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Issue 15, 2011
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Highly stereoselective reduction of prochiral ketones by a bacterial reductase coupled with cofactor regeneration

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Abstract

A carbonyl reductase gene (yueD) from Bacillus sp. ECU0013 was heterologously overexpressed in Escherichia coli, and the encoded protein (BYueD) was purified to homogeneity and characterized. The NADPH-dependent reductase showed a broad substrate spectrum towards different aromatic ketones, and α- and β-ketoesters. Although the enantioselectivity was high to moderate for the reduction of α-ketoesters, all the tested β-ketoesters and aromatic ketones were reduced to the corresponding chiral alcohols in enantiomerically pure forms. Furthermore, the practical applicability of this enzyme was evaluated for the reduction of ethyl 4-chloro-3-oxobutanoate (1a). Using Escherichia colicells coexpressing BYueD and glucose dehydrogenase, 215 g L−1 (1.3 M) of 1a was stoichiometrically converted to ethyl (R)-4-chloro-3-hydroxybutanoate ((R)-1b) in an aqueous-toluene biphasic system by using a substrate fed-batch strategy, resulting in an overall hydroxyl product yield of 91.7% with enantiomeric purity of 99.6% ee.

Graphical abstract: Highly stereoselective reduction of prochiral ketones by a bacterial reductase coupled with cofactor regeneration

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Supplementary files

Article information


Submitted
22 Feb 2011
Accepted
28 Apr 2011
First published
28 Apr 2011

Org. Biomol. Chem., 2011,9, 5463-5468
Article type
Paper

Highly stereoselective reduction of prochiral ketones by a bacterial reductase coupled with cofactor regeneration

Y. Ni, C. Li, L. Wang, J. Zhang and J. Xu, Org. Biomol. Chem., 2011, 9, 5463
DOI: 10.1039/C1OB05285C

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