Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic residues

文献类型： 外文期刊

第一作者： Huang, Lu

作者： Huang, Lu;Yang, Peilong;Yao, Bin;Huang, Lu;Wang, Ping;Tian, Jian;Jiang, Huachen;Wu, Ningfeng;Fan, Yunliu

作者机构：

关键词： Acidic amino acid;Acidic stability;Methyl parathion hydrolase;Site-directed mutagenesis

期刊名称：BIOTECHNOLOGY LETTERS （ 影响因子：2.461； 五年影响因子：2.457 ）

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收录情况： SCI

摘要： The acidic stability of a methyl parathion hydrolase (Ochr-MPH) was improved by selectively changing basic amino acids to acidic ones. Mutation sites were selected based on the position-specific amino acid replacement probabilities (more than or equal to 0.2) and the entropy of each site (more than or equal to 0.8). Three mutants (K208E, K277D, and K208E/K277D) were more stable than the wild-type (WT). Their half-lives at pH 5.0 were 64, 68, 65 min, respectively, whereas that of WT was 39 min. The acidic stability of proteins may therefore be improved by changing selected basic amino acid residues to acidic ones.

分类号： Q7

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