Abstract
Conformational analysis of the proposed tetrahedral transition state of different model esters in the active sites of the lipases of Candida rugosa and Pseudomonas cepacia are used to analyze structural reasons for the unique enantiomeric preference of lipases towards the cleavage of esters of chiral primary and secondary alcohols. The results are compared with the existing rules for the preference of one specific enantiomer in the hydrolysis of esters of chiral alcohols. Interesting results on the dynamics behaviour of some enantiomers within the lipases are reported.
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