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)


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
Issue number30
Publication statusPublished - Aug 14 2010


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