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Lipase YS-catalysed acylation of alcohols: a predictive active site model for lipase YS to identify which enantiomer of a primary or a secondary alcohol reacts faster in this acylation
44
Citations
13
References
1994
Year
EngineeringMolecular BiologySecondary Alcohol ReactsOrganic ChemistryEnzymatic ModificationBiosynthesisLipase Ys-catalysed AcylationAlcohol DehydrogenasesBiochemistryBiocatalysisPrimary AlcoholsAsymmetric CatalysisLipase YsEnantioselective SynthesisBiomolecular EngineeringHydroxymethyl GroupNatural SciencesEnzyme CatalysisEnzyme Specificity
Primary alcohols having a hydroxymethyl group at an S chiral centre and secondary alcohols with an R configuration are preferentially acylated to give the corresponding acetates by lipase YS-catalysed acylation in diisopropyl ether; a predictive cubic-spaced active site model for lipase YS is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation.
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