Elucidation of catalytic specificities of human cytochrome P450 and glutathione S-transferase enzymes and relevance to molecular epidemiology.
Author(s) -
F. Peter Guengerich,
Tsutomu Shimada,
Kevin D. Raney,
ChulHo Yun,
David J. Meyer,
B Ketterer,
Thomas M. Harris,
John D. Groopman,
Fred F. Kadlubar
Publication year - 1992
Publication title -
environmental health perspectives
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.257
H-Index - 282
eISSN - 1552-9924
pISSN - 0091-6765
DOI - 10.1289/ehp.929875
Subject(s) - cytochrome p450 , enzyme , detoxication , biochemistry , isozyme , glutathione transferase , glutathione , human liver , glutathione s transferase , pyrrolizidine , xenobiotic , chemistry , pyrrolizidine alkaloid , biology , stereochemistry
A number of different approaches have been used to determine the catalytic selectivity of individual human enzymes toward procarcinogens. Studies with cytochrome P450 (P450) enzymes and glutathione S-transferases are summarized here, and recent work with pyrrolizidine alkaloids, aflatoxins, 4,4'-methylenebis(2-chloroaniline), and ethyl carbamate is discussed. In some cases a single enzyme can catalyze both activation and detoxication reactions of a chemical. The purification and characterization of human lung P4501A1 and the development of a noninvasive assay for human P4502E1 are also described.
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