Jump to content

CYP2A6

From Wikipedia, the free encyclopedia
(Redirected from CYP2A)

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; OMA:CYP2A6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.

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.[5]

Interactive pathway map

[edit]

Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

[[File:
FluoropyrimidineActivity_WP1601go to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to PubChem Compoundgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
[[
]]
FluoropyrimidineActivity_WP1601go to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to PubChem Compoundgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to pathway articlego to pathway articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
|alt=Fluorouracil (5-FU) Activity edit]]
Fluorouracil (5-FU) Activity edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

Distribution

[edit]

CYP2A6 localizes to the endoplasmic reticulum and is found predominantly in the liver.

Variability

[edit]

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

Induction

[edit]

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

CYP2A6 Ligands

[edit]
Selected inducers, inhibitors and substrates of CYP2A6
Substrates Inhibitors Inducers

See also

[edit]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000255974Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005547Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Public Domain This article incorporates public domain material from "Entrez Gene: CYP2A6 cytochrome P450, family 2, subfamily A, polypeptide 6". Reference Sequence collection. National Center for Biotechnology Information.
  6. ^ a b c d e f g h i j k l m n o p q r s t u v w x y z aa ab ac ad Lacy CF, Armstrong LL, Goldman MP, Lance LL (2007). Cytochrome P450 Enzymes: Substrates, Inhibitors, and Inducers. Hudson, OH: LexiComp Inc. pp. 1899–1912.
  7. ^ Wen X, Wang JS, Neuvonen PJ, Backman JT (2002). "Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes". Eur. J. Clin. Pharmacol. 57 (11): 799–804. doi:10.1007/s00228-001-0396-3. PMID 11868802. S2CID 19299097.
  8. ^ Siu EC, Tyndale RF (2008). "Selegiline is a mechanism-based inactivator of CYP2A6 inhibiting nicotine metabolism in humans and mice". J. Pharmacol. Exp. Ther. 324 (3): 992–9. doi:10.1124/jpet.107.133900. PMID 18065502. S2CID 9833233.

Further reading

[edit]
[edit]