文献类型：期刊文献

英文题名：Access to optically active aryl halohydrins using a substrate-tolerant carbonyl reductase discovered from kluyveromyces thermotolerans

作者：Xu, Guo-Chao[1]; Yu, Hui-Lei[1]; Zhang, Xiao-Yan[1]; Xu, Jian-He[1]

机构：[1] Laboratory of Biocatalysis and Synthetic Biotechnology, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China

年份：2012

卷号：2

期号：12

起止页码：2566

外文期刊名：ACS Catalysis

收录：EI(收录号：20125115808143)

语种：英文

外文关键词：Data mining - Escherichia coli - Enzyme activity - Genes - Ketones

摘要：By genome data mining, a carbonyl reductase tool box was designed and developed for chiral alcohol synthesis. On the basis of systematic comparison of the specific activity and substrate tolerance toward α-chloroacetophenone among reductases in this tool box, KtCR, a highly substrate-/product-tolerant carbonyl reductase from Kluyveromyces thermotolerans, was identified. The reduction of a series of substituted aryl ketones was investigated using this newly mined biocatalyst. Almost all of the ketones tested were asymmetrically reduced into corresponding chiral alcohols in 99% ee. Substrates with substituents adjacent to the carbonyl group or those with substituents on the para position of the phenyl ring were easier to reduce. For α- choloacetophenone as a representative substrate, as much as 154 g/L (1.0 M) of the substrate was asymmetrically reduced within merely 12 h by lyophilized cells of Escherichia coli/pET28-KtCR, resulting in an isolated yield of 92%, an enantiopurity of >99% ee, and a total turnover number of 5000, which was five times higher than the highest record reported so far. These results indicate the great potential of KtCR in practical synthesis of valuable aryl halohydrins as versatile chiral synthons. ? 2012 American Chemical Society.