                 2,3,4,5-tetrahydroxy- 
                 2,3,4,5-tetrahydroxy- 
                 [87] 
               
               
                   
                   
                   
                 glyceraldehyde 
                 pentanoyl-CoA 
                 pentanoyl-CoA 
               
               
                   
                   
                   
                 3-phosphate 
                 5-phosphate 
                 5-phosphate lyase 
               
               
                 127# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, D- 
                 2,3,4,5-tetrahydroxy- 
                 2,3,4,5-tetrahydroxy- 
                 [87] 
               
               
                   
                   
                   
                 glyceraldehyde 
                 pentanoyl-CoA 
                 pentanoyl-CoA 
               
               
                   
                   
                   
                   
                   
                 lyase 
               
               
                 128# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4,5-tetrahydroxy- 
                 D-aldopentose 
                 2,3,4,5-tetrahydroxy- 
                 [88] 
               
               
                   
                   
                 dehydrogenases (acetylating) 
                 pentanoyl-CoA 
                 5-phosphate 
                 pentanoyl-CoA 
               
               
                   
                   
                   
                 5-phosphate 
                 (NAD(P), CoA) 
                 5-phosphate reductase 
               
               
                   
                   
                   
                 (NAD(P)H) 
               
               
                 129# 
                 2.7.1.X 
                 various kinases 
                 2,3,4,5-tetrahydroxy- 
                 2,3,4,5-tetrahydroxy- 
                 2,3,4,5-tetrahydroxy- 
                 [68] 
               
               
                   
                   
                   
                 pentanoyl-CoA (ADP) 
                 pentanoyl-CoA 
                 pentanoyl-CoA 
               
               
                   
                   
                   
                   
                 5-phosphate (ADP) 
                 kinase 
               
               
                 130# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4,5-tetrahydroxy- 
                 D-aldopentose 
                 2,3,4,5-tetrahydroxy- 
                 [88] 
               
               
                   
                   
                 dehydrogenases (acetylating) 
                 pentanoyl-CoA 
                 (NAD(P), CoA) 
                 pentanoyl-CoA 
               
               
                   
                   
                   
                 (NAD(P)H) 
                   
                 reductase 
               
               
                 131# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, D- 
                 2,3,4,5,6- 
                 2,3,4,5,6-pentahydroxy- 
                 [87] 
               
               
                   
                   
                   
                 aldotetrose 
                 pentahydroxy- 
                 hexanoyl-CoA 6-phosphate 
               
               
                   
                   
                   
                 4-phosphate 
                 hexanoyl-CoA 
                 lyase 
               
               
                   
                   
                   
                   
                 6-phosphate 
               
               
                 132# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, D- 
                 2,3,4,5,6- 
                 2,3,4,5,6-pentahydroxy- 
                 [87] 
               
               
                   
                   
                   
                 aldotetrose 
                 pentahydroxy- 
                 hexanoyl-CoA lyase 
               
               
                   
                   
                   
                   
                 hexanoyl-CoA 
               
               
                 133# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4,5,6- 
                 D-aldohexose 
                 2,3,4,5,6-pentahydroxy- 
                 [88] 
               
               
                   
                   
                 dehydrogenases (acetylating) 
                 pentahydroxy- 
                 6-phosphate (NAD(P), 
                 hexanoyl-CoA reductase 
               
               
                   
                   
                   
                 hexanoyl-CoA 
                 CoA) 
               
               
                   
                   
                   
                 (NAD(P)H) 
               
               
                 134# 
                 2.7.1.X 
                 various kinases 
                 2,3,4,5,6- 
                 2,3,4,5,6- 
                 2,3,4,5,6-pentahydroxy- 
                 [68] 
               
               
                   
                   
                   
                 pentahydroxy- 
                 pentahydroxy- 
                 hexanoyl-CoA kinase 
               
               
                   
                   
                   
                 hexanoyl-CoA (ATP) 
                 hexanoyl-CoA 
               
               
                   
                   
                   
                   
                 6-phosphate (ADP) 
               
               
                 135# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4,5,6- 
                 D-aldohexose 
                 2,3,4,5,6-pentahydroxy- 
                 [88] 
               
               
                   
                   
                 dehydrogenases (acetylating) 
                 pentahydroxy- 
                 (NAD(P), CoA) 
                 hexanoyl-CoA reductase 
               
               
                   
                   
                   
                 hexanoyl-CoA 
               
               
                   
                   
                   
                 (NAD(P)H) 
               
               
                 136# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, 
                 2,3,4-trihydroxy- 
                 2,3,4-trihydroxy-butyryl-CoA 
                 [87] 
               
               
                   
                   
                   
                 glycolaldehyde 
                 butyryl-CoA 
                 4-phosphate lyase 
               
               
                   
                   
                   
                 phosphate 
                 4-phosphate 
               
               
                 137# 
                 4.1.3.X 
                 various lyases 
                 glycolyl-CoA, 
                 2,3,4-trihydroxy- 
                 2,3,4-trihydroxy-butyryl-CoA 
                 [87] 
               
               
                   
                   
                   
                 glycolaldehyde 
                 butyryl-CoA 
                 lyase 
               
               
                 138# 
                 1.2.1.X 
                 various aldehyde 
                 2,3,4-trihydroxy- 
                 D-aldotetrose 
                 2,3,4-trihydroxy-butyryl-CoA 
                 [88] 
               
               
                   
                   
                 dehydrogenases (acetylating) 
                 butyryl-CoA 
                 4-phosphate (NAD(P), 
                 reductase 
               
               
                   
                   
                   
                 (NAD(P)H) 
                 CoA) 
               
               
                 139# 
                 2.7.1.X 
                 various kinases 
                 2,3,4-trihydroxy- 
                 2,3,4-trihydroxy- 
                 2,3,4-trihydroxy-butyryl-CoA 
                 [68] 
               
               
                   
                   
                   
                 butyryl-CoA (ATP) 
                 butyryl-CoA 
                 kinase 
               
               
                   
                   
                   
                   
                 4-phosphate (ADP) 
               
               
                 140# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-xylulose 5- 
                 D-xylulose 5-phosphate 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glyceraldehyde 3- 
                 phosphate (NAD(P), 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 phosphate (NAD(P)H) 
                 CoA) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 141# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-xylulose (NAD(P), 
                 D-xylulose dehydrogenase 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glyceraldehyde 
                 CoA) 
                 complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 (NAD(P)H) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 142# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ribulose 5- 
                 D-ribulose 5-phosphate 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glyceraldehyde 3- 
                 phosphate (NAD(P), 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 phosphate (NAD(P)H) 
                 CoA) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 143# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ribulose (NAD(P), 
                 D-ribulose dehydrogenase 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glyceraldehyde 
                 CoA) 
                 complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 (NAD(P)H) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 144# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ketohexose 6- 
                 D-ketohexose 6-phosphate 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 aldotetrose 4- 
                 phosphate (NAD(P), 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 phosphate (NAD(P)H) 
                 CoA) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 145# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ketohexose 
                 D-ketohexose 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 aldotetrose (NAD(P)H) 
                 (NAD(P), CoA) 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 146# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ketoheptose 7- 
                 D-ketoheptose 7-phosphate 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 aldopntose 5- 
                 phosphate (NAD(P), 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 phosphate (NAD(P)H) 
                 CoA) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 147# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, D- 
                 D-ketoheptose 
                 D-ketoheptose 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 aldopntose (NAD(P)H) 
                 (NAD(P), CoA) 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 148# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, 
                 D/L-erythrulose 4- 
                 D/L-erythrulose 4-phosphate 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glycolaldehyde 
                 phosphate (NAD(P), 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 phosphate (NAD(P)H) 
                 CoA) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 149# 
                 2.3.1.X 
                 Thiamine-dependent 
                 glycolyl-CoA, 
                 D-D/L-erythrulose 
                 D/L-erythrulose 
                 [89] 
               
               
                   
                   
                 dehydrogenase condensing 
                 glycolaldehyde 
                 (NAD(P), CoA) 
                 dehydrogenase complex 
               
               
                   
                   
                 glycolyl-CoA as an acceptor 
                 (NAD(P)H) 
               
               
                   
                   
                 (e.g., evolved acetoin 
               
               
                   
                   
                 dehydrogenase complex) 
               
               
                 Z1# 
                 4.1.2.X 
                 various aldolases 
                 D-ketohexose 1,6- 
                 D-glyceraldehyde 3- 
                 D-ketohexose 1,6- 
                 [90, 
               
               
                   
                   
                   
                 bisphosphate 
                 phosphate, 
                 bisphosphate aldolase 
                 91] 
               
               
                   
                   
                   
                   
                 dihydroxyacetone 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z2# 
                 3.1.3.X 
                 various phosphatases 
                 D-ketohexose 1,6- 
                 D-ketohexose 1- 
                 D-ketohexose 1,6- 
                 [84] 
               
               
                   
                   
                   
                 bisphosphate 
                 phosphate, phosphate 
                 bisphosphate 6- 
               
               
                   
                   
                   
                   
                   
                 phosphatase 
               
               
                 Z3# 
                 3.1.3.X 
                 various phosphatases 
                 D-ketohexose 1,6- 
                 D-ketohexose 6- 
                 D-ketohexose 1,6- 
                 [84] 
               
               
                   
                   
                   
                 bisphosphate 
                 phosphate, phosphate 
                 bisphosphate 1- 
               
               
                   
                   
                   
                   
                   
                 phosphatase 
               
               
                 Z4# 
                 5.4.2.X 
                 various mutases 
                 D-ketohexose 1- 
                 D-ketohexose 6- 
                 phosphohexomutase 
                 [92] 
               
               
                   
                   
                   
                 bisphosphate 
                 bisphosphate 
               
               
                 Z5# 
                 3.1.3.X 
                 various phosphatases 
                 D-ketohexose 1- 
                 D-ketohexose, 
                 D-ketohexose 1- 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z6# 
                 3.1.3.X 
                 various phosphatases 
                 D-ketohexose 6- 
                 D-ketohexose, 
                 D-ketohexose 6- 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z7# 
                 4.1.2.X 
                 various aldolases 
                 D-ketohexose 1- 
                 dihydroxyacetone 
                 D-ketohexose 1- 
                 [90, 
               
               
                   
                   
                   
                 phosphatase 
                 phosphate, D- 
                 phosphatase aldolase 
                 91] 
               
               
                   
                   
                   
                   
                 glyceraldehyde 
               
               
                 Z8# 
                 4.1.2.X 
                 various aldolases 
                 D-ketohexose 6- 
                 dihydroxyacetone, D- 
                 D-ketohexose 6- 
                 [90, 
               
               
                   
                   
                   
                 phosphatase 
                 glyceraldehyde 3- 
                 phosphatase aldolase 
                 91] 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z9# 
                 4.1.2.X 
                 various aldolases 
                 D-ketohexose 
                 dihydroxyacetone, D- 
                 D-ketohexose aldolase 
                 [90, 
               
               
                   
                   
                   
                   
                 glyceraldehyde 
                   
                 91] 
               
               
                 Z16# 
                 5.3.1.X 
                 various sugar isomerases 
                 D-glyceraldehyde 
                 dihydroxyacetone 
                 triose isomerase 
                 [81, 
               
               
                   
                   
                   
                   
                   
                   
                 82] 
               
               
                 Z17# 
                 3.1.3.X 
                 various phosphatases 
                 D-glyceraldehyde 3- 
                 D-glyceraldehyde, 
                 D-glyceraldehyde 3- 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z18# 
                 3.1.3.X 
                 various phosphatases 
                 dihydroxyacetone 
                 dihydroxyacetone, 
                 dihydroxyacetone 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z21# 
                 3.1.3.X 
                 various phosphatases 
                 D-sedoheptulose 1,7- 
                 D-sedoheptulose 1- 
                 D-sedoheptulose 1,7- 
                 [84] 
               
               
                   
                   
                   
                 bisphosphate 
                 phosphate, phosphate 
                 bisphosphate 7- 
               
               
                   
                   
                   
                   
                   
                 phosphatase 
               
               
                 Z22# 
                 3.1.3.X 
                 various phosphatases 
                 D-sedoheptulose 7- 
                 D-sedoheptulose, 
                 D-sedoheptulose 7- 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z23# 
                 4.1.2.X 
                 various aldolases 
                 D-sedoheptulose 7- 
                 D-erythrose 4- 
                 D-sedoheptulose 7- 
                 [93] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate, 
                 phosphate aldolase 
               
               
                   
                   
                   
                   
                 dihydroxyacetone 
               
               
                 Z24# 
                 3.1.3.X 
                 various phosphatases 
                 D-erythrose 4- 
                 D-erythrose, 
                 D-erythrose 4-phosphatase 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
               
               
                 Z25# 
                 4.1.2.X 
                 various aldolases 
                 D-sedoheptulose 
                 D-erythrose, 
                 D-sedoheptulose aldolase 
                 [93] 
               
               
                   
                   
                   
                   
                 dihydroxyacetone 
               
               
                 Z26# 
                 3.1.3.X 
                 various phosphatases 
                 D-sedoheptulose 1- 
                 D-sedoheptulose, 
                 D-sedoheptulose 1- 
                 [84] 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
                 phosphatase 
               
               
                 Z27# 
                 4.1.2.X 
                 various aldolases 
                 D-sedoheptulose 1- 
                 D-erythrose, 
                 D-sedoheptulose 1- 
                 [45] 
               
               
                   
                   
                   
                 phosphate 
                 dihydroxyacetone 
                 phosphate aldolase 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z28# 
                 5.1.3.X 
                 various sugar epimerases 
                 D-erythrose 4- 
                 D-threose 4- 
                 (D-erythrose or L-erythrose) 
                 [69] 
               
               
                   
                   
                   
                 phosphate or L- 
                 phosphate or L- 
                 4-phosphate epimerase 
               
               
                   
                   
                   
                 erythrose 4-phosphate 
                 threose 4-phosphate 
               
               
                 Z29# 
                 5.3.1.X 
                 various sugar isomerases 
                 D-erythrose 4- 
                 D-erythrulose 4- 
                 (D-erythrose or L- 
                 [69] 
               
               
                   
                   
                   
                 phosphate or L- 
                 phosphate or L- 
                 erythrose) 4-phosphate 
               
               
                   
                   
                   
                 erythrose 4-phosphate 
                 erythrulose 4- 
                 isomerase 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z30# 
                 5.3.1.X 
                 various sugar isomerases 
                 D-threose 4-phosphate 
                 D-erythrulose 4- 
                 (D-threose or L-threose) 4- 
                 [69] 
               
               
                   
                   
                   
                 or L-threose 4- 
                 phosphate or L- 
                 phosphate isomerase 
               
               
                   
                   
                   
                 phosphate 
                 erythrulose 4- 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z31# 
                 5.1.3.X 
                 various sugar epimerases 
                 D-erythrose or L- 
                 D-threose or L- 
                 (D-erythrose or L-erythrose) 
                 [81, 
               
               
                   
                   
                   
                 erythrose 
                 threose 
                 epimerase 
                 82] 
               
               
                 Z32# 
                 5.3.1.X 
                 various sugar isomerases 
                 D-erythrose or L- 
                 D-erythrulose or L- 
                 (D-erythrose or L- 
                 [81, 
               
               
                   
                   
                   
                 erythrose 
                 erythrulose 
                 erythrose) isomerase 
                 82] 
               
               
                 Z33# 
                 5.3.1.X 
                 various sugar isomerases 
                 D-threose or L- 
                 D-erythrulose or L- 
                 (D-threose or L-threose) 
                 [81, 
               
               
                   
                   
                   
                 threose 
                 erythrulose 
                 isomerase 
                 82] 
               
               
                 Z34# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrose or L- 
                 erythritol 4-phosphate 
                 (D-erythrose or L-erythrose) 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 erythrose 4-phosphate 
                   
                 4-phosphate reductase 
               
               
                 Z35# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-threose 4-phosphate 
                 D-threitol 4-phosphate 
                 (D-threose or L-threose) 4- 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 or L-threose 4- 
                 or L-threitol 4- 
                 phosphate reductase 
               
               
                   
                   
                   
                 phosphate 
                 phosphate 
               
               
                 Z36# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrulose 4- 
                 erythritol 4-phosphate 
                 (D-erythrulose or L- 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 phosphate or L- 
                   
                 erythrulose) 4-phosphate 
               
               
                   
                   
                   
                 erythrulose 4- 
                   
                 reductase (erythritol 4- 
               
               
                   
                   
                   
                 phosphate 
                   
                 phosphate forming) 
               
               
                 Z37# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrulose 4- 
                 D-threitol 4-phosphate 
                 (D-erythrulose or L- 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 phosphate or L- 
                 or L-threitol 4- 
                 erythrulose) 4-phosphate 
               
               
                   
                   
                   
                 erythrulose 4- 
                 phosphate 
                 reductase (D-threitol or L- 
               
               
                   
                   
                   
                 phosphate 
                   
                 threitol 4-phosphate 
               
               
                   
                   
                   
                   
                   
                 forming) 
               
               
                 Z38# 
                 5.1.3.X 
                 various sugar epimerases 
                 erythritol 4-phosphate 
                 D-threitol 4-phosphate 
                 erythritol 4-phosphate 
                 [97] 
               
               
                   
                   
                   
                   
                 or L-threitol 4- 
                 epimerase 
               
               
                   
                   
                   
                   
                 phosphate 
               
               
                 Z39# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrose or L- 
                 erythritol 
                 (D-erythrose or L-erythrose) 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 erythrose 
                   
                 reductase 
               
               
                 Z40# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-threose or L-threose 
                 D-threitol or L-threitol 
                 (D-threose or L-threose) 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                   
                   
                 reductase 
               
               
                 Z41# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrulose or L- 
                 erythritol 
                 (D-erythrulose or L- 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 erythrulose 
                   
                 erythrulose) reductase 
               
               
                   
                   
                   
                   
                   
                 (erythritol forming) 
               
               
                 Z42# 
                 1.1.1.X 
                 various alcohol-sugar 
                 D-erythrulose or L- 
                 D-threitol or L-threitol 
                 (D-erythrulose or L- 
                 [94-96] 
               
               
                   
                   
                 dehydrogenases 
                 erythrulose 
                   
                 erythrulose) reductase (D- 
               
               
                   
                   
                   
                   
                   
                 threitol or L-threitol forming) 
               
               
                 Z43# 
                 5.1.3.X 
                 various sugar epimerases 
                 erythritol 
                 D-threitol or L-threitol 
                 erythritol epimerase 
                 [97] 
               
               
                 Z44# 
                 2.7.1.X 
                 various sugar kinases 
                 D-erythrose or L- 
                 D-erythrose 4- 
                 (D-erythrose or L-erythrose) 
                 [46, 
               
               
                   
                   
                   
                 erythrose (ATP) 
                 phosphate or L- 
                 kinase 
                 68, 
               
               
                   
                   
                   
                   
                 erythrose 4-phosphate 
                   
                 98] 
               
               
                   
                   
                   
                   
                 (ADP) 
               
               
                 Z45# 
                 2.7.1.X 
                 various sugar kinases 
                 D-threose or L-threose 
                 D-threose 4- 
                 (D-threose or L-threose) 
                 [68] 
               
               
                   
                   
                   
                 (ATP) 
                 phosphate or L- 
                 kinase 
               
               
                   
                   
                   
                   
                 threose 4-phosphate 
               
               
                   
                   
                   
                   
                 (ADP) 
               
               
                 Z46# 
                 2.7.1.X 
                 various sugar kinases 
                 D-erythrulose or L- 
                 D-erythrulose 4- 
                 (D-erythrulose or L- 
                 [46, 
               
               
                   
                   
                   
                 erythrulose (ATP) 
                 phosphate or L- 
                 erythrulose) kinase 
                 68, 
               
               
                   
                   
                   
                   
                 erythrulose 4- 
                   
                 99] 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                 Z47# 
                 2.7.1.X 
                 various sugar kinases 
                 erythritol (ATP) 
                 Erythritol 4-phosphate 
                 erythritol kinase 
                 [68] 
               
               
                   
                   
                   
                   
                 (ADP) 
               
               
                 Z48# 
                 2.7.1.X 
                 various sugar kinases 
                 D-threitol or L-threitol 
                 D-threitol 4-phosphate 
                 (D-threitol or L-threitol) 
                 [68] 
               
               
                   
                   
                   
                 (ATP) 
                 or L-threitol 4- 
                 kinase 
               
               
                   
                   
                   
                   
                 phosphate (ADP) 
               
               
                   
               
            
           
         
       
     
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     Table 4. 
     Table 4 shows enzymes used for the synthetic photorespiratory bypass pathway illustrated in Example 6. The abbreviations (abbr.) defined herein are used in the Figures and/or corresponding Figure descriptions of  FIGS. 7 to 11 . 
     
       
         
           
               
               
               
               
             
               
                 TABLE 4 
               
               
                   
               
               
                   
                   
                   
                 NCBI accession 
               
               
                 enzyme 
                 organism 
                 abbr. 
                 no. 
               
               
                   
               
             
            
               
                 propionyl-CoA transferase 
                 
                   Ralstonia eutropha 
                 
                 PCT Re   
                 CAJ93797.1 
               
               
                 propionyl-CoA transferase 
                 
                   Clostridium propionicum 
                 
                 PCT Cp   
                 CAB77207.1 
               
               
                 propionyl-CoA 
                 
                   Methylobacterium 
                 
                 PCC Me   
                 WP_003599287.1 
               
               
                 carboxylase 
                 
                   extorquens 
                 
                   
                 (pccA subunit); 
               
               
                   
                   
                   
                 WP_003597263.1 
               
               
                   
                   
                   
                 (pccB subunit) 
               
               
                 malonyl-CoA reductase 
                 
                   Chloroflexus aurantiacus 
                 
                 MCR Ca   
                 AAS20429.1 
               
               
                 malonyl-CoA reductase 
                   Erythrobacter  sp. NAP1 
                 MCR E   
                 WP_007163680.1 
               
               
                   
               
            
           
         
       
     
     In addition to the above mentioned enzymes also the mutant variant PCC Me _D407I_Y143H was employed. This protein comprises the WT sequence of the pccA subunit and a pccB subunit comprising the amino acid substitutions D407I and Y143H (wherein the respective number indicates the amino acid position in the amino acid sequence of pccB as disclosed in the NCBI entry having the accession code WP_003597263.1. 
     Table 5. 
     Table 5 summarizes the enzymes employed in Example 6 and their kinetical properties (K m  (substrate) and v max ) as determined in Example 6. 
     
       
         
           
               
               
               
             
               
                 TABLE 5 
               
               
                   
               
               
                 enzyme 
                 K m  (substrate) 
                 v max   
               
               
                   
               
             
            
               
                 PCT Re   
                  51.7 ± 9.6 mM (glycolate) 
                 1.3 ± 0.07 U mg −1   
               
               
                 PCT Cp   
                    149 ± 35 mM (glycolate) 
                 0.03 ± 0.003 U mg −1   
               
               
                 PCC Me   
                  1.0 ± 0.15 mM (glycolyl-CoA) 
                 1.5 ± 0.09 U mg −1   
               
               
                 D407I 
               
               
                 Y143H 
               
               
                 MCR Ca   
                 0.03 ± 0.003 mM (tartronyl-CoA) 
                 0.6 ± 0.01 U mg −1   
               
               
                 MCR E   
                  0.18 ± 0.04 mM (tartronyl-CoA) 
                 0.23 ± 0.01 U mg −1