Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface

Applied Biochemistry and Biotechnology

Volumn 165, Issue 3-4, 2011, Pages 989-997

  Su, Yidan ^a,b   Tian, Jian ^a   Wang, Ping ^a   Chu, Xiaoyu ^a   Liu, Guoan ^b   Wu, Ningfeng ^a   Fan, Yunliu ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

^b NORTHWEST NORMAL UNIVERSITY   (China)

Author keywords

Ionic bond; Methyl parathion hydrolase; Site directed mutagenesis; Thermostability

Indexed keywords

ELECTROSTATIC ENERGIES; IONIC BONDS; METHYL PARATHION HYDROLASE; OCHROBACTRUM SP; ORGANOPHOSPHORUS HYDROLASE; PROTEIN SURFACE; SEQUENCE ALIGNMENTS; SITE-DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACIDS; HYDROLASES; MUTAGENESIS; THERMODYNAMIC STABILITY;

PROTEINS;

ARYLDIALKYLPHOSPHATASE; HYDROLASE; PARATHION METHYL; PROLINE;

ARTICLE; CHEMICAL BOND; CONTROLLED STUDY; ENZYME STABILITY; GENE MUTATION; NONHUMAN; OCHROBACTRUM; PROTEIN STABILITY; PSEUDOMONAS PSEUDOALCALIGENES; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY; STRUCTURE ANALYSIS; TEMPERATURE; THERMOSTABILITY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CLONING, MOLECULAR; ENZYME STABILITY; ESCHERICHIA COLI; HYDROLASES; INSECTICIDES; KINETICS; METHYL PARATHION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OCHROBACTRUM; PLASMIDS; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PSEUDOMONAS PSEUDOALCALIGENES; RECOMBINANT PROTEINS; STATIC ELECTRICITY; TEMPERATURE; TRANSFORMATION, BACTERIAL;

OCHROBACTRUM SP.; PSEUDOMONAS PSEUDOALCALIGENES;

EID: 81355149809     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-011-9314-z     Document Type: Article

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