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Mutation Report for: E197Q_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|E197Q
Torpedo number|199
Comment|p.E197Q Glu197Gln (p.E225Q Glu225Gln in primary sequence with 28 amino-acids signal peptide) Slow aging dealkylation; increases half-life of aging by DFP 60 times; ;strongly reduced substrate activation
Kinetic parameters|none

    Title: Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase
    Masson P, Xie W, Froment MT, Lockridge O
    Ref: Biochimica & Biophysica Acta, 1544:166, 2001 : PubMed


    Title: Protein engineering of a human enzyme that hydrolyzes V and G nerve agents: design, construction and characterization
    Broomfield CA, Lockridge O, Millard CB
    Ref: Chemico-Biological Interactions, 119-120:413, 1999 : PubMed


    Title: Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase
    Millard CB, Lockridge O, Broomfield CA
    Ref: Biochemistry, 37:237, 1998 : PubMed


    Title: Aging of di-isopropyl-phosphorylated human butyrylcholinesterase
    Masson P, Fortier PL, Albaret C, Froment MT, Bartels CF, Lockridge O
    Ref: Biochemical Journal, 327 ( Pt 2):601, 1997 : 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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