Issue 8, 2011
From the journal:

Chemical Communications

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

Gregory A. Applegate,a   Ross W. Cheloha,a   David L. Nelsona  and  David B. Berkowitz*a  

* Corresponding authors

a Department of Chemistry & Nebraska Center for Energy Sciences Research (NCESR), University of Nebraska, USA
E-mail: dbb@unlserve.unl.edu
Fax: 01 402 472 9402
Tel: 01 402 472 2738

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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Article information

DOI
https://doi.org/10.1039/C0CC04585C
Article type
Communication
Submitted
25 Oct 2010
Accepted
25 Nov 2010
First published
20 Dec 2010

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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