Kinetic resolution of 2-substituted esters catalyzed by a lipase ex. Pseudomonas fluorescens

Abstract

Enantioselective hydrolyses of a variety of 2-substituted racemic esters catalyzed by a bacterial lipase have been effected in high enantiomeric excess. These enzyme-catalyzed kinetic resolutions constitute an economical method of preparing enantiomerically pure 2-substituted esters and acids on a large scale. Several of the resolved enantiomers are important intermediates in the synthesis of bioactive compounds in the areas of prostanoids, angiotensin-converting enzyme inhibitors, and leukotriene antagonists