Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 441594
Title The flavin monooxygenases
Author(s) Montersino, S.; Berkel, W.J.H. van
Source In: Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods / Hille, R., Miller, S.M., Palfey, B., Berlin : De Gruyter - ISBN 9783110298284 - p. 51 - 72.
Department(s) Biochemistry
Publication type Peer reviewed book chapter
Publication year 2013
Abstract Flavin monooxygenases are ubiquitous enzymes that catalyze a wide variety of regio -and enantioselective oxygenation reactions via the formation of a fl avin C4a-(hydro)peroxide intermediate. Based on fold and function, fl avin monooxygenases can be divided into six subfamilies. Subclasses A and B comprise single-component enzymes that rely on NAD(P)H as electron donor. Subclasses C–F comprise two-component enzymes , composed of a fl avin reductase and a fl avin-specifi c monooxygenase . FAD-containing hydroxylases (subclass A ) convert many (hetero)aromatic substrates ranging from monophenols and uric acids to polyketide antibiotics and antitumor agents. FAD-containing monooxygenases (subclass B ) perform Baeyer-Villiger oxidation, sulfoxidation and heteroatom hydroxylation reactions. FMN-dependent TIM-barrel enzymes (subclass C ) catalyze Baeyer-Villiger oxidation, hydroxylation of long-chain alkanes and nitriloacetate, oxidation and desulfurization of sulfonates, and oxidation of aldehydes coupled with generation of bioluminescence. FMN/FAD hydroxylases with an acyl-CoA dehydrogenase fold (subclass D ) convert mono- and polyphenols. FAD-specifi c styrene monooxygenases (subclass E ) oxidize styrene derivatives to the corresponding epoxides. FAD-specifi c halogenases (subclass F ) catalyze the regioselective chlorination and bromination of activated organic molecules for the production of antibiotics, antitumor agents and other natural products. During the past few years, many new family members and several unprecedented fl avin monooxygenase reactions have emerged. This review illustrates selected features, tools to retrieve novel fl avin monooxygenases from genome mining, and new findings on each of the six subclasses.
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