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Mutation Report for: W543A/F547A/W550A/Y553A/W557A/F561A/Y564A/C571A_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|W543A/F547A/W550A/Y553A/W557A/F561A/Y564A/C571A
Torpedo number|545,549,552,555,559,563,566,572//545//549//552//555//559//563//566//572
Comment|p.W543A/F547A/W550A/Y553A/W557A/F561A/Y564A/C571A Trp543Ala/Phe547Ala/Trp550Ala/Tyr553Ala/Trp557Ala/Phe561Ala/Tyr564Ala/Cys571Ala (p.W571A/F575A/W578A/Y581A/W585A/F589A/Y592A/C599A Trp571Ala/Phe575Ala/Trp578Ala/Tyr581Ala/Trp585Ala/Phe589Ala/Tyr592Ala/Cys599Ala in primary sequence with 28 amino-acids signal peptide) Subunit assembly;Elimination C-terminal aromatic residues and the interchain cystein,reduces tetrameric structure
Kinetic parameters|none

    Title: Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus
    Altamirano CV, Lockridge O
    Ref: Chemico-Biological Interactions, 119-120:53, 1999 : PubMed


    Title: Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers
    Altamirano CV, Lockridge O
    Ref: Biochemistry, 38:13414, 1999 : 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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