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

Rosario Medici, Hanna Stammes, Linda G. Otten, Ulf Hanefeld, Stender Kwakernaak

Research output: Contribution to journalArticleScientificpeer-review

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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.
Original languageEnglish
Pages (from-to)1831-1837
JournalCatalysis Science & Technology
Issue number9
Publication statusPublished - 7 May 2017

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