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

研究成果 › 査読

23 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	5440-5442
ページ数	3
ジャーナル	Chemical Communications
巻	46
号	30
DOI	https://doi.org/10.1039/c001561j
出版ステータス	Published - 8月 14 2010

ASJC Scopus subject areas

触媒
電子材料、光学材料、および磁性材料
セラミックおよび複合材料
化学 (全般)
表面、皮膜および薄膜
金属および合金
材料化学

文献へのアクセス

10.1039/c001561j

他のファイルとリンク

フィンガープリント

「Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル

@article{12073a788a3343b4930279128bc68080,

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",

year = "2010",

month = aug,

day = "14",

doi = "10.1039/c001561j",

language = "English",

volume = "46",

pages = "5440--5442",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "30",

}

TY - JOUR

T1 - Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates

AU - Ema, Tadashi

AU - Kamata, Shusuke

AU - Takeda, Masahiro

AU - Nakano, Yasuko

AU - Sakai, Takashi

PY - 2010/8/14

Y1 - 2010/8/14

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=77954770949&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77954770949&partnerID=8YFLogxK

U2 - 10.1039/c001561j

DO - 10.1039/c001561j

M3 - Article

C2 - 20383389

AN - SCOPUS:77954770949

SN - 1359-7345

VL - 46

SP - 5440

EP - 5442

JO - Chemical Communications

JF - Chemical Communications

IS - 30

ER -