Chemical modification of lipase for rational enhancement of enantioselectivity

Tadashi Ema, Hiroki Inoue

Research output: Contribution to journalArticle

4 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 languageEnglish
Pages (from-to)1374-1376
Number of pages3
JournalChemistry Letters
Volume44
Issue number10
DOIs
Publication statusPublished - 2015

Fingerprint

Enantioselectivity
Chemical modification
Lipase
Bearings (structural)
Catalyst activity
Alcohols
acetanilide
Biocatalysis

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Chemical modification of lipase for rational enhancement of enantioselectivity. / Ema, Tadashi; Inoue, Hiroki.

In: Chemistry Letters, Vol. 44, No. 10, 2015, p. 1374-1376.

Research output: Contribution to journalArticle

@article{9e79d2a8f34b41189bd79a034dfda0e2,
title = "Chemical modification of lipase for rational enhancement of enantioselectivity",
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",
year = "2015",
doi = "10.1246/cl.150667",
language = "English",
volume = "44",
pages = "1374--1376",
journal = "Chemistry Letters",
issn = "0366-7022",
publisher = "Chemical Society of Japan",
number = "10",

}

TY - JOUR

T1 - Chemical modification of lipase for rational enhancement of enantioselectivity

AU - Ema, Tadashi

AU - Inoue, Hiroki

PY - 2015

Y1 - 2015

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84946923376&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84946923376&partnerID=8YFLogxK

U2 - 10.1246/cl.150667

DO - 10.1246/cl.150667

M3 - Article

AN - SCOPUS:84946923376

VL - 44

SP - 1374

EP - 1376

JO - Chemistry Letters

JF - Chemistry Letters

SN - 0366-7022

IS - 10

ER -