Abstract
An NADP-dependent alcohol dehydrogenase from Clostridium acetobutylicum (CaADH) has been expressed and characterized. CaADH enantioselectively reduces aromatic α-, β- and γ-keto esters to the corresponding D-hydroxy esters and provides a building block for the Taxotère side chain (95% yield, 95% de, 99% ee) by dynamic reductive kinetic resolution (DYRKR).
Original language | English (US) |
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Pages (from-to) | 2420-2422 |
Number of pages | 3 |
Journal | Chemical Communications |
Volume | 47 |
Issue number | 8 |
DOIs | |
State | Published - Feb 7 2011 |
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- General Chemistry
- Ceramics and Composites
- Metals and Alloys
- Materials Chemistry
- Surfaces, Coatings and Films
- Catalysis