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Cytochrome P450 3A11 is a heme-thiolate monooxygenase enzyme of the cytochrome P450 superfamily and the primary hepatic CYP3A isoform in mice, functionally homologous to human CYP3A4. It catalyzes the oxidative metabolism (hydroxylation) of a broad range of endogenous compounds (such as steroids, bile acids, cholesterol, and vitamin D) and xenobiotics, including many clinically important drugs. Its expression is transcriptionally regulated by nuclear receptors like PXR and is modulated by dietary, hormonal, circadian, and epigenetic factors. Cyp3a11 plays an essential role in drug detoxification, and variations in its activity or expression significantly affect drug efficacy and toxicity in preclinical mouse models. It is widely used in pharmacological studies for predicting drug-drug interactions and metabolic profiles in animal models before translation to human studies.
Monooxygenase activity—mediates oxidation of drugs, steroids, and lipids (drug detoxification); Substrate hydroxylation, increasing hydrophilicity for hepatic clearance; Regulation by PXR (Pregnane X Receptor)
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