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

Authors :: Applegate GA
Cheloha RW
Nelson DL
Berkowitz DB
Source :: Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2011 Feb 28; Vol. 47 (8), pp. 2420-2. Date of Electronic Publication: 2010 Dec 20.
Publication Year :: 2011
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).

Subjects :: Alcohol Oxidoreductases chemistry
Alcohol Oxidoreductases genetics
Aldehydes chemistry
Biocatalysis
Esters
Ketones chemistry
Kinetics
Oxidation-Reduction
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Stereoisomerism
Structure-Activity Relationship
Alcohol Oxidoreductases metabolism
Clostridium acetobutylicum enzymology

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