CYP2A6

Cytochrome P450 2A6 (abbreviated CYP2A6) is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. CYP2A6 is the primary enzyme responsible for the oxidation of nicotine and cotinine. It is also involved in the metabolism of several pharmaceuticals, carcinogens, and a number of coumarin-type alkaloids. CYP2A6 is the only enzyme in the human body that appreciably catalyzes the 7-hydroxylation of coumarin, such that the formation of the product of this reaction, 7-hydroxycoumarin, is used as a probe for CYP2A6 activity.

CYP2A6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCYP2A6, CPA6, CYP2A, CYP2A3, CYPIIA6, P450C2A, P450PB, cytochrome P450 family 2 subfamily A member 6
External IDsOMIM: 122720 MGI: 88597 HomoloGene: 85917 GeneCards: CYP2A6
Orthologs
SpeciesHumanMouse
Entrez

1548

13087

Ensembl

ENSG00000255974

ENSMUSG00000005547

UniProt

P11509

P20852

RefSeq (mRNA)

NM_000762

NM_007812

RefSeq (protein)

NP_000753

n/a

Location (UCSC)Chr 19: 40.84 – 40.85 MbChr 7: 26.53 – 26.54 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

The CYP2A6 gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The gene was formerly referred to as CYP2A3; however, it has been renamed CYP2A6.

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