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 journalArticle

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 languageEnglish
Pages (from-to)5440-5442
Number of pages3
JournalChemical Communications
Volume46
Issue number30
DOIs
Publication statusPublished - 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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