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.
|Title of host publication||Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods|
|Editors||R. Hille, S.M. Miller, B. Palfey|
|Place of Publication||Berlin|
|Number of pages||500|
|Publication status||Published - 2013|