By John B. Schenkman (auth.), Emel Arinç, John B. Schenkman, Ernest Hodgson (eds.)
Written through prime researchers within the fields of biochemistry, molecular biology, genetics, pharmacology, toxicology, biotechnology and melanoma, it is a complete replace on molecular biology and biochemistry of cytochromes P450 and flavin containing monoxygenases. the amount offers specialist research of the genetic polymorphism of those enzymes within the hospital, in drug discovery and improvement, and dialogue in their function in predisposition for, and prevention of chemical cancer causing agents in people.
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Extra info for Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes
Html). In key regions of the tertiary structure of these forms, regions that are suggested from x-ray crystallography to be involved in heme anchoring, oxygen activation and substrate binding, high levels of sequence identity are seen. In 1983 it was noted that some forms of cytochrome P450 have an amino acid sequence corresponding to the substrate recognition sequence, RRXS, of the cyclic AMP-dependent protein kinase, where X represents a hydrophobic residue such as phenylalanine. Incubation of one of these forms, CYP2B4, with cAMP and the protein kinase resulted in phosphorylation of the hemoprotein.
60:771-778. 26. Jansson 1, Schenkman J (1973) Evidence against participation of cytochrome b5 in the hepatic microsomal mixed function oxidase reaction. Mol. Pharmacol. 9:840-845. 27. Lu AYH, Levin W, Selander H, Jerina DM (1974) Liver microsomal electron transport systems. III. The involvement of cytochrome b5 in the NADPH-supported cytochrome P-450-dependent hydroxylation of chlorobenzene. Biochem. Biophys. Res. Commun. 61: 1348-1355. 28. Morgan E, Coon M (1984) Effects of cytochrome b5 on cytochrome P-450-catalyzed reactions.
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