Abstract
A three-dimensional active site model of lipase from Pseudomonas cepaciaone of the most popular lipases in organic synthesiswas developed on the basis of the kinetic resolution of 3-(aryloxy)propan-2-ols. Size and shape of both hydrophobic binding pockets of the active site of this lipase were determined by substrate mapping in combination with molecular modeling for substrates and nonsubstrates. This model explains and predicts whether a compound is accepted as a substrate or not and allows to assess the enantiomer selectivity of the lipase-catalyzed reaction.
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