Cytochrome p450 structure mechanism and biochemistry pdf

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cytochrome p450 structure mechanism and biochemistry pdf

Cytochrome P - Structure, Mechanism, and Biochemistry | Paul R. Ortiz de Montellano | Springer

Cytochrome P, CYP, cytochrome c peroxidase, heme-thiolate proteins, reaction mechansim. A Rosetta Stone—surely that description applies aptly today to the large superfamily of cytochrome P CYP enzymes, as well as related peroxidases, that have revealed so much about biochemical and chemical biological oxidation. Here, the languages have been the imaginative and interconnected application of structural, mechanistic, and spectroscopic idioms 1 , 2. CYP proteins have long been known to mediate the oxidative processes involved in phase 1 drug metabolism, which occur in the liver. It has become increasingly important to identify these drug metabolites and to determine the extent to which they are toxic or actually the active form of the administered drug.
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Cytochrome P450 oxidase enzyme function and co-factors/enzymes

Recent Structural Insights into Cytochrome P450 Function

Cytochrome P P enzymes are important in the metabolism of drugs, steroids, fat-soluble vitamins, carcinogens, pesticides, and many other types of chemicals. Their catalytic activities are important issues in areas such as drug-drug interactions and endocrine function. During the past 30 years, structures of Ps have been very helpful in understanding function, particularly the mammalian P structures available in the past 15 years. We review recent activity in this area, focusing on the past two years — Structural work with microbial Ps includes studies related to the biosynthesis of natural products and the use of parasitic and fungal P structures as targets for drug discovery.

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Cytochromes P CYPs are a family of enzymes containing heme as a cofactor that function as monooxygenases. In plants, these proteins are important for the biosynthesis of defensive compounds , fatty acids, and hormones. CYP enzymes have been identified in all kingdoms of life: animals , plants , fungi , protists , bacteria , archaea , and even in viruses. CYPs are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as Pcontaining systems. Most CYPs require a protein partner to deliver one or more electrons to reduce the iron and eventually molecular oxygen. Genes encoding CYP enzymes, and the enzymes themselves, are designated with the root symbol CYP for the superfamily , followed by a number indicating the gene family , a capital letter indicating the subfamily, and another numeral for the individual gene. The convention is to italicise the name when referring to the gene.

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