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Mutation Report for: E84Q_human-ACHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|E84Q
Torpedo number|82
Comment|p.E84Q Glu84Gln (p.E115Q Glu115Gln in primary sequence with 31 amino-acids signal peptide) Omega loop;No effect - Electrostatic carboxyl/attraction studies Little effect on hydrolysis or inhibition
Kinetic parameters|3,3-dimethylbutylthioacetate_E84Q_human-ACHE,

    Title: Structural modifications of the omega loop in human acetylcholinesterase
    Velan B, Barak D, Ariel N, Leitner M, Bino T, Ordentlich A, Shafferman A
    Ref: FEBS Letters, 395:22, 1996 : PubMed


    Title: The back door hypothesis for product clearance in acetylcholinesterase challenged by site-directed mutagenesis
    Kronman C, Ordentlich A, Barak D, Velan B, Shafferman A
    Ref: Journal of Biological Chemistry, 269:27819, 1994 : PubMed


    Title: Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase
    Shafferman A, Ordentlich A, Barak D, Kronman C, Ber R, Bino T, Ariel N, Osman R, Velan B
    Ref: EMBO Journal, 13:3448, 1994 : PubMed


    Title: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding
    Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N and Velan B <4 more author(s)>
    Ref: Journal of Biological Chemistry, 267:17640, 1992 : PubMed


    Title: Acetylcholinesterase Catalysis - Protein Engineering Studies
    Shafferman A, Velan B
    Ref: In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases, (Shafferman, A. and Velan, B., Eds) Plenum Press, New York:165, 1992 : PubMed


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