By David F.V. Lewis, David F. V. Lewis

ISBN-10: 0203213793

ISBN-13: 9780203213797

ISBN-10: 0748408975

ISBN-13: 9780748408979

Cytochromes are colored iron-containing proteins that move electrons in the course of mobile breathing and photosynthesis. The Cytochrome P450 relations of enzymes catalyze reactions wherein water-insoluble medicinal drugs or metabolites, that will differently succeed in poisonous degrees in mobile membranes, are rendered certainly water-soluble to depart the cellphone and be excreted within the urine. This reference stories the present prestige of the P450 box when it comes to our current wisdom and realizing of the enzymes' constitution and serve as, together with their multiplicity of types, range of substrates and selectivity. this is often introduced including the most recent study themes - together with pharmacogenetics, law, human DMEs, toxicity screening and molecule modelling - to supply a fast-track technique for these new to the sphere.

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Extra resources for Guide to Cytochromes P450: Structure and Function

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1999) between CYP2C9 polymorphisms and risk of bleeding complications from the use of the anticoagulant drug, warfarin. Mutants in human and other mammalian P450s are extremely useful for determining the likely sites of interaction with either substrates or redox partners of the P450 enzyme itself (Lewis, 1998a). Substrate recognition sites (SRSs) in the CYP2 family have been defined by Gotoh (1992) based on protein sequence 14 INTRODUCTION alignment of various CYP2 family enzymes. 3). Those amino acids which differ in allelic variants of the same P450 are emboldened, as are those which have been the subject of site-directed mutagenesis experiments (reviewed in Lewis, 1998a).

CO adduct MWt. 4). For example, it can be demonstrated that there is a ~ 99% correlation between apoprotein molecular weight and amino acid residue number for a variety of P450s (Lewis, 1996a). 4. , 1993), although the actual electronic absorption spectra extend into the visible region. , 1981; Gibson and Skett, 1994). The reasons for such characteristics in P450 electronic spectra are due to energy level transitions within the heme locus of the enzyme itself: these are profoundly influenced by the nature of the heme ligands, the environment of the heme moiety and the presence of a bound substrate or inhibitor (reviewed in Lewis, 1996a).

Consequently, it is possible that many plant toxins act upon the P450 systems of potential animal predators in a variety of ways, although these could be regarded as affecting the population size of both plant and animal species, thus achieving a self-regulatory balance over a period of time. This homeostatic mechanism for regulating population dynamics in co-evolutionary processes could represent an example, at the metabolic level, of the ‘Daisyworld’ hypothesis expounded by Lovelock (1988). Nebert and co-workers (1990) have elaborated upon the potential role of phytoalexins and other plant flavonoids in plant-animal ‘warfare’ via their action on the Ah receptor (AhR) and its associated gene battery which regulates the expression of CYP1 family P450s and related enzymes involved in metabolism.

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Guide to Cytochromes P450: Structure and Function by David F.V. Lewis, David F. V. Lewis


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