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Cytochrome P450 2C11 is the predominant male-specific CYP enzyme in rat liver, accounting for more than 50% of total hepatic P450s in adult male rats and largely responsible for the metabolism of testosterone to 2α- and 16α-hydroxytestosterone, as well as other steroid and fatty acid substrates. As part of the cytochrome P450 superfamily, it catalyzes monooxygenase reactions—including oxidation, hydroxylation, and epoxidation—of a wide range of endogenous and exogenous compounds. CYP2C11 expression is hormonally regulated via growth hormone secretion profiles and is essentially undetectable in female rat liver. While not a direct therapeutic target in clinical use, it plays a critical role in rodent drug metabolism studies, and its activity must be carefully considered in the translational interpretation of preclinical pharmacokinetic and toxicological data.
Oxidation of xenobiotics via monooxygenase mechanism; Hydroxylation of steroids such as testosterone; Epoxidation of fatty acids like arachidonic acid using NADPH as an electron donor.
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