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Literature summary for 1.4.1.2 extracted from
- Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum (1991), Biochim. Biophys. Acta, 1115, 123-130.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| [Clostridium] symbiosum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate + H2O + NAD+ | - |
[Clostridium] symbiosum | 2-oxoglutarate + NH3 + NADH + H+ | - |
? |  |
| additional information | L-alpha-amino-gamma-nitroaminobutyrate deamination at 0.5% the rate of deamination of L-glutamate | [Clostridium] symbiosum | ? | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
[Clostridium] symbiosum | |
| NADH | - |
[Clostridium] symbiosum | |
| NADPH | rate with NADPH is 300times lower than with NADH | [Clostridium] symbiosum | |
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