Abstract
The asymmetric reduction of benzylic and heteroaryl ketones to the corresponding (R)-alcohols using I86A Ther-moanaerobacter ethanolicus alcohol dehydrogenase (I86ATeSADH) is described. This single amino acid mutation not only makes the active site of I86A TeSADH able to accommodate more sterically demanding substituents than those accommodated by wild-type TeSADH, but it also reverses the substrate stereospecificity of TeSADH.
| Original language | English |
|---|---|
| Pages (from-to) | 89-93 |
| Number of pages | 5 |
| Journal | ChemCatChem |
| Volume | 1 |
| Issue number | 1 |
| DOIs | |
| State | Published - 24 Aug 2009 |
| Externally published | Yes |
Keywords
- Biocatalysis
- Biotransformations
- Enantioselectivity
- Enzymes
- Protein engineering
ASJC Scopus subject areas
- Catalysis
- Physical and Theoretical Chemistry
- Organic Chemistry
- Inorganic Chemistry
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