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 | |
| Publication status | Published - 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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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