Abstract
Among the various hydrolases, Pig Liver Esterase (PLE) is possibly the most widely used enzyme, particularly for the preparation ~f chiral synthons *'2 and for chemo 3 and regioselective transfo .~6ations. Various active site models for PLE have been proposed' , the cubic space model of Jones et al. s having received most attention. We report the reactivities of methyl esters containing large hydrophobic substituents toward PLE catalysed hydrolysis, and discuss the results in the light of Jones' model.
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