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Biology 2018, 7(3), 42;

Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities

Institute of Biosciences, Environmental Microbiology, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany
Laboratory of Biochemistry, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, The Netherlands
Department of Chemistry and Biochemistry, San Francisco State University, 1600 Holloway Avenue, San Francisco, CA 94132, USA
Allgemeine Biochemie, Technische Universität Dresden, 01062 Dresden, Germany
Microbial Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780 Bochum, Germany
Author to whom correspondence should be addressed.
Received: 31 May 2018 / Revised: 31 July 2018 / Accepted: 1 August 2018 / Published: 2 August 2018
(This article belongs to the Special Issue The Mechanism of Enzymatic Action)
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Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aromatic compounds, and biosynthesis of secondary metabolites. The monooxygenase component of these enzymes is strictly dependent on reduced FAD, which is supplied by the reductase component. More and more representatives of two-component FAD-dependent monooxygenases have been discovered and characterized in recent years, which has resulted in the identification of novel physiological roles, functional properties, and a variety of biocatalytic opportunities. View Full-Text
Keywords: hydroxylation; epoxidation; halogenation; heteroatom oxidation; biocatalysis; flavoprotein monooxygenases; flavin reductase hydroxylation; epoxidation; halogenation; heteroatom oxidation; biocatalysis; flavoprotein monooxygenases; flavin reductase

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Heine, T.; Van Berkel, W.J.H.; Gassner, G.; Van Pée, K.-H.; Tischler, D. Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities. Biology 2018, 7, 42.

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