Efficient Reduction of Ethyl 2??Oxo??4??phenylbutyrate at 620 g⋅ L− 1 by a Bacterial Reductase with Broad Substrate Spectrum

…, J Zhang, ND Shen, UT Bornscheuer…

Index: Ni, Yan; Li, Chun-Xiu; Zhang, Jie; Shen, Nai-Dong; Bornscheuer, Uwe T.; Xu, Jian-He Advanced Synthesis and Catalysis, 2011 , vol. 353, # 8 p. 1213 - 1217

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Citation Number: 36

Abstract

Abstract A β-ketoacyl-ACP reductase (FabG) gene from Bacillus sp. ECU0013 was heterologously overexpressed in Escherichia coli and the encoded protein was purified to homogeneity. The recombinant reductase could reduce a broad spectrum of prochiral ketones including aromatic ketones and keto esters and showed the highest activity in the asymmetric reduction of ethyl 2-oxo-4-phenylbutyrate (OPBE). Using E. coli cells ...