CYP1A1

From Wikipedia, the free encyclopedia

Cytochrome P450, family 1, subfamily A, polypeptide 1

Identifiers

CYP1A1; AHH; AHRR; CP11; CYP1; P1-450; P450-C; P450DX

External IDs

OMIM: 108330 MGI: 88588 HomoloGene: 68062

Gene ontology
Molecular Function:	• iron ion binding • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen • oxygen binding • heme binding • metal ion binding • unspecific monooxygenase activity
Cellular Component:	• endoplasmic reticulum • microsome • membrane
Biological Process:	• electron transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000499 (mRNA)
NP_000490 (protein)

XM_972645 (mRNA)
XP_977739 (protein)

Location

Chr 15: 72.8 - 72.8 Mb

Chr 9: 57.45 - 57.5 Mb

Pubmed search

[1]

[2]

CYP1A1 is a gene that encodes a member of the cytochrome P450 superfamily of enzymes. It is primarily involved in xenobiotic and drug metabolism (one substrate of it is theophylline). It is inhibited by fluoroquinolones and macrolides; induced by aromatic hydrocarbons. There are 3 main subtypes of CYP1A: M1, M2 and M3.

CYP1A1 and CYP1B1 are regulated by the Aryl hydrocarbon receptor, a ligand activated transcription factor. They are part of the Phase I reactions in drug metabolism.

CYP1A1 is also known as AHH (aryl hydrocarbon hydroxylase). It is involved in the metabolic activation of aromatic hydrocarbons (polycyclic aromatic hydrocarbons, PAH), for example, benzopyrene (BP), by transforming it to epoxide. In this reaction, benzo[a]pyrene is catalysed by CYP1A1 to form BP-7,8-epoxide, then it can be further oxidized by epoxide hydrolase (EH) to form BP-7,8-dihydrodiol, and finally CYP1A1 catalyses such intermediate molecule to form BP-7,8-dihydrodiol-9,10-epoxide, which is the ultimate carcinogen.

[edit] References

[edit] Further reading

Beresford AP (1994). "CYP1A1: friend or foe?". Drug Metab. Rev. 25 (4): 503–17. PMID 8313840.
Smith G, Stubbins MJ, Harries LW, Wolf CR (1999). "Molecular genetics of the human cytochrome P450 monooxygenase superfamily.". Xenobiotica 28 (12): 1129–65. PMID 9890157.
Kawajiri K (1999). "CYP1A1.". IARC Sci. Publ. (148): 159–72. PMID 10493257.
Nelson DR, Zeldin DC, Hoffman SM, et al. (2004). "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.". Pharmacogenetics 14 (1): 1–18. PMID 15128046.
Masson LF, Sharp L, Cotton SC, Little J (2005). "Cytochrome P-450 1A1 gene polymorphisms and risk of breast cancer: a HuGE review.". Am. J. Epidemiol. 161 (10): 901–15. doi:10.1093/aje/kwi121. PMID 15870154.
Hildebrandt AG, Schwarz D, Krusekopf S, et al. (2007). "Recalling P446. P4501A1 (CYP1A1) opting for clinical application.". Drug Metab. Rev. 39 (2-3): 323–41. doi:10.1080/03602530701498026. PMID 17786624.

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v • d • e Cytochromes, oxygenases: cytochrome P450 (EC 1.14)

CYP1	A1, A2, B1

CYP2	A6, A7, A13, B6, C8, C9, C18, C19, D6, E1, F1, J2, R1, S1, U1, W1

CYP3	A4, A5, A7, A43

CYP4	A11, A22, B1, F2, F3, F8, F11, F12, F22, V2, X1, Z1

CYP5-20	CYP5 (A1) - CYP7 (A1, B1) - CYP8 (A1, B1) - CYP11 (A1, B1, B2) - CYP17 (A1) - CYP19 (A1) - CYP20 (A1)

CYP21-51	CYP21 (A2) - CYP24 (A1) - CYP26 (A1, B1, C1) - CYP27 (A1, B1, C1) - CYP39 (A1) - CYP46 (A1) - CYP51 (A1)