期刊
ACS CHEMICAL BIOLOGY
卷 11, 期 4, 页码 1039-1048出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.5b01016
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资金
- Austrian science fund (Elise-Richter fellowship) [V415-B21]
- Federal Ministry of Science, Research and Economy (BMWFW)
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol
- Government of Lower Austria
- ZIT-Technology Agency of the City of Vienna through the COMET-Funding Program - Austrian Research Promotion Agency FFG
Flavin-containing mono-oxygenases are known as potent drug metabolizing enzymes, providing complementary functions to the well-investigated cytochrome P450 mono-oxygenases. While human FMO isoforms are typically involved in the oxidation of soft nucleophiles, the biocatalytic activity of human FMOS (along its physiological role) has long remained unexplored. In this study, we demonstrate the atypical in vitro activity of human FMOS as a Baeyer-Villiger mono-oxygenase on a broad range of substrates, revealing the first example to date of a human protein catalyzing such reactions. The isolated and purified protein was active on diverse carbonyl compounds, whereas soft nucleophiles were mostly non- or poorly reactive. The absence of the typical characteristic sequence motifs sets human FMOS apart from all characterized Baeyer-Villiger mono-oxygenases so far. These findings open new perspectives in human oxidative metabolism.
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