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Issue 8, 2011
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A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

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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).

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

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Publication details

The article was received on 25 Oct 2010, accepted on 25 Nov 2010 and first published on 20 Dec 2010


Article type: Communication
DOI: 10.1039/C0CC04585C
Citation: Chem. Commun., 2011,47, 2420-2422
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    A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain

    G. A. Applegate, R. W. Cheloha, D. L. Nelson and D. B. Berkowitz, Chem. Commun., 2011, 47, 2420
    DOI: 10.1039/C0CC04585C

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