A 3-DIMENSIONAL PREDICTIVE ACTIVE-SITE MODEL FOR LIPASE FROM PSEUDOMONAS-CEPACIA

A three-dimensional active site model of lipase from Pseudomonas cepac ia-one of the most popular lipases in organic synthesis-was developed on the basis of the kinetic revolution of 3-(aryloxy)propan-2-ols. Siz e and shape of both hydrophobic binding pockets of the active site of this lipase were determined by substrate mapping in combination with m olecular modeling for substrates and nonsubstrates. This model explain s and predicts whether a compound is accepted as a substrate or not an d allows to assess the enantiomer selectivity of the lipase-catalyzed reaction.