Pig liver esterase catalyzed hydrolysis: Substrate specificity and stereoselectivity

Abstract

In order to gain a more detailed insight into the relationship between substrate structure and the stereoselectivity of the enzyme pig liver esterase (E.C. 3.1.1.1.) a large series of mainly meso and prochiral diesters with an open chain or a cyclic structure has been studied and evaluated. Results obtained with 3-substituted cyclopropane-1,2-dicarboxylates are incompatible with the three-dimensional (cubic) active-site model of PLE proposed by J.B. Jones et al. Kinetic resolution of meso- and racemic diesters as well as of racemic monoesters has been observed. Their synthetic potential as versatile enantiomerically pure synthons for the construction of complex natural products is demonstrated by the synthesis of the pheromone endo-1,3 dimethyl-2,9-dioxabicyclo[3.3.1]nonane, C(19)-to-C(27)-Segment of rifamycin S and the C(1)- to C(7)-segment of 14-membered macrolide antibiotics. © 1992, IUPAC