1.1.1.88	additional information	sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, overview	723092	
1.1.1.88	additional information	sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, specificity-determining residue of HMGR from Pseudomonas mevalonii is D646, overview	723092	
1.1.1.88	additional information	the enzyme prefers NAD(H) over NADP(H) as a cofactor, suggesting an oxidative physiological role for the enzyme	740104	
1.1.1.88	additional information	very detailed kinetic studies of mutants concerning NAD+/NADP+-affinities, the best specificity improvement is achieved by the D146A/L148R-mutant	287505	
1.1.1.88	NAD+	-	287495, 287496, 287497, 287498, 287499, 287501, 287502, 287504, 287505, 287506, 287507, 287508, 654225, 657303, 723092, 740104, 760603, 761344	
1.1.1.88	NAD+	four-electron pyridine oxidoreductase	287500	
1.1.1.88	NADH	-	654225, 656615, 657303, 723092, 740104	
1.1.1.88	NADH	NADH-specific enzyme	760594	
1.1.1.88	NADH	reverse reaction	287495, 287496, 287497, 287498, 287499, 287500, 287501, 287502, 287504, 287505, 287506, 287507, 287508	
1.1.1.88	NADP+	NAD+ is 600000fold more efficient than NADP+ in wild-type enzyme	287505