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

Koichiro Naemura*, Ritsuko Fukuda, Masaki Murata, Masayoshi Konishi, Keiji Hirose, Yoshito Tobe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

Primary alcohols having a hydroxymethyl group at an S stereogemic 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.

Original languageEnglish
Pages (from-to)2385-2394
Number of pages10
JournalTetrahedron: Asymmetry
Volume6
Issue number9
DOIs
StatePublished - 1 Jan 1995

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