Journal
CHEMICAL COMMUNICATIONS
Volume 47, Issue 8, Pages 2420-2422Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0cc04585c
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Funding
- National Science Foundation [CHE-0911732, CHE-0091975, MRI-0079750]
- NCESR
- Am. Chem. Soc.
- NIH [SIG-1-510-RR-06307, RR016544]
- NATIONAL CENTER FOR RESEARCH RESOURCES [C06RR016544] Funding Source: NIH RePORTER
- Direct For Mathematical & Physical Scien [0911732] Funding Source: National Science Foundation
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An NADP-dependent alcohol dehydrogenase from Clostridium acetobutylicum (CaADH) has been expressed and characterized. CaADH enantioselectively reduces aromatic alpha-, beta- and gamma-keto esters to the corresponding D-hydroxy esters and provides a building block for the Taxotere side chain (95% yield, 95% de, 99% ee) by dynamic reductive kinetic resolution (DYRKR).
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