Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface
文献类型: 外文期刊
第一作者: Su, Yidan
作者: Su, Yidan;Tian, Jian;Wang, Ping;Chu, Xiaoyu;Wu, Ningfeng;Fan, Yunliu;Su, Yidan;Liu, Guoan
作者机构:
关键词: Ionic bond;Methyl parathion hydrolase;Site-directed mutagenesis;Thermostability
期刊名称:APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY ( 影响因子:2.926; 五年影响因子:2.685 )
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页码:
收录情况: SCI
摘要: The thermostability of the methyl parathion hydrolase (MPH-OCH) from Ochrobactrum sp. M231 was improved using site-directed mutagenesis. Two prolines (Pro76 and Pro78) located on the protein surface were selected for mutations after inspection of the sequence alignment of MPH-OCH and OPHC2, a thermostable organophosphorus hydrolase from Pseudomonas pseudoalcaligenes C2-1. The temperature of the double-point mutant (P76D/P78K) at which the mutant lost 50% of its activity (T50) was approximately 68 °C, which is higher than that of WT enzyme (64 °C), P76D (67 °C), and P78K (59 °C). Structural analysis of P76D/P78K indicated that the substituted residues (Asp76 and Lys78) could generate an ionic bond and increase the structural electrostatic energy, which could then increase the stability of the protein. These results also suggest that the thermal stability of proteins could be improved by adding the ionic bond on protein surface.
分类号: Q5
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