Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation

FEBS Journal

Volumn 277, Issue 23, 2010, Pages 4901-4908

  Tian, Jian ^a   Wang, Ping ^a   Gao, Shan ^a   Chu, Xiaoyu ^a   Wu, Ningfeng ^a   Fan, Yunliu ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Methyl parathion hydrolase; Molecular dynamics; Proline theory; Thermostability

Indexed keywords

BACTERIAL ENZYME; GLYCINE; METHYL PARATHION HYDROLASE; PROLINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL STRAIN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME STABILITY; GENETIC ENGINEERING; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; OCHROBACTRUM; PREDICTION; PRIORITY JOURNAL; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; DNA PRIMERS; ENZYME STABILITY; KINETICS; METHYL PARATHION; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; OCHROBACTRUM; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; STATIC ELECTRICITY; STRUCTURAL HOMOLOGY, PROTEIN; TEMPERATURE; THERMODYNAMICS;

OCHROBACTRUM SP.;

EID: 78449306754     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07895.x     Document Type: Article

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