CYP2A6

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cytochrome P450, family 2, subfamily A, polypeptide 6
Identifiers
Symbol(s)	CYP2A6 CYP2A3
Entrez	1548
OMIM	122720
RefSeq	NM_000762
UniProt	P11509
Other data
Locus	Chr. 19 q13.2

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.

1 Distribution
2 Variability
3 Induction
4 CYP2A6 Ligands
5 References

[edit] Distribution

CYP2A6 is found predominantly in the liver.

[edit] Variability

Significant interindividual variability in CYP2A6 apoprotein and mRNA levels has been observed.

[edit] Induction

CYP2A6 is known to be inducible by phenobarbital and rifampicin, and it is suspected that other antiepileptic drugs may also have this effect.

[edit] CYP2A6 Ligands

Selected inducers, inhibitors and substrates of CYP2A6
Type	Agent
inducers	phenobarbital, rifampicin
inhibitors	(grapefruit juice flavonoids), ketoconazole, methoxsalen, pilocarpine, tranylcypromine
substrates	aflatoxin B₁, 1,3-butadiene, cotinine, coumarin, DCBN, 7-ethoxycoumarin, halothane, losigamone, methoxyflurane, 3-methylindole, MNAN, MTBE, MOCA, NDEA, nicotine, NNK, quinoline, SM-12502, valproic acid