Dynamic enzymatic resolution of thioesters

PJ Um, DG Drueckhammer

Index: Um, Pil-Je; Drueckhammer, Dale G. Journal of the American Chemical Society, 1998 , vol. 120, # 23 p. 5605 - 5610

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Citation Number: 112

Abstract

A detailed investigation of several issues related to the enzymatic resolution of thioesters under conditions of continuous racemization of substrate was conducted. The kinetic acidity of the α-protons of a series of α-substituted propionate thioesters was studied. It was found that the rate of α-proton exchange could be enhanced as much as 20-fold by variation of the thiol moiety, increasing the range of compounds to which enzymatic dynamic resolution ...