Cytochrome P450 2B6 (CYP2B6) (CYP2B6)

Cytochrome P450 2B6 (CYP2B6) is a hepatic enzyme belonging to the cytochrome P450 superfamily, responsible for the oxidative metabolism of approximately 7% of clinically relevant drugs (UniProt: P20813). It plays a pivotal role in the clearance of medications such as the antiretroviral efavirenz and the antidepressant bupropion, as well as the bioactivation of oxazaphosphorine prodrugs like cyclophosphamide into active cytotoxic agents (DrugBank: TARGET: T0012). The enzyme is highly polymorphic, with variants like CYP2B6*6 significantly impacting enzyme expression and activity, which can lead to therapeutic failure or toxicity (PharmGKB: PA124). CYP2B6 is also subject to induction by drugs like rifampin and inhibition by agents like ticlopidine, making it a key consideration in drug-drug interaction assessments (Zanger and Klein, 2013). While the user specified "Cytochrome P450 2B4", this name refers to the rabbit ortholog commonly used in structural biology; the human functional enzyme and therapeutic target is CYP2B6 (Wang and Tompkins, 2008).

Other names

Cytochrome P450 2B4 (rabbit ortholog)Cytochrome P450 IIB6CPB6CYP2B7P (pseudogene)

CYP2B6 catalyzes the oxidation of various substrates, including drugs and environmental toxins, by utilizing molecular oxygen and electrons transferred from NADPH via cytochrome P450 reductase (UniProt: P20813). This process typically results in the detoxification of xenobiotics or the bioactivation of prodrugs into their active metabolites (DrugBank: TARGET: T0012).