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Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

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Abstract

α-Hydroxy ketones and vicinal diols constitute well-known building blocks in organic synthesis. Here we describe one enzyme that enables the enantioselective synthesis of both building blocks starting from diketones. The enzyme 2,3-butanediol dehydrogenase (BudC) from S. marcescens CECT 977 belongs to the NADH-dependent metal-independent short-chain dehydrogenases/reductases family (SDR) and catalyses the selective asymmetric reductions of prochiral α-diketones to the corresponding α-hydroxy ketones and diols. BudC is highly active towards structurally diverse diketones in combination with nicotinamide cofactor regeneration systems. Aliphatic diketones, cyclic diketones and alkyl phenyl diketones are well accepted, whereas their derivatives possessing two bulky groups are not converted. In the reverse reaction vicinal diols are preferred over other substrates with hydroxy/keto groups in non-vicinal positions.

Graphical abstract: Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

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Publication details

The article was received on 25 Jan 2017, accepted on 22 Feb 2017, published on 22 Feb 2017 and first published online on 22 Feb 2017


Article type: Paper
DOI: 10.1039/C7CY00169J
Citation: Catal. Sci. Technol., 2017, Advance Article
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    Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase

    R. Médici, H. Stammes, S. Kwakernaak, L. G. Otten and U. Hanefeld, Catal. Sci. Technol., 2017, Advance Article , DOI: 10.1039/C7CY00169J

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