4.7 Article

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

Journal

CHEMICAL COMMUNICATIONS
Volume 47, Issue 8, Pages 2420-2422

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c0cc04585c

Keywords

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Funding

  1. National Science Foundation [CHE-0911732, CHE-0091975, MRI-0079750]
  2. NCESR
  3. Am. Chem. Soc.
  4. NIH [SIG-1-510-RR-06307, RR016544]
  5. NATIONAL CENTER FOR RESEARCH RESOURCES [C06RR016544] Funding Source: NIH RePORTER
  6. 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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