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Cytochrome P450

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<StructureSection load='1og5' size='350' side='right' caption='Cytochrome P450 tetramer with heme and sulfate ions (PDB entry [[2f9q]])' scene=''>
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<StructureSection load='1og5' size='350' side='right' caption='Cytochrome P450 CypC2 tetramer with heme complex with warfarin (PDB entry [[1og5]])' scene=''>
[[Cytochrome P450]] (P450) 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> For details on the human P45019 family see [[Aromatase]].<br />
[[Cytochrome P450]] (P450) 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> For details on the human P45019 family see [[Aromatase]].<br />
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* '''Bifunctional P450/NADPH P450 reductase''' (P450 BM3) is a fatty acid monooxygenase.<br />
* '''Bifunctional P450/NADPH P450 reductase''' (P450 BM3) is a fatty acid monooxygenase.<br />
Additional details in [[Drug Metabolism by CYP450 Enzymes]].
Additional details in [[Drug Metabolism by CYP450 Enzymes]].
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== Structural highlights ==
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The heme moiety iron is pentacoordinated with Cys as one ligand. The heme is stabilized by several side chains.
</StructureSection>
</StructureSection>
== 3D Structures of Cytochrome P450 ==
== 3D Structures of Cytochrome P450 ==

Revision as of 09:51, 20 December 2015

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

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3D Structures of Cytochrome P450

Updated on 20-December-2015

References

  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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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