Cytochrome P450 2B10 (CYP2B10)

Cytochrome P450 2B10 is a heme-thiolate monooxygenase enzyme primarily expressed in mouse liver, where it constitutes about 10% of total microsomal cytochrome P450 content. It catalyzes the oxidative metabolism and detoxification of a broad spectrum of endogenous substrates (such as fatty acids) and xenobiotic compounds, including clinically used drugs like cyclophosphamide and bupropion. CYP2B10 expression and activity are regulated by nuclear receptors including constitutive androstane receptor (CAR), pregnane X receptor (PXR), glucocorticoid receptors, and vitamin D receptor, with additional modulation by circadian genes (e.g., Period 2/Per2). Functionally, it plays a central role in hepatic drug clearance, lipid homeostasis, and protection against toxic insults. In humans, the closest ortholog is CYP2B6, which shares similar roles in drug metabolism[1][2][3][5][6][7][9].

Other names

CYPIIB10CYPIIB20Cyp2bCyp2b-10Cyp2b20

Oxidative metabolism (monooxygenation) of drugs and endogenous compounds via heme-thiolate catalysis; NADPH-dependent electron transport