Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
mutant K94E, to 2.08 A resolution. Cofactor binding triggers the formation of the 32 symmetry hexamer, but substrate UDP-alpha-D-glucose is needed for the stability of the complex. Loop88-110 is the cofactor-responsive allosteric switch that drives hexamer formation, loop88-110 directly links cofactor binding to the stability of the hexamer-building interface. In the interface, loop88-110 packs against the Thr131-loop/alpha6 helix, the allosteric switch that responds to the feedback inhibitor UDP-alpha-D-xylose | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K94E | mutation in the hexamer-building interface, generates a stable enzyme dimer. 160fold decrease in kcat value | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.025 | - |
UDP-alpha-D-glucose | wild-type, pH 8.7, 25°C | Homo sapiens | |
0.384 | - |
NAD+ | wild-type, pH 8.7, 25°C | Homo sapiens | |
2.21 | - |
UDP-alpha-D-glucose | mutant K94E, pH 8.7, 25°C | Homo sapiens | |
6.3 | - |
NAD+ | mutant K94E, pH 8.7, 25°C | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O60701 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Homo sapiens | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
NAD+ | mutant K94E, pH 8.7, 25°C | Homo sapiens | |
0.02 | - |
UDP-alpha-D-glucose | mutant K94E, pH 8.7, 25°C | Homo sapiens | |
3.2 | - |
UDP-alpha-D-glucose | wild-type, pH 8.7, 25°C | Homo sapiens | |
4.4 | - |
NAD+ | wild-type, pH 8.7, 25°C | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | cofactor binding triggers the formation of the 32 symmetry enzyme hexamer, which is the catalytically relevant state | Homo sapiens |