Flavoenzymes for biocatalysis.
| Autor: | Hall M; Department of Chemistry, University of Graz, Graz, Austria. Electronic address: melanie.hall@uni-graz.at. |
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| Jazyk: | angličtina |
| Zdroj: | The Enzymes [Enzymes] 2020; Vol. 47, pp. 37-62. Date of Electronic Publication: 2020 Jul 18. |
| DOI: | 10.1016/bs.enz.2020.05.001 |
| Abstrakt: | Flavoenzymes are broadly employed as biocatalysts for a large variety of reactions, owing to the chemical versatility of the flavin cofactor. Oxidases set aside, many flavoenzymes require a source of electrons in form of the biological reductant nicotinamide NAD(P)H in order to initiate catalysis via the reduced flavin. Chemists can take advantage of the reactivity of reduced flavins with oxygen to carry out monooxygenation reactions, while the reduced flavin can also be used for formal hydrogenation reactions. The main advantage of these reactions compared to chemical approaches is the frequent regio-, chemo- and stereo-selectivity of the biocatalysts, which allows the synthesis of chiral molecules in optically active form. This chapter provides an overview of the variety of biocatalytic processes that have been developed with flavoenzymes, with a particular focus on nicotinamide-dependent enzymes. The diversity of molecules obtained is highlighted and in several cases, strategies that allow control of the stereochemical outcome of the reactions are reviewed. (© 2020 Elsevier Inc. All rights reserved.) |
| Databáze: | MEDLINE |
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