Cytochrome P450 2F1 is a protein that in humans is encoded by the CYP2F1gene.[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]
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. doi:10.1021/bi00475a012. PMID1974816.
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. doi:10.1016/0888-7543(91)90514-F. PMID2045106.
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. doi:10.1006/geno.1993.1021. PMID8432525.
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. doi:10.1007/bf00173169. PMID8587134.
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. doi:10.1016/0006-2952(95)02184-1. PMID8619884.
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. doi:10.1089/dna.1998.17.231. PMID9539103.
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. PMID10383923.
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. doi:10.1016/S0027-5107(01)00274-3. PMID11827709.
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. PMID12598524.
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. PMID17327131.