Department of Chemistry & Nebraska Center for Energy Sciences Research, University of Nebraska, Lincoln, NE, USA.
Chem Commun (Camb). 2011 Feb 28;47(8):2420-2. doi: 10.1039/c0cc04585c. Epub 2010 Dec 20.
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).
已表达和表征了来自丙酮丁醇梭菌(CaADH)的一种依赖 NADP 的醇脱氢酶。CaADH 对映选择性地将芳香族 α-、β-和 γ-酮酯还原为相应的 D-羟基酯,并通过动态还原动力学拆分(DYRKR)为 Taxotère 侧链提供构建块(95%产率、95%de、99%ee)。