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Highly Efficient Biocatalytic Reduction of Keto Esters
G. A. Applegate, R. W. Cheloha, D. L. Nelson, D. B. Berkowitz*
University of Nebraska, Lincoln, USA
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.