Figure 5
Catalytic promiscuity of natural variants of CYP102A1 towards human P450 substrates. Purified natural variants of CYP102A1 were characterized for human P450 enzyme activities using specific substrates: phenacetin O-deethylation for P450 1A2; 7-ethoxycoumarin (7-EC) O-deethylation for P450s 1A2, 2A6, and 2E1; 7-ethoxy-4-trifluoromethylcoumarin (7-EFC) O-deethylation for P450s 1A2 and 2B6; chlorzoxazone 6β-hydroxylation for P450 2E1; coumarin 7-hyroxylation for P450 2A6. Data are shown as the means ± SEM.