Cytochrome P450 family 4 subfamily B member 1 (CYP4B1)

Cytochrome P450 family 4 subfamily B member 1 (CYP4B1) is a monooxygenase enzyme belonging to the cytochrome P450 superfamily, primarily expressed in human extrahepatic tissues such as the lung[1][2][3][5]. While CYP4B1 in animal models is well-established to hydroxylate fatty acids and bioactivate certain xenobiotics (such as 4-ipomeanol and perilla ketone), the catalytic activity of human CYP4B1 is absent or extremely low due to a unique Ser427 substitution that impairs activity[2]. Nevertheless, changes in CYP4B1 gene expression have been associated with various cancers[2][3], and the enzyme is a subject of research as a potential suicide gene for selective cancer therapies[2]. No approved drugs directly target or modulate CYP4B1, and the enzyme is not involved in major hepatic drug metabolism pathways in humans. The physiological function of human CYP4B1 remains unclear, and its status as a therapeutic target is primarily investigational or experimental[2][4][5].

Other names

Cytochrome P450 4B1CYPIVB1Cytochrome P450-HPP-450HPcytochrome P450, family 4, subfamily B, polypeptide 1microsomal monooxygenase

Bioactivation (conversion of pro-toxins like 4-ipomeanol to reactive, toxic intermediates); Hydroxylation of fatty acids/xenobiotics via monooxygenase activity