{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:05:01Z","timestamp":1762099501221},"reference-count":69,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2001,12,28]],"date-time":"2001-12-28T00:00:00Z","timestamp":1009497600000},"content-version":"vor","delay-in-days":361,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Environ and Mol Mutagen"],"published-print":{"date-parts":[[2001,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A series of <jats:italic>Salmonella typhimurium<\/jats:italic> (<jats:italic>S. typhimurium<\/jats:italic>) YG7108 strains, each coexpressing a form of human cytochrome P450 (CYP) (CYP1A1, CYP1A2, CYP1B1, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP3A4, or CYP3A5) together with human NADPH\u2013cytochrome P450 reductase (OR), was established. The parental <jats:italic>S. typhimurium<\/jats:italic> YG7108, derived from TA1535, lacks two <jats:italic>O<\/jats:italic><jats:sup>6<\/jats:sup>\u2010methylguanine\u2010DNA methyltransferase genes, <jats:italic>ada<\/jats:italic> and <jats:italic>ogt,<\/jats:italic> and is highly sensitive to the mutagenicity of alkylating agents. The expression levels of CYP holo\u2010protein in the genetically engineered <jats:italic>S. typhimurium<\/jats:italic> YG7108 cells, determined by carbon monoxide (CO) difference spectra, ranged from 62 nmol\/L culture for CYP2C19 to 169 nmol\/L culture for CYP3A4. The expression level of the OR varied, depending on the form of CYP coexpressed, and ranged from 214 to 1029 units\/L culture. Each form of CYP expressed in the <jats:italic>S. typhimurium<\/jats:italic> YG7108 cells catalyzed the oxidation of a representative substrate at an efficient rate. The rates appeared comparable to the reported activities of CYP expressed in human liver microsomes or CYP in other heterologous systems, indicating that the OR was sufficiently expressed to support the catalytic activity of CYP. These <jats:italic>S. typhimurium<\/jats:italic> strains may be useful not only for predicting the metabolic activation of promutagens catalyzed by human CYP but also for identifying the CYP form involved. Environ. Mol. 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