Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp. A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

Lipase QL (from Alcaligenes sp.)-catalyzed acylation of alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether converted preferentially primary alcohols with an S configuration and secondary alcohols with an R configuration into the corresponding homochiral acetates. On the basis of observed enantiomer selectivities, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation. Copyright (C) 1996 Published by Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)3285-3294
Number of pages10
JournalTetrahedron Asymmetry
Volume7
Issue number11
DOIs
StatePublished - 8 Nov 1996

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