1.1.1.88	additional information	-	additional information	kinetic analysis, overview. The enzyme exhibits positive cooperativity toward the substrates of the reductive reaction, but the oxidative reaction exhibits unusual double-saturation kinetics, distinctive among characterized HMG-CoA reductases. The unusual kinetics may arise from the presence of multiple active oligomeric states, each with different Vmax values	740104	
1.1.1.88	0.00734	-	3-hydroxy-3-methylglutaryl-CoA	at pH 7.4, temperature not specified in the publication	760594	
1.1.1.88	0.0285	-	NADH	at pH 7.4, temperature not specified in the publication	760594	
1.1.1.88	0.03	-	CoASH	H381A mutant, oxidative acylation of mevalonate	287502	
1.1.1.88	0.032	-	NADH	reductive deacylation to mevalonate	287496, 287497	
1.1.1.88	0.039	-	CoA	oxidative acylation of mevalonate	287496, 287497	
1.1.1.88	0.046	-	CoA	mevaldate oxidation	287496, 287497	
1.1.1.88	0.05	-	CoASH	oxidative acylation of mevalonate	287499	
1.1.1.88	0.05	-	CoASH	wild-type enzyme, oxidative acylation of mevalonate	287502	
1.1.1.88	0.05	-	DL-3-hydroxy-3-methylglutaryl-CoA	reductive deacylation to mevalonate	287496, 287497