EC Number |
Cofactor |
Reference |
---|
1.2.1.36 | FAD |
metalloflavoprotein, reaction rate is maximal with FAD |
390263 |
1.2.1.36 | 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 |
1.2.1.36 | NAD+ |
- |
390264, 390268, 654168, 654553, 655208, 655432, 655948, 656048, 656159, 656252, 656611, 657155, 677280, 690142, 696437, 711154, 711854, 724722, 725461, 742258, 743142, 743375, 743660, 762790, 762796, 762833, 762901, 763070, 763136, 763150, 763337, 763348, 763529, 763530, 763752 |
1.2.1.36 | NAD+ |
cofactor is bound in the hydride transfer position in all four monomers |
654700 |
1.2.1.36 | NAD+ |
NAD+ dependent |
390271 |
1.2.1.36 | NAD+ |
reaction is NAD+ dependent, rather than NADP+ dependent |
390270 |
1.2.1.36 | NAD+ |
reaction rate is maximal with NAD+, stimulation by NAD+ reversed by direct addition of NADH |
390263 |
1.2.1.36 | NAD+ |
required |
689379 |
1.2.1.36 | NADH |
- |
668500, 671851, 672991, 673242, 673251, 673254, 673325, 675508, 677080, 686690 |
1.2.1.36 | NADP+ |
- |
763136 |