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The Cytochrome P450 2C (CYP2C) subfamily consists of a group of heme-thiolate enzymes primarily expressed in the liver that play a critical role in the Phase I metabolism of approximately 20% of clinically used drugs (StatPearls, 2023). This subfamily includes four main human enzymes: CYP2C8, CYP2C9, CYP2C18, and CYP2C19, which catalyze the oxidation, hydroxylation, and dealkylation of diverse substrates ranging from non-steroidal anti-inflammatory drugs (NSAIDs) to anticoagulants and proton pump inhibitors (UniProt, 2024). Beyond exogenous compounds, these enzymes are involved in the metabolism of endogenous substances such as arachidonic acid and steroid hormones (PubMed, PMID: 21172313). The CYP2C subfamily is clinically significant due to extensive genetic polymorphisms that lead to wide inter-individual variability in drug efficacy and safety (PharmGKB, 2024). For instance, variants in CYP2C9 and CYP2C19 are major determinants of the clinical response to warfarin and clopidogrel, respectively (FDA, 2023). Consequently, these enzymes are frequent targets for pharmacogenomic testing to optimize dosing and avoid adverse drug reactions. Their susceptibility to inhibition and induction also makes them a primary focus for evaluating potential drug-drug interactions during pharmaceutical development (NIH, 2024).
The CYP2C subfamily enzymes catalyze the metabolic transformation of substrates via oxidative reactions, including hydroxylation, dealkylation, and epoxidation, which typically lead to drug inactivation for elimination or the bioactivation of prodrugs into their active forms (StatPearls, 2023; UniProt, 2024).
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