Spreadsheet: 21be9a43-55db-4626-9a16-dab4513f1748
Sheet: Sheet1

Enzyme | Reaction | Substrates / Inhibitors | Kinetic Mechanism | Km | kcat | KI | Acitivity (purified) | Hill coefficient | Species/tissue | Referrence | Comments
2.7.1.1 - Hexokinase | r1a | Glucose | Ordered bi-bi mechanism | 0.11 mM |  |  |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r1a | ATP (Binds before glucose) | Ordered bi-bi mechanism | 0.8 mM |  |  |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r1a | D-Glucose | Ordered bi-bi mechanism |  |  |  | 120 (µM/min/mg protein) |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r1a | ATP | Ordered bi-bi mechanism |  | 53.2 /s |  |  |  | 37°C, pH 7.4, mus musculus | [NAME]
2.7.1.1 - Hexokinase | r1a | Fructose (competitive with Glc) | Ordered bi-bi mechanism |  |  | 0.9 mM |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r1a | Glucosamine (competitive with Glc) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r1a | Mannose (competitive with Glc) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r1a | [NAME] (non-competitive with hexose) | Ordered bi-bi mechanism |  |  | 0.026 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r1a | [NAME] (non-competitive with ATP) | Ordered bi-bi mechanism |  |  | 0.015 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r1a | Glc6 (enzyme only) | Ordered bi-bi mechanism |  |  | 0.043 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r1a | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 3.5 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.2 - Glucokinase | r1c | D-glucose | Ordered mnemonical bi-bi | 6 mM |  |  | 80 µM/min/mg | 1.73 | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r1c | ATP | Ordered mnemonical bi-bi | 0.63 mM |  |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r1c | Glc6P (competitive with Hexose) | Ordered mnemonical bi-bi |  |  | 12 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r1c | GlcNAc (competitive with Hexose | Ordered mnemonical bi-bi |  |  | 0.2 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r1c | ADP (competitive with ATP) | Ordered mnemonical bi-bi |  |  | 9 mM |  |  | 30°C, pH 8.0, Rattus norvegicus, liver | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1164869/pdf/biochemj00507-0070.pdf
2.7.1.2 - Glucokinase | r1c | Mannose (competitive with Glc) |  |  |  | 4.4 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r1c |  |  |  | 66.7 /s |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/269/44/27458.full.pdf
5.3.1.9 - Glucose-6-phosphate isomerase | r2a |  | Push-pull mechanism (Michaelis-Menten) |  |  |  |  |  | [NAME] | http://www.ncbi.nlm.nih.gov/pubmed/15342241
5.3.1.9 - Glucose-6-phosphate isomerase | r2aF | Glucose-6-P | Push-pull mechanism (Michaelis-Menten) | 0.25 mM |  |  |  |  | 30C, pH 8.5, mus musculus, [NAME] ascites tumor cells | http://www.sciencedirect.com/science/article/pii/0014579373801668
5.3.1.9 - Glucose-6-phosphate isomerase | r2aF | D-Glucose-6-P | Push-pull mechanism (Michaelis-Menten) |  | 1000 /s |  |  |  | 30C, pH 7.5, homo sapiens, liver | http://www.sciencedirect.com/science/article/pii/S1570963908003531
5.3.1.9 - Glucose-6-phosphate isomerase | r2aB | D-Fructose-6-P | Push-pull mechanism (Michaelis-Menten) | 0.037 [NAME] | 650 /s |  |  |  | 30C, pH 7.5, homo sapiens, liver | http://www.sciencedirect.com/science/article/pii/S1570963908003531
2.6.1.16 - glutamine-fructose-6-phosphate transaminase | r3a | Glutamine (second to bind) | Ordered bi-bi mechanism | 0.8 mM | 1.08 /s (as calculated from specific activity) |  | 200 pmol/min/mg |  | 37°C, pH 7.5, rat, liver | http://www.sciencedirect.com/science/article/pii/S0003986100918952 | kcat based on homogeneous protein with a Mr of 75 kDa
2.6.1.16 - glutamine-fructose-6-phosphate transaminase | r3a | Fru-6-P (first to bind) | Ordered bi-bi mechanism | 0.4 mM |  |  |  |  | 37°C, pH 7.5, rat, liver | http://www.sciencedirect.com/science/article/pii/S0003986100918952
2.6.1.16 - glutamine-fructose-6-phosphate transaminase | r3a |  | Ordered bi-bi mechanism |  |  | 0.0183 mM |  |  | 37°C, pH 7.5, rat, liver | http://www.sciencedirect.com/science/article/pii/S0003986100918952
2.6.1.16 - glutamine-fructose-6-phosphate transaminase | r3a |  | Ordered bi-bi mechanism |  |  |  |  |  |  | http://www.sciencedirect.com/science/article/pii/S0167483802003187
3.5.99.6 - glucosamine-6-phosphate deaminase | r3b | GlcNAc-6-P (Allosteric activator of the V-type) | Bireactant sequential mechanism | 0.0175 mM | 61.6 /s |  |  |  | 30C, pH 7.7, bos taurus, kidney | http://www.sciencedirect.com/science/article/pii/S0167483898001411 | Michaelis-Menten activation kinetics
3.5.99.6 - glucosamine-6-phosphate deaminase | r3b | GlcN-6P | Bireactant sequential mechanism | 0.65 mM | 61.6 /s |  |  |  | 30C, pH 7.7, bos taurus, kidney | http://www.sciencedirect.com/science/article/pii/S0167483898001411
2.3.1.4 - glucosamine-phosphate N-acetyltransferase | r4a |  | [NAME] pong bi-bi mechanism |  |  |  |  |  | 37C, pH 7.4, rattus norvegicus | http://www-06.all-portland.net/bst/012/0656/0120656.pdf
2.3.1.4 - glucosamine-phosphate N-acetyltransferase | r4a | CoA (competitive with actyl-CoA | [NAME] pong bi-bi mechanism |  |  | 0.05 - 0.15 mM |  |  | 37C, pH 7.4, rattus norvegicus | http://www-06.all-portland.net/bst/012/0656/0120656.pdf
2.3.1.4 - glucosamine-phosphate N-acetyltransferase | r4a | GlcN-6-P | [NAME] pong bi-bi mechanism | 0.040 mM |  |  |  |  | 37°C, pH 7.5, mus musculus | http://www.jbc.org/content/275/17/12821.full.pdf+html
2.3.1.4 - glucosamine-phosphate N-acetyltransferase | r4a | acetyl-CoA | [NAME] pong bi-bi mechanism | 0.120 mM |  |  |  |  | 37°C, pH 7.5, mus musculus | http://www.jbc.org/content/275/17/12821.full.pdf+html
2.3.1.4 - glucosamine-phosphate N-acetyltransferase | r4a | GlcN-6-P | [NAME] pong bi-bi mechanism |  | 22.1 /s |  |  |  | 30C, pH 8.0, homo sapiens | http://www.sciencedirect.com/science/article/pii/S0014579308006406
3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase | r4b | GlcNAc-6-P | Michaelis-Menten | 0.029 mM | 0.04 /s |  | 1.4*10^6 cpm/h/mg |  | 37°C, pH 7.5, homo sapiens, erythrocyte | http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2141.1996.d01-1955.x/pdf | 16,000-fold purified was assumed to be pure enzyme
5.4.2.3 - phosphoacetylglucosamine mutase | r5aF | GlcNAc-6-P | [NAME] mechanism | 0.046 mM | 1.8 /s |  |  |  | 30°C, pH 8.3, homo sapiens, expressed in E. Coli | http://www.sciencedirect.com/science/article/pii/S0167478100001202
5.4.2.3 - phosphoacetylglucosamine mutase | r5aB | GlcNAc-1-P | [NAME] mechanism |  | 1.8 /s (assumed same as forward) |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | r5aB | GlcNAc-1-P | [NAME] mechanism | 0.024 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long | vm data read from graph in supplementary material
5.4.2.3 - phosphoacetylglucosamine mutase | r5aB | GlcNAc-1-P | [NAME] mechanism |  |  | 0.023 mM |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | r5aB | GlcNAc-1,6-P2 (intermediate) | [NAME] mechanism | 0.00038 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | r5aB | Glc-1,6-P2 (intermediate) | [NAME] mechanism | 0.028 [NAME] |  |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aF | UTP (binds second) | [NAME] mechanism | 0.42 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aF | GlcNAc-1-P (binds first) | [NAME] mechanism | 0.29 mM | 31 /s (as calculated from specific activity) |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html | kcat based on homogeneous protein with a Mr of 125kDa
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aF | GalNAc-1-P (competes with GlcNAc-1-P) | [NAME] mechanism |  |  | 1.1 mM |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aF | Glc-1-P (competes with GlcNAc-1-P) | [NAME] mechanism |  |  | 5.8 mM |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aF |  | [NAME] mechanism |  |  |  |  |  |  | http://www.jbc.org/content/273/23/14392.full.pdf
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aB | ADP | [NAME] mechanism | 0.79 mM |  |  |  |  | 37°C, pH 7.4, ovis aries, brain | http://www.brenda-enzymes.org/literature/lit.php4?e=2.7.7.23&r=643057
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aB | UDP-GlcNAc (5 mM Ppi) | [NAME] mechanism | 0.23 mM | 31 /s (assumed same as forward) |  |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aB | UDP-GalNAc (competes with UDP-GlcNAc) | [NAME] mechanism |  |  | 2.2 mM |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r6aB | UDP-Glc (competes with UDP-GlcNAc) | [NAME] mechanism |  |  | 6.3 mM |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase | r7a | Although activity has been reported in mammalian cells no kinetic data can be found for this enzyme |  |  |  |  | 200 nmol/hr/mg |  | 37°C, pH 8.4, CHO cells | http://www.sciencedirect.com/science/article/pii/009286748690841X
5.1.3.2 - UDP-glucose 4-epimerase | r7bB | UDP-GalNAc | Single substrate Michaelis-Menten mechanism |  | 26 /s (based on repored activity ratios and UDP-Gal turnover) |  | 36.4 µM/min/mg protein |  | 37°C, pH 8.7, homo sapiens, expressed in Saccharomyces | http://www.jbc.org/content/279/31/32796.full.pdf
5.1.3.2 - UDP-glucose 4-epimerase | r7bB | UDP-GalNAc | Single substrate Michaelis-Menten mechanism | 0.29 mM |  |  |  |  | 37°C, pH 8.7, homo sapiens, expressed in Saccharomyces | http://www.jbc.org/content/276/23/20617.full.pdf+html
5.1.3.2 - UDP-glucose 4-epimerase | r7bB | UDP-Gal | Single substrate Michaelis-Menten mechanism |  |  | 0.048 [NAME] |  |  | Homo sapiens, expressed in Saccharomyces | [NAME]
5.1.3.2 - UDP-glucose 4-epimerase | r7bF | UDP-GlcNAc | Single substrate Michaelis-Menten mechanism | 0.53 mM (based on UDP-GalNAc/UDP-GlcNAc ratio) | 26 /s (assumed same as forward) |  |  |  | 37°C, pH 7.8, CHO-K1 | http://onlinelibrary.wiley.com/doi/10.1002/bit.21816/abstract | An average UDP-GalNAc/UDP-GlcNAc of 0.551 was calculated
5.1.3.2 - UDP-glucose 4-epimerase | r7bF | UDP-GlcNAc | Single substrate Michaelis-Menten mechanism | UDP-Glc equilibrates 4-fold faster than UDP-GlcNAc |  |  |  |  | Homo sapiens | http://www.biochemj.org/bj/389/0173/3890173.pdf
5.1.3.2 - UDP-glucose 4-epimerase | r7bF | UDP-GlcNAc | Single substrate Michaelis-Menten mechanism | UDP-GlcNAc to UDP-GalNAc ratios during different stages of cell cycle |  |  |  |  | CHO | http://www.jbc.org/content/280/14/13493.full.pdf
5.1.3.2 - UDP-glucose 4-epimerase | r7bF | UDP-Glc | Single substrate Michaelis-Menten mechanism |  |  | 0.020 [NAME] |  |  | Homo sapiens, expressed in Saccharomyces | [NAME]
2.7.1.59 - N-acetylglucosamine kinase | r8a | GlcNAc | Random order (assumed) | 0.2 mM |  |  |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf | Activity: 12 (kidney), 4 (liver)
2.7.1.59 - N-acetylglucosamine kinase | r8a | ATP | Random order (assumed) | 0.5 mM |  |  |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf
2.7.1.59 - N-acetylglucosamine kinase | r8a | GlcNAc (co-operative kinetics) | Random order (assumed) |  |  |  |  | 1.54 | 32°C, pH 7.5, rattus norvegicus, kindey and liver | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1161433/pdf/biochemj00430-0042.pdf
2.7.1.59 - N-acetylglucosamine kinase | r8a | GlcNAc | Random order (assumed) |  | 68.1 /s |  | 52.4 μmol/min/mg |  | 37°C, pH 7.5, rattus norvegicus, liver | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.[PHONE].x/pdf | Obtained from specific activity data and Mr of 78 kDa
2.7.1.59 - N-acetylglucosamine kinase | r8a | ADP (competitive with ATP) | Random order (assumed) |  |  | 0.9 mM |  |  | 37°C, pH 9.0, sus scrofa, liver | http://www.sciencedirect.com/science/article/pii/0005274470902287
2.7.1.59 - N-acetylglucosamine kinase | r8a | ManNAc | Random order (assumed) |  |  | 4 mM |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf
2.7.1.2 - Glucokinase | r8b | GlcNAc | Ordered bi-bi mechanism | 0.20 mM |  |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long | No effect on co-operativity
2.7.1.2 - Glucokinase | r8b | ATP | Ordered bi-bi mechanism | 0.63 mM |  |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r8b | D-glucose (competitive with Hexose) | Ordered bi-bi mechanism |  |  | 6.0 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r8b | Glc6P (competitive with Hexose) | Ordered bi-bi mechanism |  |  | 12 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long | No effect on co-operativity
2.7.1.2 - Glucokinase | r8b | Mannose (competitive with Hexose) | Ordered bi-bi mechanism |  |  | 4.4 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r8b | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 9.0 mM |  |  | 30°C, pH 8.0, Rattus norvegicus, liver | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1164869/pdf/biochemj00507-0070.pdf | No effect on co-operativity
2.7.1.2 - Glucokinase | r8b |  |  |  | 66.7 /s |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/269/44/27458.full.pdf
3.5.1.33 - N-acetylglucosamine deacetylase | r9a | Although reported in mammalian cells no kinetic data can be found for this enzyme |  |  |  |  |  |  |  | http://www.jbc.org/content/266/14/8671.long
2.3.1.3 - Glucosamine N-acetyltransferase | r9b | Although reported in pidgeons no kinetic data can be found for this enzyme |  |  |  |  |  |  |  | http://www.jbc.org/content/196/1/105.long
2.7.1.1 - Hexokinase | r10a | Glucosamine | Ordered bi-bi mechanism | 0.06 [NAME] | 53.2 /s (assumed to be the same as for Glc) |  |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r10a | ATP (Binds before glucose) | Ordered bi-bi mechanism | 0.8 mM |  |  |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r10a | D-Glucose | Ordered bi-bi mechanism |  |  |  | 120 (µM/min/mg protein) |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r10a | ATP | Ordered bi-bi mechanism |  |  |  |  |  | 37°C, pH 7.4, mus musculus | [NAME]
2.7.1.1 - Hexokinase | r10a | Glucose (competitive with GlcN) | Ordered bi-bi mechanism |  |  | 0.11 mM |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r10a | Fructose (competitive with GlcN) | Ordered bi-bi mechanism |  |  | 0.9 mM |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r10a | Mannose (competitive with GlcN) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r10a | [NAME] (non-competitive with hexose) | Ordered bi-bi mechanism |  |  | 0.026 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r10a | [NAME] (non-competitive with ATP) | Ordered bi-bi mechanism |  |  | 0.015 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r10a | Glc6 (enzyme only) | Ordered bi-bi mechanism |  |  | 0.043 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r10a | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 3.5 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r11a | Fructose | Ordered bi-bi mechanism | 0.9 mM | 53.2 /s (assumed to be the same as for Glc) |  |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r11a | ATP (Binds before glucose) | Ordered bi-bi mechanism | 0.8 mM |  |  |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r11a | D-Glucose | Ordered bi-bi mechanism |  |  |  | 120 (µM/min/mg protein) |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r11a | ATP | Ordered bi-bi mechanism |  |  |  |  |  | 37°C, pH 7.4, mus musculus | [NAME]
2.7.1.1 - Hexokinase | r11a | Glucose (competitive with Fru) | Ordered bi-bi mechanism |  |  | 0.11 mM |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r11a | Glucosamine (competitive with Fru) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r11a | Mannose (competitive with Fru) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r11a | [NAME] (non-competitive with hexose) | Ordered bi-bi mechanism |  |  | 0.026 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r11a | [NAME] (non-competitive with ATP) | Ordered bi-bi mechanism |  |  | 0.015 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r11a | Glc6 (enzyme only) | Ordered bi-bi mechanism |  |  | 0.043 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r11a | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 3.5 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.52 - Fucokinase | r12a | L-fucose (at 5mM ATP) | Random order bi-bi (assumed) | 0.027 mM | 9.3 /s |  | 1270 nmol/min/mg |  | 37°C, pH 8.0, sus scrofa, kidney | http://www.jbc.org/content/273/10/5685.full.pdf+html | kcat obtained from specific activity assumed to be of homogeneous enzyme and an Mr of 440kDa
2.7.1.52 - Fucokinase | r12a | ATP (at 0.1 mM Fucose) | Random order bi-bi (assumed) | 0.6 mM |  |  |  |  | 37°C, pH 8.0, sus scrofa, kidney | http://www.jbc.org/content/273/10/5685.full.pdf+html
2.7.1.52 - Fucokinase | r12a | GDP-fucose (data suggest non-competitive inhibition) | Random order bi-bi (assumed) |  |  | 0.01 mM |  |  | 37°C, pH 8.0, sus scrofa, kidney | http://www.jbc.org/content/273/10/5685.full.pdf+html
2.7.1.52 - Fucokinase | r12a | Michaelis-Menten kinetics | Random order bi-bi (assumed) |  |  |  |  |  | 37°C, rattus norvegicus, liver | http://informahealthcare.com/doi/abs/10.3109/14756369709027655
2.7.7.30 - fucose-1-phosphate guanylyltransferase | [NAME] | Fucose-1-P | [NAME] mechanism (assumed) | 0.067 [NAME] | 3.6 /s |  |  |  | 37°C, pH 7.0, homo sapiens, liver | http://pubs.acs.org/doi/abs/10.1021/bi0503605 | different kcat values and analogy to UDP-GlcNAc point towards ping-pong mechanism
2.7.7.30 - fucose-1-phosphate guanylyltransferase | [NAME] | GTP | [NAME] mechanism (assumed) | 0.05 mM | 2.5 /s |  |  |  | 37°C, pH 7.0, homo sapiens, liver | http://pubs.acs.org/doi/abs/10.1021/bi0503605
2.7.7.30 - fucose-1-phosphate guanylyltransferase | r13aB | GDP-fucose | [NAME] mechanism (assumed) | 0.120 mM | (overall value assumed to be same as forward) |  |  |  | 37°C, pH 7.8, sus scrofa, kidney | http://www.jbc.org/content/273/46/30165.full.pdf+html | Activity data seems to appear as two parallel lines suggesting a ping-pong mechanism
2.7.7.30 - fucose-1-phosphate guanylyltransferase | r13aB | PPi | [NAME] mechanism (assumed) | 0.135 mM |  |  |  |  | 37°C, pH 7.8, sus scrofa, kidney | http://www.jbc.org/content/273/46/30165.full.pdf+html | Overall kcat=(kF*kG/(kF+kG)) = 1.5 /s
1.1.1.271 - GDP-L-fucose synthase | r14a | GDP-4-keto-6-deoxy-D-mannose | [NAME] mechanism | 0.014 mM | 0.20 /s (from activity) |  | 194 nmol/min/mg |  | 37°C, pH 7, sus scrofa | http://www.jbc.org/content/263/4/1693.full.pdf | Apparent homogeneity of protein and an Mr of 63.1 kDa
1.1.1.271 - GDP-L-fucose synthase | r14a | NADPH | [NAME] mechanism | 0.023 mM |  |  |  |  | 37°C, pH 7.8, sus scrofa, kidney | http://www.jbc.org/content/263/4/1693.full.pdf
1.1.1.271 - GDP-L-fucose synthase | r14a | NADPH (substrate inhibition at high concentrations) | [NAME] mechanism |  |  |  |  |  | 37°C, pH 7.8, sus scrofa, kidney | http://www.jbc.org/content/263/4/1693.full.pdf
4.2.1.47 - GDP-mannose 4,6-dehydratase | r15a | GDP-Mannose | Random order bi-bi (assumed) | 0.0035 mM |  |  | 700 nmol/min/mg |  | 37°C, pH 8.0, homo sapiens, expressed in E. Coli | http://www.sciencedirect.com/science/article/pii/S0014579398006152
4.2.1.47 - GDP-mannose 4,6-dehydratase | r15a | NADP | Random order bi-bi (assumed) | 0.0036 mM | 0.8 /s |  |  |  | 37°C, pH 8.0, homo sapiens, expressed in E. Coli | http://www.sciencedirect.com/science/article/pii/S0014579399009825
4.2.1.47 - GDP-mannose 4,6-dehydratase | r15a | GDP-L-fucose (non-competitive inhibition) | Random order bi-bi (assumed) |  |  | 0.011 mM |  |  | 37°C, pH 8.0, homo sapiens, expressed in E. Coli | http://www.sciencedirect.com/science/article/pii/S0014579399009825
2.7.7.13 - mannose-1-phosphate guanylyltransferase | r16aF | Mannose-1-P | [NAME] mechanism (assumed to be the same as for r6a and r14a) | 0.13 mM | 78 /s (based on Keq) |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/268/24/17943.long | Keq = 0.38 = (GDP-Man*Ppi)/(GTP*Man-1P)
2.7.7.13 - mannose-1-phosphate guanylyltransferase | r16aF | GTP | [NAME] mechanism (assumed to be the same as for r6a and r14a) | 0.10 [NAME] |  |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/268/24/17943.long
2.7.7.13 - mannose-1-phosphate guanylyltransferase | r16aF | Glucose-1-P (competitive with Man-1P) | [NAME] mechanism (assumed to be the same as for r6a and r14a) |  |  | 2.5 mM |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/268/24/17943.long
2.7.7.13 - mannose-1-phosphate guanylyltransferase | [NAME] | GDP-mannose | [NAME] mechanism (assumed to be the same as for r6a and r14a) | 0.020 [NAME] | 69 /s (from activity) |  | 9250 nmol/min/mg |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/268/24/17943.long
2.7.7.13 - mannose-1-phosphate guanylyltransferase | [NAME] | PPi | [NAME] mechanism (assumed to be the same as for r6a and r14a) | 0.031 [NAME] |  |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/268/24/17943.long | Apparent homogeneity of protein and Mr of 450 kDa
5.4.2.8 - phosphomannomutase | r17aF | Man-6-P | Single substrate M-M with allosteric activator | 0.074 mM | 24 /s (assumed same as backward) |  |  |  | Oryctolagus cuniculus | http://www.brenda-enzymes.info/literature/lit.php4?e=5.4.2.8&r=3352
5.4.2.8 - phosphomannomutase | r17aF | Glucose-6-P (competitive with Man-6P) | Single substrate M-M with allosteric activator |  | 0.049 mM (assumed same ratio as Man6P to Man1P) |  |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/
5.4.2.8 - phosphomannomutase | [NAME] | Mannose-1-P | Single substrate M-M with allosteric activator | 0.018 [NAME] | 24 /s (from activity) |  | 49 000 nmol/min/mg |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/ | Apparent homogeneity of protein and Mr of 28 kDa
5.4.2.8 - phosphomannomutase | [NAME] | Glucose-1-P (competitive with Man-1P) | Single substrate M-M with allosteric activator |  | 0.012 mM |  |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/
5.4.2.8 - phosphomannomutase | [NAME] | Hex-1,6-PP co-substrate required for activation | Single substrate M-M with allosteric activator | 0.00046 mM (Kdiss) |  |  |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/pdf/10085245.pdf | 0.30 mol/mol phosphorylation stoichometry
2.7.1.1 - Hexokinase | r18a | Mannose | Ordered bi-bi mechanism | 0.06 [NAME] |  |  |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r18a | ATP (Binds before glucose) | Ordered bi-bi mechanism | 0.8 mM |  |  |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r18a | D-Glucose | Ordered bi-bi mechanism |  |  |  | 120 µM/min/mg protein |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r18a | ATP | Ordered bi-bi mechanism |  | 53.2 /s (assumed same for Man reactio) |  |  |  | 37°C, pH 7.4, mus musculus | [NAME]
2.7.1.1 - Hexokinase | r18a | Glucose (competitive with Man) | Ordered bi-bi mechanism |  |  | 0.11 mM |  |  | 29°C, pH 8.0, rattus norvegicus, skeletal muscle | http://www.biochemj.org/bj/100/0739/1000739.pdf
2.7.1.1 - Hexokinase | r18a | Fructose (competitive with Man) | Ordered bi-bi mechanism |  |  | 0.9 mM |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r18a | Glucosamine (competitive with Man) | Ordered bi-bi mechanism |  |  | 0.06 [NAME] |  |  | 30°C, pH 7.5, rattus norvegicus, skeletal muscle | http://www.sciencedirect.com/science/article/pii/S0076687982900982
2.7.1.1 - Hexokinase | r18a | [NAME] (non-competitive with hexose) | Ordered bi-bi mechanism |  |  | 0.026 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r18a | [NAME] (non-competitive with ATP) | Ordered bi-bi mechanism |  |  | 0.015 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r18a | Glc6 (enzyme only) | Ordered bi-bi mechanism |  |  | 0.043 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.1 - Hexokinase | r18a | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 3.5 mM |  |  | 30°C, pH 7.5, Rattus norvegicus | http://ac.els-cdn.com/S0076687982900982/1-s2.0-S0076687982900982-main.pdf?_tid=06f150b839f8719f984c766779abb6de&acdnat=1336482973_8a49f0e1aa7bef0ec914ad9555cbd118
2.7.1.2 - Glucokinase | r18b | Mannose | Ordered bi-bi mechanism | 4.4 mM |  |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r18b | ATP | Ordered bi-bi mechanism | 0.63 mM |  |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r18b | D-glucose (competitive with Hexose) | Ordered bi-bi mechanism |  |  | 6.0 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r18b | Glc6P (competitive with Hexose) | Ordered bi-bi mechanism |  |  | 12 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r18b | GlcNAc (competitive with Hexose | Ordered bi-bi mechanism |  |  | 0.20 mM |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/270/17/9939.long
2.7.1.2 - Glucokinase | r18b | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 9.0 mM |  |  | 30°C, pH 8.0, Rattus norvegicus, liver | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1164869/pdf/biochemj00507-0070.pdf
2.7.1.2 - Glucokinase | r18b |  |  |  | 66.7 /s |  |  |  | 30°C, pH 7.5, [NAME], liver | http://www.jbc.org/content/269/44/27458.full.pdf
5.3.1.8 - Mannose-6-phosphate isomerase | 19aF | Fru-6P | Single substrate Michaelis-Menten kinetics (assumed) | 0.031 [NAME] | 56 /s (assumed same as backward) |  |  |  | 25°C, pH 8.0, oryctolagus cuniculus, skeletal muscle | http://www.jbc.org/content/235/8/2178.long
5.3.1.8 - Mannose-6-phosphate isomerase | 19aF | Fru-6P | Single substrate Michaelis-Menten kinetics (assumed) | 0.10 [NAME] |  |  |  |  | 25°C, pH 8.0, oryctolagus cuniculus, skeletal muscle | http://www.jbc.org/content/235/8/2178.long
5.3.1.8 - Mannose-6-phosphate isomerase | 19aB | Man-6-P | Single substrate Michaelis-Menten kinetics (assumed) | 0.25 mM | 56 /s (from activity) |  | 75 µM/min/mg protein |  | 37°C, pH 8.0, homo sapiens, placenta | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1994.tb19954.x/pdf | Apparent homogeneity of protein and Mr of 45 kDa
5.3.1.8 - Mannose-6-phosphate isomerase | 19aB | Fru-1P (competitive inhibitor) | Single substrate Michaelis-Menten kinetics (assumed) |  |  | 0.03 mM |  |  | 30°C, pH 7.1, rattus norvegicus, liver | http://www.nature.com/pr/journal/v40/n5/full/pr19962957a.html
2.7.1.6 - galactokinase | r20a | galactose (second to bind) | Ordered bi-bi mechanism | 0.97 | 8.7 /s |  |  |  | 37°C, pH 8.0, homo sapiens | http://www.sciencedirect.com/science/article/pii/S016816560900128X
2.7.1.6 - galactokinase | r20a | ATP (first to bind) | Ordered bi-bi mechanism | 0.034 |  |  |  |  | 37°C, pH 8.0, homo sapiens | http://www.sciencedirect.com/science/article/pii/S016816560900128X
2.7.1.6 - galactokinase | r20a | Gal-1-P (uncompetitive with respect to ATP) | Ordered bi-bi mechanism |  |  | 39 mM |  |  | 37°C, pH 8.0, homo sapiens | http://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=2003&volume=270&issue=8&spage=1767
2.7.1.6 - galactokinase | r20a | Gal-1-P (uncompetitive with respect to [NAME]) | Ordered bi-bi mechanism |  |  | 28 mM |  |  | 37°C, pH 8.0, homo sapiens | http://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=2003&volume=270&issue=8&spage=1767
2.7.1.6 - galactokinase | r20a | ADP (competitive with ATP) | Ordered bi-bi mechanism |  |  | 0.2 mM |  |  | 37°C, pH 7.8, sus scrofa, liver | http://www.sciencedirect.com/science/article/pii/0076687975420900
2.7.1.6 - galactokinase | r20a | AMP | Ordered bi-bi mechanism |  |  | 10.2 mM |  |  | 34°C, pH 7.5, rattus norvegicus, liver | http://www.sciencedirect.com/science/article/pii/S016816560900128X
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | Galactose-1-P (second to bind) | Ordered bi-bi mechanism | 7.3 mM | 170 /s (assumed same as backwards) |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | Galactose-1-P (second to bind) | Ordered bi-bi mechanism | 1.9 mM | 170 /s (assumed same as backwards) |  |  |  | 25°C, pH 8.0, homo sapiens, transfected cell line | http://glycob.oxfordjournals.org/content/13/4/285.full.pdf
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | UTP (First to bind) | Ordered bi-bi mechanism | 0.038 mM |  |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | Glucose 1-P (competitive with Gal-1P) | Ordered bi-bi mechanism |  |  | 0.046 mM |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | UDP-Galactose (competitive with Gal-1P) | Ordered bi-bi mechanism |  |  | 0.22 mM |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r21aB | UDP-Galactose | Ordered bi-bi mechanism | 0.22 mM | 170 /s (from activity) |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r21aB | PPi | Ordered bi-bi mechanism | 0.21 mM |  |  |  |  | 32°C, pH 8.0, homo sapiens, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r21aB | UDP-glucose (competitive with UDP-Gal) | Ordered bi-bi mechanism |  |  | 0.066 mM | 200 µM/min/mg protein |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long | Apparent homogeneity of protein and Mr of 50kDa
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r21aB | Galactose-1-P (competitive with UDP-Gal) | Ordered bi-bi mechanism |  |  | 1.9 mM |  |  | 25°C, pH 8.0, homo sapiens, transfected cell line | http://glycob.oxfordjournals.org/content/13/4/285.full.pdf
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r21a |  | Ordered bi-bi mechanism |  |  |  |  |  | Homo sapiens and bos taurus | http://www.jbc.org/content/246/8/2551.full.pdf
5.1.3.2 - UDP-glucose 4-epimerase | r22aF | UDP-Gal | Single substrate Michaelis-Menten mechanism |  | 6 /s (assumed same as backwards) |  |  |  | 37°C, pH 8.8, homo sapiens, | [NAME]
5.1.3.2 - UDP-glucose 4-epimerase | r22aF | UDP-Gal | Single substrate Michaelis-Menten mechanism | 0.048 [NAME] |  |  |  |  | 37°C, pH 7.5, homo sapiens, | [NAME]
5.1.3.2 - UDP-glucose 4-epimerase | r22aF | UDP-galactose | Single substrate Michaelis-Menten mechanism |  | 36 /s |  |  |  | 37°C, pH 8.8, homo sapiens | http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2005.05017.x/pdf
5.1.3.2 - UDP-glucose 4-epimerase | r22aF | UDP-GalNAc (competes with UDP-Gal) | Single substrate Michaelis-Menten mechanism |  |  | 0.29 mM |  |  | 37°C, pH 8.7, homo sapiens, expressed in Saccharomyces | http://www.jbc.org/content/279/31/32796.full.pdf
5.1.3.2 - UDP-glucose 4-epimerase | [NAME] | UDP-Glc | Single substrate Michaelis-Menten mechanism | Estimated |  |  |  |  | Homo sapiens, expressed in Saccharomyces | http://www.sciencedirect.com/science/article/pii/S1074552102000935
5.1.3.2 - UDP-glucose 4-epimerase | [NAME] | UDP-GlcNAc (competes with UDP-Glc) | Single substrate Michaelis-Menten mechanism |  |  | 0.53 mM (based on UDP-GalNAc/UDP-GlcNAc ratio) |  |  | 37°C, pH 7.8, CHO-K1 | http://onlinelibrary.wiley.com/doi/10.1002/bit.21816/abstract | An average UDP-GalNAc/UDP-GlcNAc of 0.551 was calculated
2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase | [NAME] | UDP-Glucose | Bi-bi double displacement reaction (following ping pong kinetics) | 0.6 mM ([NAME]) | 98 /s |  |  |  | 37°C, pH 8.7, homo sapiens, expressed in yeast | http://www.jbc.org/content/275/30/22847.full.pdf+html
2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase | [NAME] | UDP-Glucose | Bi-bi double displacement reaction (following ping pong kinetics) | 0.2 mM (Kia) |  |  |  |  | 37°C, pH 8.7, homo sapiens, expressed in yeast | http://www.jbc.org/content/275/30/22847.full.pdf+html
2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase | [NAME] | Gal-1-P | Bi-bi double displacement reaction (following ping pong kinetics) | 0.4 mM (Kb) |  |  |  |  | 37°C, pH 8.7, homo sapiens, expressed in yeast | http://www.jbc.org/content/275/30/22847.full.pdf+html
5.4.2.8 - phosphomannomutase | [NAME] | Glucose-6-P | [NAME] mechanism | 0.049 mM (assumed same ratio as Man6P to Man1P) | 1.2 /s (assumed same as backward) |  |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/
5.4.2.8 - phosphomannomutase | [NAME] | Mannose-6-P (competitive with Glc-6P) | [NAME] mechanism |  |  | 0.074 mM |  |  | Oryctolagus cuniculus | http://www.brenda-enzymes.info/literature/lit.php4?e=5.4.2.8&r=3352
5.4.2.8 - phosphomannomutase | r26aB | Glucose-1-P | [NAME] mechanism | 0.012 mM | 1.2 /s (20 times less activity than Man-1P) |  |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/
5.4.2.8 - phosphomannomutase | r26aB | Mannose-1-P (competitive with Glc-1P) | [NAME] mechanism |  |  | 0.018 [NAME] |  |  | 30°C, pH 7.1, homo sapiens, lymphocytes | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220145/ | Apparent homogeneity of protein and Mr of 28 kDa
5.4.2.8 - phosphomannomutase | r26a | hex-1,6-PP co-substrate required for activation | [NAME] mechanism | 0.003 mM |  |  |  |  | Mammals | [NAME] | Acitvation assumed to be not limiting
5.4.2.2 - phosphoglucomutase | r26bF | Glucose-6-P | Single substrate Michaelis-Menten mechanism | 0.057 mM | 57 /s |  |  |  | 30°C, pH 7.4, Oryctolagus cuniculus, liver | http://www.sciencedirect.com/science/article/pii/S0003269704002258
5.4.2.2 - phosphoglucomutase | r26bB | Glucose-1-P | Single substrate Michaelis-Menten mechanism | 0.011 mM | 181 /s |  | 160 µM/min/mg |  | 37°C, pH 7.4, Oryctolagus cuniculus, liver | http://www.sciencedirect.com/science/article/pii/S0003269704002258
5.4.2.3 - phosphoacetylglucosamine mutase | [NAME] | Glc-6-P | [NAME] mechanism | 1.3 mM (assumed same ratio as GlcNAc-1P to GlcNAc-6P) | 1.8 /s (assumed same as for GlcNAc-6P) |  |  |  | 30°C, pH 8.3, homo sapiens, erythrocyte | http://www.sciencedirect.com/science/article/pii/S0167478100001202
5.4.2.3 - phosphoacetylglucosamine mutase | [NAME] | Glc-1,6-P (intermediate) | [NAME] mechanism | 0.278 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | [NAME] | GlcNAc-1,6-P2 | [NAME] mechanism |  |  | 0.00083 |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | [NAME] | GlcNAc-6-P | [NAME] mechanism |  |  | 0.046 mM |  |  | 30°C, pH 8.3, homo sapiens, expressed in E. Coli | http://www.sciencedirect.com/science/article/pii/S0167478100001202
5.4.2.3 - phosphoacetylglucosamine mutase | r26cB | Glc-1-P | [NAME] mechanism | 0.66 mM | 1.8 /s (assumed same as forward) |  |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
5.4.2.3 - phosphoacetylglucosamine mutase | r26cB | GlcNAc-1-P | [NAME] mechanism |  |  | 0.023 mM |  |  | 37°C, pH 7.5, sus scrofa, submaxillary gland | http://www.jbc.org/content/254/17/8353.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r27aF | Glucose 1-P (second to bind) | Ordered bi-bi mechanism | 0.046 mM | 170 /s (assumed same as backward) |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r27aF | UTP (first to bind) | Ordered bi-bi mechanism | 0.038 mM |  |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r27aF | Galactose-1-P | Ordered bi-bi mechanism |  |  | 7.3 mM |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r27aF | Galactose-1-P | Ordered bi-bi mechanism |  |  | 0.47 mM |  |  | 25°C, pH 8.0, homo sapiens, transfected cell line | http://glycob.oxfordjournals.org/content/13/4/285.full.pdf
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | UDP-glucose | Ordered bi-bi mechanism | 0.066 mM | 170 /s (from activity) |  |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | PPi | Ordered bi-bi mechanism | 0.21 mM |  |  |  |  | 32°C, pH 8.0, homo sapiens, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | [NAME] | UDP-Galactose | Ordered bi-bi mechanism |  |  | 0.22 mM |  |  | 32°C, pH 8.0, Oryctolagus cuniculus, liver | http://www.jbc.org/content/249/23/7695.long
2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase | r27a |  | Ordered bi-bi mechanism |  |  |  |  |  | Homo sapiens and bos taurus | http://www.jbc.org/content/246/8/2551.full.pdf
1.1.1.22 - UDP-glucose 6-dehydrogenase | r28a | UDP-Glucose | Rate constant 110.7 nmol/min/mg | 0.011 mM | 0.10 /s |  | 110 nmol/min/mg |  | room temp, ph 7.4, homo sapiens, expressed in E. Coli | http://www.jbc.org/content/279/22/23590.full.pdf | Apparent homogeneity of protein and Mr of 57 kDa
1.1.1.22 - UDP-glucose 6-dehydrogenase | r28a | NAD+ |  | 0.355 [NAME] |  |  |  |  | room temp, ph 7.4, homo sapiens, expressed in E. Coli | http://www.jbc.org/content/279/22/23590.full.pdf
 |  | UDP-GlcA is a weak competitive inhibitor with respect to UDP-Glc |  |  |  |  |  |  |  | http://www.brenda-enzymes.info/literature/lit.php4?e=1.1.1.22&r=286296
5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase | r29a | UDP-GlcNAc | Single substrate Michaelis-Menten kinetics (ordered two step mechanism) | 0.011 mM | 2.3 /s (based on activity) |  |  | 0.45 | 37°C, pH 7.5, rattus norvegicus | http://www.jbc.org/content/272/39/24313.full.pdf | Based on homogeneous hexamer structure and Mr of 75kDa for monomer
5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase | r29a | CMP-Neu5Ac (non-competitive) | Single substrate Michaelis-Menten kinetics (ordered two step mechanism) |  |  |  |  |  | [NAME], pH 7.4, rattus norvegicus | http://www.pnas.org/content/52/2/371.full.pdf | Co-operative inhibition kinetics are not taken into account due to lack of data
5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase | r29a | CMP-Neu5Ac (non-competitive) | Single substrate Michaelis-Menten kinetics (ordered two step mechanism) |  |  | 0.025 |  | 4.1 | 37°C, pH 7.5, rattus norvegicus | http://www.jbc.org/content/272/39/24313.full.pdf
2.7.1.59 - N-acetylglucosamine kinase | r30a | ManNAc | Random order bi-bi (assumed) | 4 mM | 68.1 /s (assumed same as for GlcNAc) |  |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf
2.7.1.59 - N-acetylglucosamine kinase | r30a | ATP | Random order bi-bi (assumed) | 0.5 mM |  |  |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf
2.7.1.59 - N-acetylglucosamine kinase | r30a | ADP (competitive with ATP) | Random order bi-bi (assumed) |  |  | 0.9 mM |  |  | 37°C, pH 9.0, sus scrofa, liver | http://www.sciencedirect.com/science/article/pii/0005274470902287
2.7.1.59 - N-acetylglucosamine kinase | r30a | GlcNAc | Random order bi-bi (assumed) |  |  | 0.2 mM |  |  | 37°C, pH 7.5, mus musculus, spleen | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01360.x/pdf | Activity: 12 (kidney), 4 (liver)
2.7.1.59 - N-acetylglucosamine kinase | r30a | GlcNAc (co-operative inhibition) | Random order bi-bi (assumed) |  |  |  |  | 1.54 | 32°C, pH 7.5, rattus norvegicus, kindey and liver | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1161433/pdf/biochemj00430-0042.pdf
2.7.1.60 - N-acylmannosamine kinase | r30b | ManNAc | Random order bi-bi (assumed) | 0.093 mM | 5.1 /s (based on activity) |  |  | 1.42 | 37°C, pH 7.5, rattus norvegicus, liver | http://www.jbc.org/content/272/39/24313.full.pdf | Based on homogeneous hexamer structure and Mr of 75kDa for monomer
2.7.1.60 - N-acylmannosamine kinase | r30b | ATP | Random order bi-bi (assumed) | 1.2 mM |  |  |  | 1.3 | 37°C, pH 7.5, rattus norvegicus, liver | http://www.jbc.org/content/272/39/24313.full.pdf
2.5.1.57 - N-acylneuraminate-9-phosphate synthase | r31a | ManNAc-6-P | Random order bi-bi (assumed) | 0.035 [NAME] | 0.30 /s |  | 505 nmol/min/mg |  | 37°C, pH 7.5, rattus norvegicus, liver | http://glycob.oxfordjournals.org/content/12/2/65.full.pdf+html | Apparent homogeneity of protein and Mr of 37 [NAME]
2.5.1.57 - N-acylneuraminate-9-phosphate synthase | r31a | Phosphoenolpyruvate (PEP) | Random order bi-bi (assumed) | 0.105 mM |  |  |  |  | 37°C, pH 7.5, rattus norvegicus, liver | http://glycob.oxfordjournals.org/content/12/2/65.full.pdf+html
3.1.3.29 - N-acylneuraminate-9-phosphatase | r32a | Neu5Ac-9-P | Single substrate Michaelis-Menten kinetics | 0.09 mM | 56 /s |  |  |  | 37°C, pH 7.4, homo sapiens, liver | http://glycob.oxfordjournals.org/content/16/2/165.full.pdf+html
2.7.7.43 - N-acylneuraminate cytidylyltransferase | r33a | Neu5Ac | Random order bi-bi (assumed) | 1.3 mM | 1.9 /s (purification by 241-fold) |  |  |  | 37°C, pH 8.0, rattus norvegicus, liver | http://www.jbc.org/content/267/13/9257.long | Apparent homogeneity of protein and Mr of 58 kDa
2.7.7.43 - N-acylneuraminate cytidylyltransferase | r33a | CTP | Random order bi-bi (assumed) | 1.5 mM |  |  |  |  | 37°C, pH 8.0, rattus norvegicus, liver | http://www.jbc.org/content/267/13/9257.long
1.14.18.2 - N-acetylneuraminate monooxygenase | r34a | CMP-Neu5Ac | Single substrate Michaelis-Menten kinetics | 0.005 mM | 7.3 /s (from activity) |  | 6800 nmol/min/mg |  | 37°C, pH 7.5, mus musculus, liver | http://www.jbc.org/content/269/12/9024.full.pdf | Apparent homogeneity of protein and Mr of 64 kDa,
1.14.18.2 - N-acetylneuraminate monooxygenase | r34a | CMP-Neu5Ac | Single substrate Michaelis-Menten kinetics | 0.0055 mM | 0.13 /s (from activity) |  | 126 nmol/min/mg |  | 37°C, pH 7.4, mus musculus, liver | http://www.springerlink.com/content/u14266135173862p/fulltext.pdf | CMP-Neu5Ac levels may be controlled by varying the amount of enzyme concentration
1.14.18.2 - N-acetylneuraminate monooxygenase | r34a | cytochrome b5 | Single substrate Michaelis-Menten kinetics | 0.00024 mM |  |  |  |  | 37°C, pH 7.5, mus musculus, sus scorfa | http://glycob.oxfordjournals.org/content/4/5/675 | cytochrome [NAME] was not taken into account although rate-limiting in vitro
 |  | Fraction of CMP-Neu5Gc in different bovine tissues |  |  |  |  |  |  |  | http://ac.els-cdn.com/S0008621500906232/1-s2.0-S0008621500906232-main.pdf?_tid=04c7f4095054418be0253d8d5abeddc3&acdnat=1338379521_b563b86160283e405d51ff1f3377300a
 |  | Fraction of CMP-Neu5Gc in rat and mouse liver |  |  |  |  |  |  |  | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1990.tb19391.x/pdf
 |  | Weak product inhibition through Neu5Gc in mouse |  |  |  |  |  |  |  | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1992.tb16925.x/pdf
 |  | Biosynthesis of sialic acids in murine myeloma cells (90% Neu5Gc at steady state) |  |  |  |  |  |  |  | http://www.jbc.org/content/264/34/20216.full.pdf
4.1.3.3 - N-acetylneuraminate lyase | r37a | Neu5Ac | Single substrate Michaelis-Menten kinetics | 1.7 mM | 0.93 /s |  | 1548 nmol/min/mg |  | 37°C, pH 7.4, sus scrofa, liver | http://www.springerlink.com/content/g6w13635t1u4n70j/ | Apparent homogeneity of protein and Mr of 36 [NAME]
4.1.3.3 - N-acetylneuraminate lyase | r37a | pyruvate (competitive) | Single substrate Michaelis-Menten kinetics |  |  | 1.2 mM |  |  | 37°C, pH 7.4, homo sapiens | http://www.sciencedirect.com/science/article/pii/S0300908402014360
5.1.3.8 - N-Acylglucosamine 2-epimerase | r38aF | ManNAc | Single substrate Michaelis-Menten kinetics | 12.8 mM | 27 /s (from activity) |  | 35800 nmol/min/mg |  | 37°C, pH 7.5, homo sapiens, kidney | http://jb.oxfordjournals.org/content/125/2/348.long
5.1.3.8 - N-Acylglucosamine 2-epimerase | r38aB | GlcNAc | Single substrate Michaelis-Menten kinetics | 21.3 mM | 3.4 /s (from activity ratio) |  |  |  | 37°C, pH 7.5, homo sapiens, kidney | http://jb.oxfordjournals.org/content/125/2/348.long | Apparent homogeneity of protein and Mr of 45 kDa
5.1.3.8 - N-Acylglucosamine 2-epimerase | r38a | ATP (activator) | Single substrate Michaelis-Menten kinetics | 0.13 mM |  |  |  |  | 37°C, pH 7.5, homo sapiens, kidney | http://jb.oxfordjournals.org/content/125/2/348.long
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aF | UTP (binds second) | [NAME] mechanism | 0.42 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aF | GalNAc-1-P (binds first) | [NAME] mechanism | 1.1 mM |  |  |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aF | GalNAc-1-P | [NAME] mechanism |  | 73 /s (as calculated from specific activity) |  |  |  |  | http://www.jbc.org/content/275/2/1433.full.pdf
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aF | GlcNAc-1-P (competes with GalNAc-1-P) | [NAME] mechanism |  |  | 0.29 mM |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aF | Glc-1-P (competes with GalNAc-1-P) | [NAME] mechanism |  |  | 5.8 mM |  |  | 37°C, pH 7.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aB | UDP-GalNAc | [NAME] mechanism | 2.2 mM | 73 /s (assumed same as for GalNAc-1P) |  |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aB | ADP | [NAME] mechanism | 0.79 mM |  |  |  |  | 37°C, pH 7.4, ovis aries, brain | http://www.brenda-enzymes.org/literature/lit.php4?e=2.7.7.23&r=643057
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aB | UDP-GlcNAc (competes with UDP-GalNAc) | [NAME] mechanism |  |  | 0.23 mM |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.7.23 - UDP-N-acetylglucosamine diphsophorylase | r39aB | UDP-Glc (competes with UDP-GlcNAc) | [NAME] mechanism |  |  | 6.3 mM |  |  | 37°C, pH 8.5, sus scrofa, liver | http://www.jbc.org/content/271/22/13147.full.pdf+html
2.7.1.157 - N-acetylgalactosamine kinase | r40a | GalNAc (binds second) | Ordered bi-bi mechanism | 0.040 mM | 1.0 /s |  |  |  | 37°C, pH 8.0, homo sapiens, expressed in E. Coli | http://informahealthcare.com/doi/pdfplus/10.3109/14756360903179492
2.7.1.157 - N-acetylgalactosamine kinase | r40a | ATP (binds first) | Ordered bi-bi mechanism | 0.014 mM |  |  |  |  | 37°C, pH 8.0, homo sapiens, expressed in E. Coli | http://informahealthcare.com/doi/pdfplus/10.3109/14756360903179492
Nucleotide thriphosphate concentrations |  |  |  |  |  |  |  |  | Rat liver | http://www.jbc.org/content/249/1/211.full.pdf+html
NSD - Transporters
CMP-Neu5Ac - Transporter |  | CMP-Neu5Ac | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0013 mM | 6.6
CMP-Neu5Gc - Transporter |  | CMP-Neu5Gc | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0013 mM | 6.6 |  |  |  |  |  | Same kinetic data assumed as for CMP-Neu5Ac
GDP-Fuc - Transporter |  | GDP-Fuc | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0075 mM | 2.2
GDP-Man - Transporter |  | GDP-Man | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0075 mM | 2.2 |  |  |  |  |  | Same kinetic data assumed as for GDP-Fuc
UDP-Gal - Transporter |  | UDP-Gal | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0024 mM | 11.5
UDP-GalNAc - Transporter |  | UDP-GalNAc | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0071 mM | 18.1 |  |  |  |  | http://onlinelibrary.wiley.com/doi/10.1002/btpr.470/pdf | Same kinetic data assumed as for UDP-GlcNAc
UDP-Glc - Transporter |  | UDP-Glc | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0024 mM | 11.5 |  |  |  |  |  | Same kinetic data assumed as for UDP-Gal
UDP-GlcA - Transporter |  | UDP-GlcA | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0024 mM | 11.5 |  |  |  |  |  | Same kinetic data assumed as for UDP-Gal
UDP-GlcNAc - Transporter |  | UDP-GlcNAc | Single substrate Michaelis-Menten kinetics (simplified from anti-port kinetics) | 0.0071 mM | 18.1 |  |  |  |  | http://onlinelibrary.wiley.com/doi/10.1002/btpr.470/pdf