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Literature summary for 1.4.1.2 extracted from
- An NAD-specific glutamate dehydrogenase from cyanobacteria. Identification and properties (1991), FEBS Lett., 285, 35-38.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48500 | - |
6 * 48500, SDS-PAGE | Synechocystis sp. |
| 295000 | - |
gel filtration | Synechocystis sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechocystis sp. | - |
PCC 6803 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate + H2O + NAD+ | strict substrate specificity | Synechocystis sp. | 2-oxoglutarate + NH3 + NADH + H+ | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 48500, SDS-PAGE | Synechocystis sp. |
| More | - |
Synechocystis sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
20 min, 50% loss of activity | Synechocystis sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | 9 | reductive amination | Synechocystis sp. |
| 9.5 | 10 | oxidative deamination | Synechocystis sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no activity with NADPH and NADP+ | Synechocystis sp. | |
| NAD+ | - |
Synechocystis sp. | |
| NADH | - |
Synechocystis sp. | |
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