EC Number   |
Cofactor |
Reference |
|---|
    1.2.1.5 | more |
the nicotinamide moieties of NAD+ and NADP+ directly interact with the conserved catalytic residues Cys300 and Glu266, and binding causes concerted conformational changes. Flexible cofactor-binding pocket of BcALDH. Cofactor-enzyme binding structure analysis, overview |
763136 |
| 1.2.1.5 | NAD(P)+ |
- |
711110, 724720 |
| 1.2.1.5 | NAD+ |
- |
348793, 671511, 688414, 690142, 698095, 711635, 723877, 724620, 725085, 739913, 740294, 741087, 741167, 762793, 763136, 763348, 763529 |
| 1.2.1.5 | NAD+ |
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+ |
722210 |
| 1.2.1.5 | NAD+ |
preferred before NADP+ |
762546 |
| 1.2.1.5 | NAD+ |
preferred cofactor |
725948 |
| 1.2.1.5 | NAD+ |
prefers NADP+ over NAD+ |
348790 |
| 1.2.1.5 | NAD+ |
relative but not absolute specificity for NAD+ over NADP+ |
348792 |
| 1.2.1.5 | NAD+ |
required |
689379 |
| 1.2.1.5 | NADH |
- |
735898 |
