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Mutation Report for: K544H/R549H/K558H/K568H/K569H_human-BCHE

K544H/R549H/K558H/K568H/K569H_human-BCHE
Gene_Locus|human-BCHE
Mode of mutation|Site directed mutagenesis
Amino Acid change|K544H/R549H/K558H/K568H/K569H
Torpedo number|546,551,560,569,570//546//551//560//569//570
Summary|
Comment|p.K544H/R549H/K558H/K568H/K569H Lys544His/Lys549His/Lys558His/Lys568His/Lys569His (p.K572H/R577H/K586H/K596H/K569H Lys572His/Lys577His/Lys586His/Lys596His/Lys597His in primary sequence with 28 amino-acids signal peptide) Elimination of common targets of proteases Does not increase tetramer formation
Kinetic parameters|none


References:
    Title: Tetramerization domain of human butyrylcholinesterase is at the C- terminus
    Blong RM, Bedows E, Lockridge O
    Ref: Biochemical Journal, 327:747, 1997 : PubMed

            




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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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