1.1.1.100	additional information	NADH is used by NADH-dependent 3-oxoacyl [ACP]-reductase, EC 1.1.1.121	285676, 285678	
1.1.1.100	NADH	-	740013, 741044	
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	NADP+	cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative cofactor binding	668574	
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	3fold enhancement in acyl-carrier protein binding to wild-type in the presence of NADPH	703630	
1.1.1.100	NADPH	absolute specificity for NADPH	285670, 285672, 285683	
1.1.1.100	NADPH	cofactor binding structure and mechanism	667520	
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	
1.1.1.100	NADPH	dependent on	701808	
1.1.1.100	NADPH	exhibits negative cooperativity for its interaction with the enzyme	654432	
1.1.1.100	NADPH	low activity with NADPH	741044	
1.1.1.100	NADPH	much more effective than NADH	285677	
1.1.1.100	NADPH	numerous residues trigger steric hindrance to the binding of NADPH and substrate. Upon NADPH binding, these residues are pushed away from the active site, allowing the enzyme to adopt an open conformation. The transition from an NADPH-bound to an NADP+-bound form is likely to facilitate release of the product	762566	
1.1.1.100	NADPH	positive cooperativity in binding to enzyme	684702