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

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

*Corresponding author for this work

Research output: Contribution to journalArticle

56 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1253-1256
Number of pages4
JournalJournal of the Chemical Society, Perkin Transactions 1
Issue number10
DOIs
StatePublished - 1 Dec 1994

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