Print Email Facebook Twitter Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase Title Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase Author Medici, R. (TU Delft BT/Biocatalysis) Stammes, J.K. (TU Delft Science Education and Communication) Otten, L.G. (TU Delft BT/Biocatalysis) Hanefeld, U. (TU Delft BT/Biocatalysis) Kwakernaak, Stender (Student TU Delft) Date 2017-05-07 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. To reference this document use: http://resolver.tudelft.nl/uuid:2ceb2f31-d532-4b0d-8259-bb4b96e79cd2 DOI https://doi.org/10.1039/c7cy00169j ISSN 2044-4753 Source Catalysis Science & Technology, 7 (9), 1831-1837 Part of collection Institutional Repository Document type journal article Rights © 2017 R. Medici, J.K. Stammes, L.G. Otten, U. Hanefeld, Stender Kwakernaak Files PDF c7cy00169j.pdf 1.11 MB Close viewer /islandora/object/uuid:2ceb2f31-d532-4b0d-8259-bb4b96e79cd2/datastream/OBJ/view