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Unusual cytochrome p450 enzymes and reactions.

Guengerich FP, Munro AW
J Biol Chem. 2013 288 (24): 17065-73

PMID: 23632016 · PMCID: PMC3682512 · DOI:10.1074/jbc.R113.462275

Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high-valent iron-oxygen complex (FeO(3+)), to explain seemingly unusual reactions, including ring couplings, ring expansion and contraction, and fusion of substrates. Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H. In some cases, P450s are fused to protein partners. Other P450s catalyze non-redox isomerization reactions. A number of permutations on the P450 theme reveal the diversity of cytochrome P450 form and function.

MeSH Terms (9)

Animals Biocatalysis Coenzymes Cytochrome P-450 Enzyme System Humans Hydroxylation Oxidation-Reduction Prostaglandins Recombinant Fusion Proteins

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