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

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

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

19 Citations (Scopus)

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.

Original language	English
Pages (from-to)	5440-5442
Number of pages	3
Journal	Chemical Communications
Volume	46
Issue number	30
DOIs	https://doi.org/10.1039/c001561j
Publication status	Published - Aug 14 2010

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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title = "Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates",

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.",

author = "Tadashi Ema and Shusuke Kamata and Masahiro Takeda and Yasuko Nakano and Takashi Sakai",

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AU - Nakano, Yasuko

AU - Sakai, Takashi

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AB - 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.

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