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

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

Fingerprint

ASJC Scopus subject areas

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

Cite this

Ema, T., Kamata, S., Takeda, M., Nakano, Y., & Sakai, T. (2010). Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates. Chemical Communications, 46(30), 5440-5442. https://doi.org/10.1039/c001561j

@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

VL - 46

SP - 5440

EP - 5442

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 30

ER -

Access to Document

10.1039/c001561j