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Literature summary for 1.2.1.12 extracted from
- Structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues (2002), Acta Crystallogr. Sect. D, 58, 1287-1297.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues ADPribose and thio-NAD+. The crystals of both GAPDH complexes belong to the same space group C2 as holeenzyme or apoenzyme, but with different unit-cell parameters | Panulirus versicolor |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP-ribose | coenzyme analogue with a non-cooperative behaviour of binding, is a potent competitive inhibitor | Panulirus versicolor |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Panulirus versicolor | P56649 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| tail muscle | - |
Panulirus versicolor | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-glyceraldehyde-3-phosphate dehydrogenase | - |
Panulirus versicolor |
| GAPDH | - |
Panulirus versicolor |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thio-NAD+ | the coenzyme analogue binds in a non-productive manner, resulting in a disordered thionicotinamide ring and rearranged active-site residues, effective as substrate to replace NAD+ | Panulirus versicolor | |
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