Issue 9, 2017

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

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

Supplementary files

Article information

Article type
Paper
Submitted
25 Jan 2017
Accepted
22 Feb 2017
First published
22 Feb 2017
This article is Open Access
Creative Commons BY license

Catal. Sci. Technol., 2017,7, 1831-1837

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, 7, 1831 DOI: 10.1039/C7CY00169J

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