期刊
CHEMBIOCHEM
卷 10, 期 13, 页码 2230-2235出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200900102
关键词
acid phosphatases; aldol reaction; cascade reactions; dihydroxyacetone phosphate; directed evolution; high-throughput screening
资金
- Dutch National Research School Combination Catalysis (NRSC-Catalysis).
To enhance the phosphorylating activity of the bacterial nonspecific acid phosphatase from Salmonella enterica ser. typhimurium LT2 towards dihydroxyacetone (DHA), a mutant library was generated from the native enzyme. Three different variants that showed enhanced activity were identified after one round of epPCR. The single mutant V78L was the most active and showed an increase in the maximal DHAP concentration to 25% higher than that of the wild-type enzyme at pH 6.0. This variant is 17 times more active than the wild-type acid phosphatase from Salmonella enterica ser. typhimurium LT2 in the acid phosphatase/aldolase cascade reaction at pH 6.0 and is also six times more active than the phosphatase from Shigella flexneri that we previously used.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据