Cytochrome P - WikipediaCytochromes 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.
Biochemistry of cytochrome P 450 enzymes
Summary: Cytochrome P450
It seems that you're in Germany. We have a dedicated site for Germany. This authoritative Fourth Edition summarizes the advances of the past decade concerning the structure, mechanism, and biochemistry of cytochrome P enzymes, with sufficient coverage of earlier work to make each chapter a comprehensive review of the field. Thirteen chapters are divided into two detailed volumes, the first covering the fundamentals of cytochrome P biochemistry, as well as the microbial, plant, and insect systems, and the second exclusively focusing on mammalian systems. Volume 1 begins with an exploration of the biophysics and mechanistic enzymology of cytochrome P enzymes, with a discussion of the structures of P enzymes and their electron donor partners, the mechanisms of oxygen activation and substrate oxidation, and the approaches and nature of cytochrome P inhibition.
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. For example, the platelet aggregation inhibitor, Plavix, which contains a thiophene ring, is a prodrug, inactive in its administrated form, which is first transformed by liver P enzymes to a thiolactone structure. The active form of the drug evolves subsequently in a second, hydrolytic step Figure 1.
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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. They were implicated in a number of reactions involved in the metabolism of drugs, steroids, and carcinogens, which had already been demonstrated [ 2 — 4 ]. Because of this, the repertoire of fields in which Ps are of interest has expanded to include bioremediation, agriculture, bacteriology, and drug development.