Chemical modification of lipase for rational enhancement of enantioselectivity

Tadashi Ema; Hiroki Inoue

doi:10.1246/cl.150667

Chemical modification of lipase for rational enhancement of enantioselectivity

Tadashi Ema, Hiroki Inoue

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Chemical modifications of the I287C mutant of a Burkholderia cepacia lipase afforded various I287C-X conjugates, among which I287C-PAA bearing an N-phenylacetamide (PAA) moiety showed excellent enantioselectivity and catalytic activity for secondary alcohols. Site-directed chemical modifications are powerful tools to control enantioselective biocatalysis.

Original language	English
Pages (from-to)	1374-1376
Number of pages	3
Journal	Chemistry Letters
Volume	44
Issue number	10
DOIs	https://doi.org/10.1246/cl.150667
Publication status	Published - 2015

ASJC Scopus subject areas

Chemistry(all)

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abstract = "Chemical modifications of the I287C mutant of a Burkholderia cepacia lipase afforded various I287C-X conjugates, among which I287C-PAA bearing an N-phenylacetamide (PAA) moiety showed excellent enantioselectivity and catalytic activity for secondary alcohols. Site-directed chemical modifications are powerful tools to control enantioselective biocatalysis.",

author = "Tadashi Ema and Hiroki Inoue",

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AU - Inoue, Hiroki

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AB - Chemical modifications of the I287C mutant of a Burkholderia cepacia lipase afforded various I287C-X conjugates, among which I287C-PAA bearing an N-phenylacetamide (PAA) moiety showed excellent enantioselectivity and catalytic activity for secondary alcohols. Site-directed chemical modifications are powerful tools to control enantioselective biocatalysis.

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M3 - Article

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JO - Chemistry Letters

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Chemical modification of lipase for rational enhancement of enantioselectivity

Abstract

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