Assessing the stereoselectivity of Serratia marcescens CECT 977 2,3-butanediol dehydrogenase
Rosario Médici (TU Delft - BT/Biocatalysis)
Hanna Stammes (TU Delft - Science Education and Communication)
LG Otten (TU Delft - BT/Biocatalysis)
U. Hanefeld (TU Delft - BT/Biocatalysis)
Stender Kwakernaak (Student TU Delft)
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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.
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