Crystallization (Comment) | Organism |
---|---|
structures of unliganded and UDP-xylose bound UGDH. The A109P substitution that differs human and Caenorhabditis elgans enzymes is accommodated by an Asn-to-Ser substitution at position 290. The allosteric transition is conserved in UGDH, and UDP-Xyl binding induces formation of the Eomega hexamer. The enzyme also exhibits hysteresis in progress curves and negative cooperativity with respect to NAD+ binding | Caenorhabditis elegans |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
UDP-xylose | - |
Caenorhabditis elegans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.055 | - |
UDP-alpha-D-glucose | Hill coefficient 1, pH 7.5, 25°C | Caenorhabditis elegans | |
0.333 | - |
NAD+ | K0.5 value, Hill coefficient 0.8, pH 7.5, 25°C | Caenorhabditis elegans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Caenorhabditis elegans | Q19905 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Caenorhabditis elegans | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
sqv-4 | - |
Caenorhabditis elegans |
UGDH | - |
Caenorhabditis elegans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.23 | - |
UDP-alpha-D-glucose | pH 7.5, 25°C | Caenorhabditis elegans | |
1.7 | - |
NAD+ | Hill coefficient 0.8, pH 7.5, 25°C | Caenorhabditis elegans |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0069 | - |
UDP-xylose | pH 7.5, 25°C | Caenorhabditis elegans |