3.1.1.45	A150T	site-directed mutagenesis, the mutant shows slightly higher Vmax with olmesartan medoxomil compared to the wild-type enzyme	729629	
3.1.1.45	C123A	inactive	94355	
3.1.1.45	C123S	-	94357	
3.1.1.45	C123S	100% activity towards alpha-naphthyl acetate compared with the wild type enzyme	-, 671042	
3.1.1.45	C123S	burst kinetics with p-nitrophenyl acetate, 10% as active as DLH	94355	
3.1.1.45	C123S	maximal activity 20% that of the wild type protein	94356, 94358	
3.1.1.45	C123S	site-directed mutagenesis, mutation of the active site cysteine to a serine, giving a catalytic triad found in serine proteases, completely changes the catalytic activity to a dienelactone isomerase	-, 650835	
3.1.1.45	C123S/R206A	65% activity towards alpha-naphthyl acetate compared with the wild type enzyme	671042	
3.1.1.45	C132A	mutant shows a drastic reduction of the olmesartan medoxomil-hydrolyzing activity	704653	
3.1.1.45	C132A	mutant shows a low activity, 30% of wild-type	704653