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Literature summary for 5.1.3.7 extracted from
- The structural basis of substrate promiscuity in UDP-hexose 4-epimerase from the hyperthermophilic Eubacterium Thermotoga maritima (2015), Arch. Biochem. Biophys., 585, 39-51 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in in Escherichia coli | Thermotoga maritima |
| 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 |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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 |
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Thermotoga maritima | |
| 1.06 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima |  |
| 1.06 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
| 2.4 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
| 2.4 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
| 5.53 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
| 12.9 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
gel filtration | Thermotoga maritima |
| 70000 | - |
recombinant His6-tagged enzyme, gel filtration | Thermotoga maritima |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-N-acetyl-alpha-D-glucosamine | Thermotoga maritima | - |
UDP-N-acetyl-alpha-D-galactosamine | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q9WYX9 | - |
- |
| Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 | Q9WYX9 | - |
- |
| Thermotoga maritima DSM 3109 | Q9WYX9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermotoga maritima |
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Thermotoga maritima |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 48.7 | - |
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-glucosamine | Thermotoga maritima |
| 93.7 | - |
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-galactosamine | Thermotoga maritima |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| UDP-alpha-D-galactose | - |
Thermotoga maritima | UDP-alpha-D-glucose | - |
r | |
| UDP-alpha-D-glucose | epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose | Thermotoga maritima | UDP-alpha-D-galactose | - |
r | |
| 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 | |
| UDP-N-acetyl-alpha-D-glucosamine | - |
Thermotoga maritima | UDP-N-acetyl-alpha-D-galactosamine | - |
r | |
| 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 | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 35000, SDS-PAGE | Thermotoga maritima |
| homodimer | 2 * 34899, calculated from sequence | Thermotoga maritima |
| homodimer | 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation | Thermotoga maritima |
| More | enzyme structure analysis, overview | Thermotoga maritima |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GalE | - |
Thermotoga maritima |
| More | cf. EC 5.1.3.2 | Thermotoga maritima |
| TM0509 | - |
Thermotoga maritima |
| TMGalE | - |
Thermotoga maritima |
| UDP-hexose 4-epimerase | - |
Thermotoga maritima |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
- |
Thermotoga maritima |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 100 | over 50% of maximal activity within this range | Thermotoga maritima |
| 30 | 100 | 30°C: 53% of the maximal activity, 100°C: 90% of maximal activity | Thermotoga maritima |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
3 h, no significant decrease in activity | Thermotoga maritima |
| 70 | - |
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h | Thermotoga maritima |
| 80 | - |
3 h, the enzyme retains more than 85% of its original activity | Thermotoga maritima |
| 80 | - |
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h | Thermotoga maritima |
| 90 | - |
40 min, almost 50% of its original activity | Thermotoga maritima |
| 90 | - |
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min | Thermotoga maritima |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7757 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
| 14677 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
| 27671 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
| 27671 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
| 38295 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
| 38295 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Thermotoga maritima |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 10 | over 50% of maximal activity within this range | Thermotoga maritima |
| 5 | 10 | pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity | Thermotoga maritima |
| 6 | 8 | over 95% of maximal activity within this range | Thermotoga maritima |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Thermotoga maritima | sequence calculation | - |
5.72 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is involved in D-galactose metabolism | Thermotoga maritima |
| 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 |
| 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 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1134 | - |
UDP-alpha-D-glucose | pH 7.0, 80°C | Thermotoga maritima | |
| 1406 | - |
UDP-alpha-D-galactose | pH 7.0, 80°C | Thermotoga maritima | |
| 11465 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.0, 80°C | Thermotoga maritima | |
| 11465 | - |
UDP-N-acetyl-alpha-D-galactosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
| 36120 | - |
UDP-N-acetyl-alpha-D-galactosamine | pH 7.0, 80°C | Thermotoga maritima | |
| 36120 | - |
UDP-N-acetyl-alpha-D-glucosamine | recombinant enzyme, pH 7.0, 80°C | Thermotoga maritima | |
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