Cytochrome P450: Difference between revisions

Latest revision as of 11:03, 6 January 2025

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Cytochrome P450 CypC2 with heme C complex with warfarin (PDB entry 1og5)

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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.

P450cam, also known as camphor 5-monooxygenase, catalyzes the hydroxylation of camphor^[2].
P450nor is a Nitric Oxide Reductase P450^[3].
P450epoK converts epothilone D to epothilone B^[4].
P450cin monooxygenates 1,8-cineole which is similar to camphor^[5].
Bifunctional P450/NADPH P450 reductase (P450 BM3) is a fatty acid monooxygenase.
P450 3A4 see CYP3A4.
P450 19 family see Aromatase.
P450 17A1 see Human steroidogenic cytochrome P450 17A1 with inhibitor abiraterone

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

References

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Joel L. Sussman, Michal Harel

[1] Danielson PB. The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr Drug Metab. 2002 Dec;3(6):561-97. PMID:12369887

[2] 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

[3] 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

[4] 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

[5] 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

[6] 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

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-[[Image:2f9q.png|left|200px|thumb|Crystal Structure of Cytochrome P450 [[2f9q]]]]
+<StructureSection load='' size='350' side='right' caption='Cytochrome P450 CypC2 with heme C complex with warfarin (PDB entry [[1og5]])' scene='43/430105/Cv/2'>
-{{STRUCTURE_2f9q|  PDB=2f9q  | SIZE=300| SCENE= |right|CAPTION=Cytochrome P450 [[2f9q]] }}
+__TOC__
+== 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.<ref>PMID:12369887</ref> P450 CYP121 is called '''mycocyclosin synthase'''.
+*  '''P450cam''', also known as camphor 5-monooxygenase, catalyzes the hydroxylation of camphor<ref>PMID:10698731</ref>.<br />
+* '''P450nor''' is a Nitric Oxide Reductase P450<ref>PMID:15598501</ref>.<br />
+*  '''P450epoK''' converts epothilone D to epothilone B<ref>PMID:12933799</ref>.<br />
+*  '''P450cin''' monooxygenates 1,8-cineole which is similar to camphor<ref>PMID:26002741</ref>.<br />
+*  '''Bifunctional P450/NADPH P450 reductase''' (P450 BM3) is a fatty acid monooxygenase.<br />
+*  '''P450 3A4''' see [[CYP3A4]].<br />
+*  '''P450 19 family''' see [[Aromatase]].<br />
+* '''P450 17A1''' see [[Abiraterone acetate|Human steroidogenic cytochrome P450 17A1 with inhibitor abiraterone]]
+See also [[Hemeproteins]].
+Additional details on cytochrome P450 interactions with drugs see
+*[[Drug Metabolism by CYP450 Enzymes]]<br />
+*[[Montelukast]] - anti rhinitis
+*[[Noxafil]] - antifungal drug which binds to CYP51.
+*[[Antifungal drugs]] - antifungal drugs which binds to CYP51.
+*[[Cobicistat]] - anti HIV/AIDS drug which binds to CYP3A4.
+*[[Cytochrome P450 inhibitors]]
+== Structural highlights ==
+The <scene name='43/430105/Cv/6'>heme moiety is stabilized by several side chains</scene>.  The <scene name='43/430105/Cv/7'>heme iron is pentacoordinated with Cys as one ligand</scene>.<ref>PMID:12861225</ref>
+== 3D Structures of Cytochrome P450  ==
+[[Cytochrome P450  3D structures]]
+</StructureSection>
+== References ==
+<references/>
+[[Category:Topic Page]]

Cytochrome P450: Difference between revisions

Latest revision as of 11:03, 6 January 2025

Contents

Function

Structural highlights

3D Structures of Cytochrome P450

References

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