Lipase-catalyzed enantioselective acylation of alcohols: A predictive active site model for lipase YS to identify which enantiomer of an alcohol reacts faster in this acylation

Article abstract of DOI:10.1016/0957-4166(95)00316-H

Primary alcohols having a hydroxymethyl group at an S sterogemic center and secondary alcohols with an R configuration are preferentially acylated to give the corresponding acetates by lipase YS (from Pseudomonas fluorescens)-catalyzed acylation using isopropenyl acetate as the acylating agent in diisopropyl ether. On the basis of enantiomer selectivities observed, a predictive active site model for lipase YS is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation.