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Literature summary for 1.4.1.3 extracted from
- Fundamental differences in bioaffinity of amino acid dehydrogenases for N6- and S6-linked immobilized cofactors using kinetic-based enzyme-capture strategies (2005), Anal. Biochem., 338, 102-112.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Glutarate | shows no affinity for N6-linked NAD+ but is biospecifically adsorbed to S6-linked NAD+ derivatives in the presence of its soluble kinetic-based enzyme capture ligand glutarate | Bos taurus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
L-glutamate | at pH 8.5 | Bos taurus | |
| 1.01 | - |
L-glutamate | at pH 7.4 | Bos taurus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxoglutarate + NAD(P)H + NH3 | - |
Bos taurus | L-glutamate + NAD(P)+ + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDH | - |
Bos taurus |
| NAD(P)+-dependent glutamate dehydrogenase | - |
Bos taurus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | 8.5 | - |
Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD(P)H | - |
Bos taurus | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.07 | - |
Glutarate | at pH 8.5 | Bos taurus | |
| 0.09 | - |
Glutarate | at pH 7.4 | Bos taurus | |
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Release 2023.1 (January 2023)
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