Isoenzymes of Pig‐Liver Esterase Reveal Striking Differences in Enantioselectivities

An esterase toolbox: A set of isoenzymes of pig liver esterases (PLE) is identified, cloned, and overexpressed in E. coli. They show striking differences in enantioselectivity and enantiopreference in the kinetic resolution of acetates of secondary alcohols as well as the desymmetrization of cis-3,5-diacetoxycyclopent-1-ene to 1 a and 1 b (see picture: enantiopreference of the new isoenzymes and a commercial PLE isoenzyme mixture). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z703256_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.