Enzyme-catalyzed asymmetric acylation and hydrolysis of cis-2,5-disubstituted tetrahydrofuran derivatives: Contribution to development of models for reactions catalyzed by porcine liver esterase and porcine pancreatic lipase

Koichiro Naemura*, Ritsuko Fukuda, Nobuo Takahashi, Masayoshi Konishi, Yoshiki Hirose, Tobe Yoshito

*Corresponding author for this work

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Pig liver esterase, lipase from porcine pancreas, lipase from Pseudomonas sp. (lipase YS), and lipase from Candida cylindracea catalyzed hydrolyses of the cis-diacetate 1 and the trans-diacetate (±)-4 to give the cis-monoacetate 3 and the trans-monoacetate 6 in optically active forms, respectively. Lipase YS-catalyzed acylations of the cis-diol 2 and the trans-diol (±)-5 with an acylating agent in cyclohexane yielded (-)-3 and (-)-6, respectively. The group adjacent to the R stereogenic center preferentially reacted in lipase YS-catalyzed hydrolyses of 1 and (±)-4 and acylations of 2 and (±)-5, and the enantioselectivities are rationalized by our rule recently proposed for lipase YS.

Original languageEnglish
Pages (from-to)911-918
Number of pages8
JournalTetrahedron: Asymmetry
Volume4
Issue number5
DOIs
StatePublished - 1 Jan 1993

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