A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase

Biochemistry

Volumn 36, Issue 4, 1997, Pages 786-795

  Lockridge, Oksana ^a,d   Blong, Renee M ^a   Masson, Patrick ^b   Froment, Marie Thérèse ^b   Millard, Charles B ^c   Broomfield, Clarence A ^c  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b CENTRE DE RECHERCHES   (France)

^c U S ARMY   (United States)

^d UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 NITROPHENOL; ACID ANHYDRIDE; BENZOYLCHOLINE; BUTYRIC ACID DERIVATIVE; BUTYRYLTHIOCHOLINE; CHOLINESTERASE; ECOTHIOPATE; HYDROLASE; MUTANT PROTEIN; ORGANOPHOSPHORUS COMPOUND; PARAOXON;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHO CELL; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; HUMAN; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALS; ARYLDIALKYLPHOSPHATASE; BASE SEQUENCE; BUTYRYLCHOLINESTERASE; CHO CELLS; CRICETINAE; DNA; ECHOTHIOPHATE IODIDE; ESTERASES; HUMANS; INSECTICIDES; KINETICS; MIOTICS; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PARAOXON; POINT MUTATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS; FELIS CATUS;

EID: 0031054145     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961412g     Document Type: Article

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