A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: Dynamic reductive kinetic resolution entry into the Taxotère side chain

Gregory A. Applegate, Ross W. Cheloha, David L. Nelson, David B Berkowitz

Research output: Contribution to journalArticle

32 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2420-2422
Number of pages3
JournalChemical Communications
Volume47
Issue number8
DOIs
StatePublished - Feb 28 2011

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Clostridium
Esters
Oxidoreductases
Kinetics
Alcohols
alcohol dehydrogenase (NAD(P)+)

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Cite this

A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis : Dynamic reductive kinetic resolution entry into the Taxotère side chain. / Applegate, Gregory A.; Cheloha, Ross W.; Nelson, David L.; Berkowitz, David B.

In: Chemical Communications, Vol. 47, No. 8, 28.02.2011, p. 2420-2422.

Research output: Contribution to journalArticle

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