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• W2169389640 abstract "In recent studies, the wild-type and mutant forms of cytochrome P450 (P450) BM3 (CYP102A1) from <i>Bacillus megaterium</i> were found to metabolize various drugs through reactions similar to those catalyzed by human P450 enzymes. Therefore, it was suggested that CYP102A1 can be used to produce large quantities of the metabolites of human P450-catalyzed reactions. <i>trans</i>-Resveratrol (3,4′,5-trihydroxystilbene), an anticancer-preventive agent, is oxidized by human P450 1A2 to produce two major metabolites, piceatannol (3,5,3′,4′-tetrahydroxystilbene) and another hydroxylated product. In this report, we show that the oxidation of <i>trans</i>-resveratrol, a human P450 1A2 substrate, is catalyzed by wild-type and a set of CYP102A1 mutants. One major hydroxylated product, piceatannol, was produced as a result of the hydroxylation reaction. Other hydroxylated products were not produced. Piceatannol formation was confirmed by high-performance liquid chromatography and gas chromatograph-mass spectrometry by comparing the metabolite with the authentic piceatannol compound. These results demonstrate that CYP102A1 mutants can be used to produce piceatannol, a human metabolite of resveratrol." @default.
• W2169389640 created "2016-06-24" @default.
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• W2169389640 date "2009-02-23" @default.
• W2169389640 modified "2023-09-30" @default.
• W2169389640 title "Generation of the Human Metabolite Piceatannol from the Anticancer-Preventive Agent Resveratrol by Bacterial Cytochrome P450 BM3" @default.
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• W2169389640 doi "https://doi.org/10.1124/dmd.108.026484" @default.
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