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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
Chem. Commun., 2011,47, 2420-2422
DOI:
10.1039/C0CC04585C
Received
25 Oct 2010,
Accepted
25 Nov 2010
First published online
20 Dec 2010
An NADP-dependent alcohol dehydrogenase from Clostridium acetobutylicum (CaADH) has been expressed and characterized. CaADH enantioselectively reduces aromatic α-, β- and γ-ketoesters to the corresponding D-hydroxyesters and provides a building block for the Taxotère side chain (95% yield, 95% de, 99% ee) by dynamic reductive kinetic resolution (DYRKR).
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