Function
Cytochrome P450 (P450) or cytochrome P450 monooxygenase catalyzes the oxidation of organic substances like lipids. The P450 contains a heme cofactor. The protein is numbered by its gene.[1] P450 CYP121 is called mycocyclosin synthase.
See also Hemeproteins.
Additional details on cytochrome P450 interactions with drugs see
Structural highlights
The heme moiety is stabilized by several side chains. The heme iron is pentacoordinated with Cys as one ligand.[6]
3D Structures of Cytochrome P450
Cytochrome P450 3D structures
- ↑ Danielson PB. The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr Drug Metab. 2002 Dec;3(6):561-97. PMID:12369887
- ↑ Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG. The catalytic pathway of cytochrome p450cam at atomic resolution. Science. 2000 Mar 3;287(5458):1615-22. PMID:10698731
- ↑ Daiber A, Shoun H, Ullrich V. Nitric oxide reductase (P450nor) from Fusarium oxysporum. J Inorg Biochem. 2005 Jan;99(1):185-93. PMID:15598501 doi:10.1016/j.jinorgbio.2004.09.018
- ↑ Nagano S, Li H, Shimizu H, Nishida C, Ogura H, Ortiz de Montellano PR, Poulos TL. Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK. J Biol Chem. 2003 Nov 7;278(45):44886-93. Epub 2003 Aug 21. PMID:12933799 doi:https://dx.doi.org/10.1074/jbc.M308115200
- ↑ Stok JE, Slessor KE, Farlow AJ, Hawkes DB, De Voss JJ. Cytochrome P450cin (CYP176A1). Adv Exp Med Biol. 2015;851:319-39. PMID:26002741 doi:10.1007/978-3-319-16009-2_12
- ↑ Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H. Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:12861225 doi:https://dx.doi.org/10.1038/nature01862
