CYP2F1

From Wikipedia, the free encyclopedia

Cytochrome P450, family 2, subfamily F, polypeptide 1

Identifiers

CYP2F1; C2F1; CYP2F; MGC126121

External IDs

OMIM: 124070 MGI: 88608 HomoloGene: 73898

Gene ontology
Molecular Function:	• monooxygenase activity • iron ion binding • oxygen binding • heme binding • metal ion binding • unspecific monooxygenase activity
Cellular Component:	• endoplasmic reticulum • microsome • membrane
Biological Process:	• electron transport

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_000774 (mRNA)
NP_000765 (protein)

NM_007817 (mRNA)
NP_031843 (protein)

Location

n/a

Chr 7: 26.83 - 26.84 Mb

Pubmed search

[1]

[2]

Cytochrome P450, family 2, subfamily F, polypeptide 1, also known as CYP2F1, is a human gene.^[1]

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is known to dehydrogenate 3-methylindole, an endogenous toxin derived from the fermentation of tryptophan, as well as xenobiotic substrates such as naphthalene and ethoxycoumarin. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.^[1]

[edit] References

^ ^a ^b Entrez Gene: CYP2F1 cytochrome P450, family 2, subfamily F, polypeptide 1.

[edit] Further reading

Nhamburo PT, Kimura S, McBride OW, et al. (1990). "The human CYP2F gene subfamily: identification of a cDNA encoding a new cytochrome P450, cDNA-directed expression, and chromosome mapping.". Biochemistry 29 (23): 5491–9. PMID 1974816.
Bale AE, Mitchell AL, Gonzalez FJ, McBride OW (1991). "Localization of CYP2F1 by multipoint linkage analysis and pulsed-field gel electrophoresis.". Genomics 10 (1): 284–6. PMID 2045106.
Trask B, Fertitta A, Christensen M, et al. (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers.". Genomics 15 (1): 133–45. PMID 8432525.
Hoffman SM, Fernandez-Salguero P, Gonzalez FJ, Mohrenweiser HW (1996). "Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19.". J. Mol. Evol. 41 (6): 894–900. PMID 8587134.
Hakkola J, Pasanen M, Hukkanen J, et al. (1996). "Expression of xenobiotic-metabolizing cytochrome P450 forms in human full-term placenta.". Biochem. Pharmacol. 51 (4): 403–11. PMID 8619884.
Andersen MR, Farin FM, Omiecinski CJ (1998). "Quantification of multiple human cytochrome P450 mRNA molecules using competitive reverse transcriptase-PCR.". DNA Cell Biol. 17 (3): 231–8. PMID 9539103.
Lanza DL, Code E, Crespi CL, et al. (1999). "Specific dehydrogenation of 3-methylindole and epoxidation of naphthalene by recombinant human CYP2F1 expressed in lymphoblastoid cells.". Drug Metab. Dispos. 27 (7): 798–803. PMID 10383923.
Chen N, Whitehead SE, Caillat AW, et al. (2002). "Identification and cross-species comparisons of CYP2F subfamily genes in mammals.". Mutat. Res. 499 (2): 155–61. PMID 11827709.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Carr BA, Wan J, Hines RN, Yost GS (2003). "Characterization of the human lung CYP2F1 gene and identification of a novel lung-specific binding motif.". J. Biol. Chem. 278 (18): 15473–83. doi:10.1074/jbc.M300319200. PMID 12598524.
Tournel G, Cauffiez C, Billaut-Laden I, et al. (2007). "Molecular analysis of the CYP2F1 gene: identification of a frequent non-functional allelic variant.". Mutat. Res. 617 (1-2): 79–89. doi:10.1016/j.mrfmmm.2007.01.007. PMID 17327131.