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

Biotechnology Letters

Volumn 34, Issue 6, 2012, Pages 1115-1121

  Huang, Lu ^a   Wang, Ping ^a   Tian, Jian ^a   Jiang, Huachen ^a   Wu, Ningfeng ^a   Yang, Peilong ^a   Yao, Bin ^a   Fan, Yunliu ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Acidic amino acid; Acidic stability; Methyl parathion hydrolase; Site directed mutagenesis

Indexed keywords

ACIDIC AMINO ACIDS; ACIDIC RESIDUES; AMINO ACID RESIDUES; HALF LIVES; METHYL PARATHION HYDROLASE; MUTATION SITES; SITE DIRECTED MUTAGENESIS; WILD TYPES;

AMINO ACIDS; HYDROLASES;

STABILITY;

MUTANT PROTEIN; PARATHION METHYL; PHOSPHATASE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENZYME STABILITY; ENZYMOLOGY; METABOLISM; OCHROBACTRUM; PH; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; METHYL PARATHION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; OCHROBACTRUM; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION;

EID: 84862785138     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-012-0882-y     Document Type: Article

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