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A meta-analysis was performed on the reported literature regarding followings. First, values of the MichaelisMenten constants (Km), maximal velocities (Vmax), and intrinsic clearance (Vmax/Km) and the metabolic activities mediated by human cytochrome P450 3A4 and/or 3A5; second, inhibition constants (Ki); and third, maximum inactivation rate constants (kinact) to establish the contribution of P450 3A5 to drug metabolism. At least 120 of the 127 metabolic reactions investigated (> 94%) were catalyzed by P450 3A4 and by P450 3A5. In the 73 metabolic reactions for which data were available, the mean P450 3A5/P450 3A4 ratios of Km ,V max ,a nd V max/Km values were 1.93, 1.25, and 1.20, respectively, but the median ratios were 1.17, 0.64, and 0.56, respectively. In 14–18% of the metabolic reactions, the Vmax and Vmax/Km values for P450 3A5 were more than twice those for P450 3A4. The Ki values for P450 3A5 were on average approximately 5 times those for P450 3A4. Five of 13 mechanism-based inhibitors of P450 3A4 (38%) did not exhibit similar mechanism-based inhibition of P450 3A5. These collective findings give insight into the contribution of polymorphic P450 3A5 to drug metabolism and adverse drug interactions.

Comparison of the Contributions of Cytochromes P450 3A4 and 3A5 in Drug Oxidation Rates and Substrate Inhibition