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• W1485674955 abstract "Methyl parathion hydrolase (MPH) from Pseudomonas sp. HS-D36 has been reported to be highly specific in the hydrolysis of methyl parathion (MP) but little active towards paraoxon. In this paper, we employed error-prone polymerase chain reaction (epPCR) to obtain directed evolved MPH with enhanced ability to degrade paraoxon. After one round of epPCR, several MPH variants with improved activities towards paraoxon had been selected from the mutant library. The best mutant of rMPH-m.3 showed nearly 15-fold increased activity towards paraoxon compared with the wild type. Molecular modeling analysis suggested that the four amino acid substitutions (S180R/V268I/G308S/R318C) in the mutant MPH were not directly located in the active site but resulted in a dramatically increased binding for paraoxon. These results provided important information on directed evolution of MPH to enlarge its substrate spectrum." @default.
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• W1485674955 date "2011-05-01" @default.
• W1485674955 modified "2023-09-22" @default.
• W1485674955 title "Notice of Retraction: Altering the Substrate Specificity of Methyl Parathion Hydrolase for Enhanced Hydrolysis of Paraoxon by Error-Prone PCR" @default.
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• W1485674955 doi "https://doi.org/10.1109/icbbe.2011.5780042" @default.
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