Novel Regioselective Ester Hydrolysis by Pig-Liver Esterase

Article abstract of DOI:10.1246/bcsj.70.2509

Pig-liver esterase, which catalyzed the hydrolysis of substrates containing both saturated and αβ-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.