(1997). Human Cytochrome P450 Enzymes: A Status Report Summarizing Their Reactions, Substrates, Inducers, and Inhibitors. Drug Metabolism Reviews: Vol. 29, No. 1-2, pp. 413-580.

Human Cytochrome P450 Enzymes: A Status Report Summarizing Their Reactions, Substrates, Inducers, and Inhibitors

This chapter is an update of the data on substrates, reactions, inducers, and inhibitors of human CYP enzymes published previously by Rendic and DiCarlo (1), now covering selection of the literature through 2001 in the reference section. The data are presented in a tabular form (Table 1) to provide a framework for predicting and interpreting the new P450 metabolic data. The data are formatted in an Excel format as most suitable for off-line searching and management of the Web-database. The data are presented as stated by the author(s) and in the case when several references are cited the data are presented according to the latest published information. The searchable database is available either as an Excel file (for information contact the author), or as a Web-searchable database (Human P450 Metabolism Database, www.gentest.com) enabling the readers easy and quick approach to the latest updates on human CYP metabolic reactions.

Summary of information on human cyp enzymes: human p450 metabolism data

In the past decade there has been considerable progress in the characterization of individual human P450 enzymes. These advances were initiated by early work on the purification of individual enzymes from human liver and other sources. The early work in the area was guided by a focus on the most abundant and easily purified enzymes.1–4It is now apparent, in retrospect, that these proteins were in the 2C and 3A families. Efforts were shifted to attempts to purify individual P450s on the basis of catalytic activities with the evidence that in some cases a single P450 could be identified in this way; e.g., the P450 now known as P450 2D6 was found to be under monogenic control. 5 The approach is technically demanding because of the need to do separations in the presence of detergents and then remove them before analysis of catalytic activity. Nevertheless, human P450s 1A1,6 1A2,7 2A6,8 2C8,9 2C9,9,10 2D67,11,12 2E1 13,14 3A4,15 3A5,16 4A11,17 and lanosterol 14α-demethylase18 were isolated in this general manner. Another approach that has been used, sometimes in a mode complementary to catalytic specificity, is purification on the basis of immunochemical similarity to animal P450s. 7,11,19,20

Human Cytochrome P450 Enzymes

The genetic polymorphism of debrisoquine/sparteine metabolism — Clinical aspects

In this review, an overview is presented of the current knowledge of genetic polymorphisms of four of the most important enzyme families involved in the metabolism of xenobiotics, that is, the N-acetyltransf erase (NAT), cytochrome P450 (P450), glutathione-S-transferase (GST), and microsomal epoxide hydrolase (mEH) enzymes. The emphasis is on two main topics, the molecular genetics of the polymorphisms and the consequences for xenobiotic metabolism and toxicity. Studies are described in which wild-type and mutant alleles of biotransformation enzymes have been expressed in heterologous systems to study the molecular genetics and the metabolism and pharmacological or toxicological effects of xenobiotics. Furthermore, studies are described that have investigated the effects of genetic polymorphisms of biotransformation enzymes on the metabolism of drugs in humans and on the metabolism of genotoxic compounds in vivo as well. The effects of the polymorphisms are highly dependent on the enzyme systems involved ...

Genetic polymorphisms of human N-acetyltransferase, cytochrome P450, glutathione-S-transferase, and epoxide hydrolase enzymes: relevance to xenobiotic metabolism and toxicity.

1. The qualitative and quantitative aspects of the urinary elimination of orally administered 4-methoxy[14C]amphetamine have been examined in the rat and guinea-pig and in three volunteer human subjects, to determine interspecies and interindividual variations in disposition of the drug.2. Both rat and guinea-pig excreted 70-80% of the administered dose (6 mg/kg) in the urine within 24 h, mainly as metabolites.3. In the guinea-pig, the drug was metabolized by O-demethylation to give 4-hydroxyamphetamine, which was excreted free (4% dose) and conjugated (73%). No other metabolite was detected.4. The rat metabolizes the drug both by O-dealkylation and by side-chain oxidation, the products being 4-hydroxyamphetamine (5% of dose free and 60% conjugated) and 1-(4'-methoxyphenyl)propan-2-one oxime (5% dose, free and conjugated).5. In man the drug (dose 5 mg) is metabolized by O-demethylation and by side-chain oxidation. Marked intersubject variations were observed both in the array and quantitative aspects of m...

Interindividual and interspecies variation in the metabolism of the hallucinogen 4-methoxyamphetamine.

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Interindividual and interspecies variation in the metabolism of the hallucinogen 4-methoxyamphetamine.