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Mutation Report for: G117C_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|G117C
Torpedo number|119
Comment|p.G117C Gly117Cys (p.G145C Gly145Cys in primary sequence with 28 amino-acids signal peptide) Changing to acidic residues G117E and G117D were significantly reactive, but less nucleophilic residues such as G117S, G117C, and G117Y were not.
Kinetic parameters|none

    Title: Mutants of human butyrylcholinesterase with organophosphate hydrolase activity; evidence that His117 is a general base catalyst for hydrolysis of echothiophate
    Schopfer LM, Boeck AT, Broomfield CA, Lockridge O
    Ref: Journal of Medicinal Chemistryical Biology Radiol Def, 2:1, 2004 : PubMed


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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