Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ADP | allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 1100% activation by ADP. Relative activation by ADP of GDH-catalyzed NAD+reduction is 36%, compared with 198% for NADP+ reduction | Bos taurus | |
L-leucine | allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 725% activation by L-leucine, respectively. Activation of NAD+ and NADP+ reduction by 40% and 135%, respectively | Bos taurus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
GTP | - |
Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Bos taurus | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | Bos taurus | - |
2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NADP+ | Bos taurus | - |
2-oxoglutarate + NH3 + NADPH + H+ | - |
r | |
additional information | Bos taurus | the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NAD+ | - |
Bos taurus | 2-oxoglutarate + NH3 + NADH + H+ | - |
r | |
L-glutamate + H2O + NADP+ | - |
Bos taurus | 2-oxoglutarate + NH3 + NADPH + H+ | - |
r | |
additional information | the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH | Bos taurus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GDH | - |
Bos taurus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bos taurus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bos taurus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH. In the reductive amination direction, the rates of product formation are always greater for NADH oxidation than NADPH oxidation | Bos taurus | |
NAD+ | - |
Bos taurus | |
NADH | - |
Bos taurus | |
NADP+ | - |
Bos taurus | |
NADPH | - |
Bos taurus |
General Information | Comment | Organism |
---|---|---|
physiological function | allosteric activation and inhibition is important for enzyme regulation, overview | Bos taurus |