Enantioselective acylation of alcohols catalyzed by lipase QL from Alcaligenes sp. A predictive active site model for lipase QL to identify the faster reacting enantiomer of an alcohol in this acylation

Koichiro Naemura*, Masaki Murata, Rie Tanaka, Masashi Yano, Keiji Hirose, Tobe Yoshito

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Lipase QL-catalyzed acylation of secondary alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether gave preferentially the corresponding acetate with an R configuration. On the basis of the results, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a secondary alcohol reacts faster in this reaction.

Original languageEnglish
Pages (from-to)1581-1584
Number of pages4
JournalTetrahedron Asymmetry
Volume7
Issue number6
DOIs
StatePublished - 1 Jan 1996

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