EC Number | Cloned (Comment) | Organism |
---|---|---|
5.1.3.2 | expression in in Escherichia coli | Thermotoga maritima |
5.1.3.2 | gene galE, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and functional complementation of enzyme-deficient Escherichia coli strain BW25113 DELTAgalE | Thermotoga maritima |
5.1.3.7 | expression in in Escherichia coli | Thermotoga maritima |
5.1.3.7 | gene galE, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and functional complementation of enzyme-deficient Escherichia coli strain BW25113 DELTAgalE | Thermotoga maritima |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.1.3.2 | hanging drop vapor diffusion method, crystal structure of the enzyme (TMGalE) and the enzyme bound to UDP-glucose is determined at resolutions of 1.9 A and 2.0 A, respectively | Thermotoga maritima |
5.1.3.2 | purified recombinant unbound enzyme TMGalE, and TMGalE bound to UDP-Glc, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution | Thermotoga maritima |
5.1.3.7 | hanging drop vapor diffusion method, crystal structure of the enzyme (TMGalE) and the enzyme bound to UDP-glucose is determined at resolutions of 1.9 A and 2.0 A, respectively | Thermotoga maritima |
5.1.3.7 | purified recombinant unbound enzyme TMGalE, and TMGalE bound to UDP-Glc, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution | Thermotoga maritima |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.3.2 | additional information | - |
additional information | Michaelis-Menten kinetics | Thermotoga maritima | |
5.1.3.2 | 1.06 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 2.4 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 5.53 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 5.53 | - |
UDP-alpha-D-glucose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 12.9 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 12.9 | - |
UDP-alpha-D-galactose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | additional information | - |
additional information | Michaelis-Menten kinetics | Thermotoga maritima | |
5.1.3.7 | 1.06 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 1.06 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 2.4 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 2.4 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 5.53 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 12.9 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.2 | additional information | the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+ | Thermotoga maritima | |
5.1.3.7 | additional information | the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+ | Thermotoga maritima |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 70000 | - |
gel filtration | Thermotoga maritima |
5.1.3.2 | 70000 | - |
recombinant His6-tagged enzyme, gel filtration | Thermotoga maritima |
5.1.3.7 | 70000 | - |
gel filtration | Thermotoga maritima |
5.1.3.7 | 70000 | - |
recombinant His6-tagged enzyme, gel filtration | Thermotoga maritima |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.3.2 | UDP-alpha-D-glucose | Thermotoga maritima | - |
UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | Thermotoga maritima DSM 3109 | - |
UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | - |
UDP-alpha-D-galactose | - |
r | |
5.1.3.7 | UDP-N-acetyl-alpha-D-glucosamine | Thermotoga maritima | - |
UDP-N-acetyl-alpha-D-galactosamine | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.3.2 | Thermotoga maritima | Q9WYX9 | - |
- |
5.1.3.2 | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | Q9WYX9 | - |
- |
5.1.3.2 | Thermotoga maritima DSM 3109 | Q9WYX9 | - |
- |
5.1.3.7 | Thermotoga maritima | Q9WYX9 | - |
- |
5.1.3.7 | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | Q9WYX9 | - |
- |
5.1.3.7 | Thermotoga maritima DSM 3109 | Q9WYX9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.1.3.2 | - |
Thermotoga maritima |
5.1.3.2 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Thermotoga maritima |
5.1.3.7 | - |
Thermotoga maritima |
5.1.3.7 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Thermotoga maritima |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 69.7 | - |
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-glucose | Thermotoga maritima |
5.1.3.2 | 192.4 | - |
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-galactose | Thermotoga maritima |
5.1.3.7 | 48.7 | - |
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-glucosamine | Thermotoga maritima |
5.1.3.7 | 93.7 | - |
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-galactosamine | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.3.2 | additional information | enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively | Thermotoga maritima | ? | - |
? | |
5.1.3.2 | additional information | enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively | Thermotoga maritima DSM 3109 | ? | - |
? | |
5.1.3.2 | additional information | enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | ? | - |
? | |
5.1.3.2 | UDP-alpha-D-galactose | - |
Thermotoga maritima | UDP-alpha-D-glucose | - |
r | |
5.1.3.2 | UDP-alpha-D-galactose | enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium | Thermotoga maritima | UDP-alpha-D-glucose | - |
r | |
5.1.3.2 | UDP-alpha-D-galactose | - |
Thermotoga maritima DSM 3109 | UDP-alpha-D-glucose | - |
r | |
5.1.3.2 | UDP-alpha-D-galactose | - |
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | UDP-alpha-D-glucose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | - |
Thermotoga maritima | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium | Thermotoga maritima | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | - |
Thermotoga maritima DSM 3109 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium | Thermotoga maritima DSM 3109 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima DSM 3109 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | - |
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-alpha-D-glucose | epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | UDP-alpha-D-galactose | - |
r | |
5.1.3.2 | UDP-N-acetyl-alpha-D-galactosamine | epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-N-acetyl-alpha-D-glucosamine | - |
r | |
5.1.3.2 | UDP-N-acetyl-alpha-D-glucosamine | epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-N-acetyl-alpha-D-galactosamine | - |
r | |
5.1.3.7 | additional information | enzyme TMGalE also has high activity for epimerization of UDP-Gal to UDP-Glc, EC 5.1.3.2. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively | Thermotoga maritima | ? | - |
? | |
5.1.3.7 | UDP-alpha-D-galactose | - |
Thermotoga maritima | UDP-alpha-D-glucose | - |
r | |
5.1.3.7 | UDP-alpha-D-glucose | epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-alpha-D-galactose | - |
r | |
5.1.3.7 | UDP-N-acetyl-alpha-D-galactosamine | epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-N-acetyl-alpha-D-glucosamine | - |
r | |
5.1.3.7 | UDP-N-acetyl-alpha-D-glucosamine | - |
Thermotoga maritima | UDP-N-acetyl-alpha-D-galactosamine | - |
r | |
5.1.3.7 | UDP-N-acetyl-alpha-D-glucosamine | epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-N-acetyl-alpha-D-galactosamine | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.1.3.2 | homodimer | 2 * 35000, SDS-PAGE | Thermotoga maritima |
5.1.3.2 | homodimer | 2 * 34899, calculated from sequence | Thermotoga maritima |
5.1.3.2 | homodimer | 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation | Thermotoga maritima |
5.1.3.2 | More | enzyme structure analysis, overview | Thermotoga maritima |
5.1.3.7 | homodimer | 2 * 35000, SDS-PAGE | Thermotoga maritima |
5.1.3.7 | homodimer | 2 * 34899, calculated from sequence | Thermotoga maritima |
5.1.3.7 | homodimer | 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation | Thermotoga maritima |
5.1.3.7 | More | enzyme structure analysis, overview | Thermotoga maritima |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.3.2 | GalE | - |
Thermotoga maritima |
5.1.3.2 | More | cf. EC 5.1.3.7 | Thermotoga maritima |
5.1.3.2 | TM0509 | - |
Thermotoga maritima |
5.1.3.2 | TMGalE | - |
Thermotoga maritima |
5.1.3.2 | UDP-galactose 4-epimerase | - |
Thermotoga maritima |
5.1.3.2 | UDP-hexose 4-epimerase | - |
Thermotoga maritima |
5.1.3.7 | GalE | - |
Thermotoga maritima |
5.1.3.7 | More | cf. EC 5.1.3.2 | Thermotoga maritima |
5.1.3.7 | TM0509 | - |
Thermotoga maritima |
5.1.3.7 | TMGalE | - |
Thermotoga maritima |
5.1.3.7 | UDP-hexose 4-epimerase | - |
Thermotoga maritima |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 80 | - |
- |
Thermotoga maritima |
5.1.3.7 | 80 | - |
- |
Thermotoga maritima |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 30 | 100 | over 50% of maximal activity within this range | Thermotoga maritima |
5.1.3.2 | 30 | 100 | 30°C: 53% of the maximal activity, 100°C: 90% of maximal activity | Thermotoga maritima |
5.1.3.7 | 30 | 100 | over 50% of maximal activity within this range | Thermotoga maritima |
5.1.3.7 | 30 | 100 | 30°C: 53% of the maximal activity, 100°C: 90% of maximal activity | Thermotoga maritima |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 70 | - |
3 h, no significant decrease in activity | Thermotoga maritima |
5.1.3.2 | 70 | - |
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h | Thermotoga maritima |
5.1.3.2 | 80 | - |
3 h, the enzyme retains more than 85% of its original activity | Thermotoga maritima |
5.1.3.2 | 80 | - |
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h | Thermotoga maritima |
5.1.3.2 | 90 | - |
40 min, almost 50% of its original activity | Thermotoga maritima |
5.1.3.2 | 90 | - |
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min | Thermotoga maritima |
5.1.3.7 | 70 | - |
3 h, no significant decrease in activity | Thermotoga maritima |
5.1.3.7 | 70 | - |
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h | Thermotoga maritima |
5.1.3.7 | 80 | - |
3 h, the enzyme retains more than 85% of its original activity | Thermotoga maritima |
5.1.3.7 | 80 | - |
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h | Thermotoga maritima |
5.1.3.7 | 90 | - |
40 min, almost 50% of its original activity | Thermotoga maritima |
5.1.3.7 | 90 | - |
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min | Thermotoga maritima |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.3.2 | 7757 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 7757 | - |
UDP-alpha-D-glucose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 14677 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 14677 | - |
UDP-alpha-D-galactose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 27671 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 38295 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 7757 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 14677 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 27671 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 27671 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 38295 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 38295 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 7 | - |
- |
Thermotoga maritima |
5.1.3.7 | 7 | - |
- |
Thermotoga maritima |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
5.1.3.2 | 5 | 10 | over 50% of maximal activity within this range | Thermotoga maritima |
5.1.3.2 | 5 | 10 | pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity | Thermotoga maritima |
5.1.3.2 | 6 | 8 | over 95% of maximal activity within this range | Thermotoga maritima |
5.1.3.7 | 5 | 10 | over 50% of maximal activity within this range | Thermotoga maritima |
5.1.3.7 | 5 | 10 | pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity | Thermotoga maritima |
5.1.3.7 | 6 | 8 | over 95% of maximal activity within this range | Thermotoga maritima |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.2 | NAD+ | enzyme-bound, exogenous NAD+ does not appear to be a strong activator of enzyme activity, there is no significant difference in enzyme activity regardless of the presence and absence of NAD+ | Thermotoga maritima | |
5.1.3.7 | NAD+ | enzyme-bound, exogenous NAD+ does not appear to be a strong activator of enzyme activity, there is no significant difference in enzyme activity regardless of the presence and absence of NAD+ | Thermotoga maritima |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
5.1.3.2 | Thermotoga maritima | sequence calculation | - |
5.72 |
5.1.3.7 | Thermotoga maritima | sequence calculation | - |
5.72 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.1.3.2 | metabolism | the enzyme is involved in D-galactose metabolism | Thermotoga maritima |
5.1.3.2 | additional information | dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc | Thermotoga maritima |
5.1.3.2 | physiological function | UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism | Thermotoga maritima |
5.1.3.7 | metabolism | the enzyme is involved in D-galactose metabolism | Thermotoga maritima |
5.1.3.7 | additional information | dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc | Thermotoga maritima |
5.1.3.7 | physiological function | UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism | Thermotoga maritima |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.3.2 | 1134 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 1134 | - |
UDP-alpha-D-galactose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 1406 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 1406 | - |
UDP-alpha-D-glucose | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 11465 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.2 | 36120 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 1134 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 1406 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 11465 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 11465 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 36120 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
5.1.3.7 | 36120 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima |