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Literature summary for 1.1.1.45 extracted from
- Unraveling the mechanism of L-gulonate-3-dehydrogenase inhibition by ascorbic acid insights from molecular modeling (2018), Comput. Biol. Chem., 77, 146-153 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ascorbic acid | molecular dockings of ascorbate to gulonate-3-dehydrogenase indicated its binding near the co-factor binding site. Docking revealed that ascorbate binding could lead to steric clashes between ascorbate and the co-factor (NADH) | Bubalus bubalis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bubalus bubalis | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GuDH | - |
Bubalus bubalis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | crucial enzyme in the non-phosphorylated sugar metabolism or glucuronate-xylulose pathway | Bubalus bubalis |
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Release 2023.1 (January 2023)
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