Cytochrome P450 2B6 (CYP2B6)

Cytochrome P450 2B6 (CYP2B6) is a member of the cytochrome P450 superfamily of enzymes, functioning as a monooxygenase that introduces an oxygen atom into a broad range of substrates[1][2][7]. It plays a significant role in the oxidative metabolism of 2–10% of all clinically used drugs, including antineoplastic, antiviral, anesthetic, and neuropsychiatric agents[4][2][6]. CYP2B6 is highly polymorphic, resulting in interindividual and interethnic variability in enzyme activity and drug response, which can impact both efficacy and risk of adverse drug reactions[5][8]. It localizes to the endoplasmic reticulum and is regulated at the transcriptional level by nuclear receptors such as CAR and PXR[4][2]. Substrate specificity centers on lipophilic, non-planar molecules, and the enzyme participates in the bioactivation of certain prodrugs (such as cyclophosphamide) and in the clearance of active drugs (such as efavirenz and bupropion)[1][4][2]. Clinical importance is underscored by the risk of drug-drug interactions and the clinical relevance of pharmacogenetic testing, particularly for drugs with narrow therapeutic indices or high interindividual variability in response[8][2].

Other names

CYP2B6Cytochrome P450, family 2, subfamily B, polypeptide 6Cytochrome P450, 2B6CYP2B6 enzyme

Drug metabolism via oxidation (hydroxylation, N-demethylation, O-dealkylation, etc.) of substrates; Activation of prodrugs; Inactivation or clearance of active drugs; Drug-drug interaction through enzyme induction or inhibition