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

Abstract

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.

DOI: 10.1007/s10529-012-0882-y

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@article{Huang2012ImprovingTA, title={Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic residues}, author={Lu Huang and Ping Wang and Jian Tian and Huachen Jiang and Ningfeng Wu and Peilong Yang and Bin Yao and Yunliu Fan}, journal={Biotechnology Letters}, year={2012}, volume={34}, pages={1115-1121} }