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Mutation Report for: N322E/E325G_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|N322E/E325G
Torpedo number|324//327//324,327
Comment|p.N322E/E325G Asn322Glu/Glu325Gly The original glutamic acid residue of the catlytic triad at position 322 was converted to glycine and a new glutamic acid residue was introduced at position 322 in place of asparagine.
Kinetic parameters|none

    Title: Computer-designed active human butyrylcholinesterase double mutant with a new catalytic triad
    Grigorenko BL, Novichkova DA, Lushchekina SV, Zueva IV, Schopfer LM, Nemukhin AV, Varfolomeev SD, Lockridge O, Masson P
    Ref: Chemico-Biological Interactions, 306:138, 2019 : 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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