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Cited by 477

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Survey of Human Oxidoreductases and Cytochrome P450 Enzymes Involved in the Metabolism of Xenobiotic and Natural Chemicals

Open access
Rendic, Slobodan, Guengerich, F. Peter·2015·Chemical Research in Toxicology

Abstract

Analyzing the literature resources used in our previous reports, we calculated the fractions of the oxidoreductase enzymes FMO (microsomal flavin-containing monooxygenase), AKR (aldo-keto reductase), MAO (monoamine oxidase), and cytochrome P450 participating in metabolic reactions. The calculations show that the fractions of P450s involved in the metabolism of all chemicals (general chemicals, natural, and physiological compounds, and drugs) are rather consistent in the findings that >90% of enzymatic reactions are catalyzed by P450s. Regarding drug metabolism, three-fourths of the human P450 reactions can be accounted for by a set of five P450s: 1A2, 2C9, 2C19, 2D6, and 3A4, and the largest fraction of the P450 reactions is catalyzed by P450 3A enzymes. P450 3A4 participation in metabolic reactions of drugs varied from 13% for general chemicals to 27% for drugs.

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Metadata

Authors
Rendic, S., & Guengerich, F. P.
Venue
Chemical Research in Toxicology
Published
2014-12-19
Volume
28
Issue
1
Pages
38-42
ISSN
  • 0893-228X (ISSN-L)
  • 1520-5010
OpenAlex
W2322012164
Cited by
477
References
11
FWCI
19.63
Type
journal article
Language
en
Open access
hybrid

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.