Bulletin of the Chemical Society of Japan p. 2509 - 2513 (1997)
Update date:2022-08-03
Topics:
Basak, Amit
Bhattacharya, Gautam
Palit, Sunanda K.
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.
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