EC Number |
Cofactor |
Reference |
---|
1.1.1.100 | NADH |
NADPH is much more effective than NADH |
285668, 285677 |
1.1.1.100 | NADP+ |
- |
285668, 285681, 667708, 693287, 739774, 739901 |
1.1.1.100 | NADPH |
absolute specificity for NADPH |
285670, 285672, 285683 |
1.1.1.100 | more |
NADH is used by NADH-dependent 3-oxoacyl [ACP]-reductase, EC 1.1.1.121 |
285676, 285678 |
1.1.1.100 | NADPH |
much more effective than NADH |
285677 |
1.1.1.100 | NADPH |
exhibits negative cooperativity for its interaction with the enzyme |
654432 |
1.1.1.100 | NADPH |
- |
285668, 285669, 285671, 285673, 285674, 285675, 285676, 285678, 285679, 655871, 656723, 667257, 667646, 667708, 669013, 670774, 689435, 703163, 704337, 704843, 706142, 706639, 740023, 740558, 740630, 741114, 763071, 763477 |
1.1.1.100 | NADPH |
cofactor binding structure and mechanism |
667520 |
1.1.1.100 | NADP+ |
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative cofactor binding |
668574 |
1.1.1.100 | NADPH |
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative allosteric cofactor binding in presence of [acyl-carrier-protein] |
668574 |