EC Number   |
Cofactor |
Reference |
|---|
    1.4.1.2 | acetyl-NAD+ |
- |
391557 |
| 1.4.1.2 | more |
AtGDH1 in the presence of NADP+ instead of NAD+ shows no activity. Dynamics of the coafctor binding domain II, cofactor binding mode, overview |
763098 |
| 1.4.1.2 | more |
cofactor recognition and differentiation method, three-dimensional cofactor binding structure, modelling, detailed overview |
725834 |
| 1.4.1.2 | more |
in the wild-type enzyme there is a strong pH dependence in the level of discrimination between NADH and NADPH |
724888 |
| 1.4.1.2 | more |
NADP+ and NADPH are poor cofactors. The presence of an acidic residue at the P7 position, adjacent to the 2'-OH group, typically discriminates against NADP+. PaGDH contains a P7 glutamate and has high specificity for NAD(H), with a kcat/Km for NAD+ that is approximately 1000fold greater than that for NADP+ |
710758 |
| 1.4.1.2 | more |
no activity with NADPH |
673495 |
| 1.4.1.2 | more |
no activity with NADPH and NADP+ |
391542 |
| 1.4.1.2 | more |
no cofactor: NADP+ |
742464 |
| 1.4.1.2 | more |
no detectable activity with NADP+ |
763098 |
| 1.4.1.2 | more |
when NAD+ is replaced by NADP+, the GDH activity in the wild-type occurs only some specific homohexamer and heterohexamers with very low level |
726245 |
