Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates

Tadashi Ema; Shusuke Kamata; Masahiro Takeda; Yasuko Nakano; Takashi Sakai

doi:10.1039/C001561J

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Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates†‡

Tadashi Ema,*^a Shusuke Kamata,^a Masahiro Takeda,^a Yasuko Nakano^a and Takashi Sakai*^a

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* Corresponding authors

^a Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University, Tsushima, Okayama 700-8530, Japan
E-mail: ema@cc.okayama-u.ac.jp
Fax: +81-86-251-8092
Tel: +81-86-251-8091

Abstract

Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the E value for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F/I290A double mutant) with an acceleration of the reaction rate.

This article is part of the themed collection: Enzymes and Proteins

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Supplementary files

Site-directed mutagenesis, synthesis of 1, lipase-catalyzed kinetic resolution of 1, determination of kinetic constants, design of mutants, and copies of NMR spectra PDF (1567K)

Article information

DOI: https://doi.org/10.1039/C001561J
Article type: Communication
Submitted: 26 Jan 2010
Accepted: 23 Mar 2010
First published: 09 Apr 2010

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Chem. Commun., 2010,46, 5440-5442

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Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates

T. Ema, S. Kamata, M. Takeda, Y. Nakano and T. Sakai, Chem. Commun., 2010, 46, 5440 DOI: 10.1039/C001561J

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Chemical Communications

Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates†‡

Abstract

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Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates

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