Synfacts 2011(3): 0333-0333  
DOI: 10.1055/s-0030-1259448
Organo- and Biocatalysis
© Georg Thieme Verlag Stuttgart ˙ New York

Highly Efficient Biocatalytic Reduction of Keto Esters

Contributor(s): Benjamin List, Lars Ratjen
G. A. Applegate, R. W. Cheloha, D. L. Nelson, D. B. Berkowitz*
University of Nebraska, Lincoln, USA
Further Information

Publication History

Publication Date:
16 February 2011 (online)


The biocatalytic reduction of carbonyl compounds with an alcohol dehydrogenase (ADH) by means of a dynamic reductive kinetic resolution is reported. The utilized enzyme, iso­lated from Clostridium acetobutylicum and expressed in pure form from E. coli, performed ­exceptionally well in the reduction of keto esters. Some of the products delivered represent intermediates of pharmaceutical compounds, such as taxoids. Since the enzyme is NADPH-dependent, the regeneration of the co-factor is an important feature. In this case it is regenerated by a glu­tamate dehydrogenase (GDH), which uses d-glucose as the terminal reductant, forming gluconic acid under the reported reaction conditions.