Novel regioselective ester hydrolysis by pig-liver esterase

Abstract

Pig-liver esterase, which catalyzed the hydrolysis of substrates containing both saturated and α,β-unsaturated/cyclopropanecarboxylic esters (methyl and ethyl), was studied. An exclusive hydrolysis of the saturated esters was observed. Kinetic experiments revealed that the presence of deactivated carbonyl in the unsaturated/cyclopropanecarboxylic esters and their weaker bindings are both responsible for the observed specificity. The relative binding abilities of the substrates have been explained in light of Jones active-site model. The regioselectivity has been exploited in the synthesis of intermediates for the thromboxane synthetase inhibitor.