Jump to main content
Jump to site search

Issue 30, 2010
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 26 Jan 2010, accepted on 23 Mar 2010 and first published on 09 Apr 2010


Article type: Communication
DOI: 10.1039/C001561J
Chem. Commun., 2010,46, 5440-5442

  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements