CYP2A6
CYP2A6 (cytochrome P450 family 2 subfamily A member 6) is an endoplasmic reticulum monooxygenase of the cytochrome P450 superfamily. It hydroxylates coumarin and is the major nicotine C-oxidase; it was formerly named CYP2A3 and is also known as CPA6 and CYP2A. Browse Assay Genie's current range of CYP2A6 research reagents below, or read on for the biology behind the target.
CYP2A6 belongs to the cytochrome P450 family, whose members are monooxygenases that catalyse many reactions involved in drug metabolism and in the synthesis of cholesterol, steroids and other lipids. CYP2A6 exhibits high coumarin 7-hydroxylase activity and constitutes the major nicotine C-oxidase. It also acts as a 1,4-cineole 2-exo-monooxygenase and has low phenacetin O-deethylation activity.
The enzyme contributes to the metabolism of several xenobiotics. It can hydroxylate the anti-cancer drugs cyclophosphamide, ifosphamide and tegafur, and it is competent in the metabolic activation of aflatoxin B1. NCBI Gene also lists nitrosamines and some other pharmaceuticals among its substrates. These activities make the CYP2A6 protein a frequent subject in studies of drug metabolism and chemical activation.
The CYP2A6 gene sits within a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The protein localises to the endoplasmic reticulum and microsome membranes, and its expression is induced by phenobarbital. Individuals carrying certain allelic variants have a poor metabolizer phenotype, meaning they do not efficiently metabolise coumarin or nicotine. The gene was formerly referred to as CYP2A3 before being renamed CYP2A6; HGNC also records the earlier name cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 6.
CYP2A6 is the major nicotine C-oxidase, and poor metabolizer alleles reduce the efficiency of nicotine metabolism.
The enzyme hydroxylates the anti-cancer drugs cyclophosphamide, ifosphamide and tegafur, and metabolises some other pharmaceuticals.
CYP2A6 is competent in the metabolic activation of aflatoxin B1 and also metabolises nitrosamines.
Allelic variants give a poor metabolizer phenotype with inefficient handling of coumarin and nicotine.
CYP2A6 is a cytochrome P450 monooxygenase with high coumarin 7-hydroxylase activity. It is the major nicotine C-oxidase, activates aflatoxin B1, hydroxylates cyclophosphamide, ifosphamide and tegafur, and acts as a 1,4-cineole 2-exo-monooxygenase.
The protein is also called cytochrome P450 2A6, and aliases include CPA6, CYP2A and CYP2A3. The gene was formerly referred to as CYP2A3 before being renamed CYP2A6. Older HGNC names describe it as cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 6.
Yes. NCBI Gene notes that individuals with certain CYP2A6 allelic variants have a poor metabolizer phenotype and do not efficiently metabolise coumarin or nicotine. The gene lies in a cluster of CYP2A, CYP2B and CYP2F genes on chromosome 19q. Check the datasheet of any product for its validated reactivity.
Other CYP2A subfamily members, CYP2 family drug-metabolising enzymes and related cytochrome P450 targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P11509; product specifications from Assay Genie datasheets.