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The distribution of mitochondria, including the mitochondrial genome, into daughter cells after mitosis or meiosis, mediated by interactions between mitochondria and the cytoskeleton. [GOC:mcc, PMID:10873824, PMID:11389764] | null |
Enables the transfer of zinc ions (Zn2+) from one side of a membrane to the other, probably powered by proton motive force. In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations. [TC:2.A.5.1.1] | null |
Enables the transfer of zinc ions (Zn2+) from one side of a membrane to the other, probably powered by proton motive force. In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations. [TC:2.A.5.1.1] | null |
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. [PMID:9708911, RHEA:27794] | null |
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. [PMID:9708911, RHEA:27794] | null |
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. [PMID:9708911, RHEA:27794] | null |
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. [PMID:9708911, RHEA:27794] | null |
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate. [PMID:9708911, RHEA:27794] | null |
A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water. [GOC:jl, ISBN:0198506732] | null |
Catalysis of the reaction: lactose + H2O = D-glucose + D-galactose. [PMID:12023280] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). [GOC:jl, ISBN:0198506732] | null |
The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. [GOC:ai] | null |
The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. [GOC:ai] | null |
The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. [GOC:ai] | null |
The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. [GOC:ai] | null |
Catalysis of the reaction: adenine + H+ + H2O = hypoxanthine + NH4+. [RHEA:23688] | null |
Catalysis of the reaction: adenine + H+ + H2O = hypoxanthine + NH4+. [RHEA:23688] | null |
Catalysis of the reaction: adenine + H+ + H2O = hypoxanthine + NH4+. [RHEA:23688] | null |
Catalysis of the reaction: adenine + H+ + H2O = hypoxanthine + NH4+. [RHEA:23688] | null |
Binding to an acyl group, any group formally derived by removal of the hydroxyl group from the acid function of a carboxylic acid. [GOC:curators, ISBN:0198506732] | null |
Binding an acyl group and presenting it for processing or offloading to a cognate enzyme. Covalently binds the acyl group via a phosphopantetheine prosthetic group and mediates protein-protein interactions with the enzyme conferring specificity. The acyl carrier protein (ACP) presents substrates to enzymes involved in fatty acid biosynthesis or in polyketide secondary metabolite biosynthesis. [GOC:jl, GOC:vw] | null |
The sequence of reactions by which arginine is synthesized from ornithine, then cleaved to yield urea and regenerate ornithine. The overall reaction equation is NH3 + CO2 + aspartate + 3 ATP + 2 H2O = urea + fumarate + 2 ADP + 2 phosphate + AMP + diphosphate. [GOC:pde, GOC:vw, ISBN:0198506732] | null |
The sequence of reactions by which arginine is synthesized from ornithine, then cleaved to yield urea and regenerate ornithine. The overall reaction equation is NH3 + CO2 + aspartate + 3 ATP + 2 H2O = urea + fumarate + 2 ADP + 2 phosphate + AMP + diphosphate. [GOC:pde, GOC:vw, ISBN:0198506732] | null |
The sequence of reactions by which arginine is synthesized from ornithine, then cleaved to yield urea and regenerate ornithine. The overall reaction equation is NH3 + CO2 + aspartate + 3 ATP + 2 H2O = urea + fumarate + 2 ADP + 2 phosphate + AMP + diphosphate. [GOC:pde, GOC:vw, ISBN:0198506732] | null |
The chemical reactions and pathways involving argininosuccinate, 2-(N(omega)-arginino)succinate, an intermediate in the ornithine-urea cycle, where it is synthesized from citrulline and aspartate. [ISBN:0198506732] | null |
The cell cycle 'gap' phase which is the interval between the completion of DNA segregation by mitosis and the beginning of DNA synthesis. [GOC:mtg_cell_cycle] | null |
The cell cycle phase, following G1, during which DNA synthesis takes place as part of a mitotic cell cycle. [GOC:mtg_cell_cycle] | null |
The cell cycle phase, following G1, during which DNA synthesis takes place as part of a mitotic cell cycle. [GOC:mtg_cell_cycle] | null |
The cell cycle 'gap' phase which is the interval between the completion of DNA synthesis and the beginning of DNA segregation by mitosis. [GOC:mtg_cell_cycle] | null |
Enables the transfer of S-methylmethionine from one side of a membrane to the other. [GOC:ai] | null |
Enables the transfer of S-methylmethionine from one side of a membrane to the other. [GOC:ai] | null |
Enables the transfer of L-methionine from one side of a membrane to the other, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters. [GOC:mtg_transport] | null |
Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. [RHEA:24793] | null |
Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. [RHEA:24793] | null |
Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. [RHEA:24793] | null |
Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. [RHEA:24793] | null |
One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities. In S. cerevisiae, it is composed of Rad1p, Rad10p, and Rad14p; in human the subunits are ERCC4/XPF, ERCC1 and XPA, respectively. [PMID:10915862] | null |
One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities. In S. cerevisiae, it is composed of Rad1p, Rad10p, and Rad14p; in human the subunits are ERCC4/XPF, ERCC1 and XPA, respectively. [PMID:10915862] | null |
One of several protein complexes involved in nucleotide-excision repair; possesses damaged DNA binding activity. In S. cerevisiae, it is composed of Rad4p and Rad23p. [PMID:10915862] | null |
One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and DNA-dependent ATPase activities. In S. cerevisiae, it is composed of Rad7p and Rad16p. [PMID:10915862] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
Catalysis of the reaction: H2O + sn-glycerol 1-phosphate = glycerol + phosphate. [RHEA:46084] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
A SAGA-type histone acetyltransferase complex that deubiquitinates H2A and/or H2B. This complex is organized into several functional submodules: a structural core including the activator binding module and consisting of ADA1 or a homolog, members of the SPT and TAF protein families as well as promotor recruitment factor TRRAP/TRA1, a histone acetyltransferase (HAT) module consisting of GCN5/KAT2A or PCAF/KAT2B, ADA2, ADA3/NGG1, and SGF29 or homologues thereof, a histone deubiquitinase (DUB) module consisting of ATXN7/SGF73, ATXN7L3/SGF11, ENY2/SUS1 and USP22/UBP8 or homologues thereof, and in some taxa a splicing module consisting of SF3B3 and SF3B5 or homologues thereof (not in fungi). In budding yeast also contains Spt8 which distinguishes it from SAGA-like (SLIK) complex (GO:0046695). [PMID:10637607, PMID:17337012, PMID:19056896, PMID:20838651, PMID:33004486] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
Catalysis of the reaction: 1-hexadecanoyl-sn-glycero-3-phosphate + NADP+ = 1-hexadecanoylglycerone 3-phosphate + H+ + NADPH. [RHEA:17341] | null |
A contractile ring, i.e. a cytoskeletal structure composed of actin filaments and myosin, that forms beneath the plasma membrane at the mother-bud neck in mitotic cells that divide by budding in preparation for completing cytokinesis. An example of this structure is found in Saccharomyces cerevisiae. [GOC:krc, PMID:16009555] | null |
A protein complex peripherally associated with the plasma membrane that determines where vesicles dock and fuse. At least eight complex components are conserved between yeast and mammals. [GOC:cilia, PMID:15292201, PMID:27243008, PMID:9700152] | null |
A protein complex peripherally associated with the plasma membrane that determines where vesicles dock and fuse. At least eight complex components are conserved between yeast and mammals. [GOC:cilia, PMID:15292201, PMID:27243008, PMID:9700152] | null |
A protein complex that catalyzes the transfer of a glucose group from UDP-glucose to a (1->3)-beta-D-glucan chain. [PMID:7983071] | null |
A protein complex that catalyzes the transfer of a glucose group from UDP-glucose to a (1->3)-beta-D-glucan chain. [PMID:7983071] | null |
Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA. [GOC:elh] | null |
Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA. [GOC:elh] | null |
Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA. [GOC:elh] | null |
Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA. [GOC:elh] | null |
Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. [GOC:bf, GOC:mcc, PMID:10966457, PMID:20223701, PMID:31386843, PMID:9191038] | null |
Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. [GOC:bf, GOC:mcc, PMID:10966457, PMID:20223701, PMID:31386843, PMID:9191038] | null |
Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. [GOC:bf, GOC:mcc, PMID:10966457, PMID:20223701, PMID:31386843, PMID:9191038] | null |
Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response. [GOC:bf, PMID:10966457, PMID:11842140] | null |
A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. [GOC:mah, ISBN:0198547684, PMID:17245430] | null |
A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. [GOC:mah, ISBN:0198547684, PMID:17245430] | null |
A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. [GOC:mah, ISBN:0198547684, PMID:17245430] | null |
A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. [GOC:mah, ISBN:0198547684, PMID:17245430] | null |
The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. [GOC:mah, ISBN:0471331309, MetaCyc:TRPSYN-PWY] | null |
The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. [GOC:mah, ISBN:0471331309, MetaCyc:TRPSYN-PWY] | null |
The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. [GOC:mah, ISBN:0471331309, MetaCyc:TRPSYN-PWY] | null |
The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. [GOC:mah, ISBN:0471331309, MetaCyc:TRPSYN-PWY] | null |
The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. [GOC:mah, ISBN:0471331309, MetaCyc:TRPSYN-PWY] | null |
Catalysis of the site-specific cleavage of RNA by a catalytic RNA-mediated mechanism; substrates include the A3 site in the ITS1 of pre-rRNA. [PMID:17881380] | null |
A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication. [GOC:sgd_curators, PMID:10690410, PMID:14729943, PMID:7510714] | null |
A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication. [GOC:sgd_curators, PMID:10690410, PMID:14729943, PMID:7510714] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |
Catalysis of the reaction: NAD+ + H2O = AMP + NMN. [RHEA:11800] | null |