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Mutation Report for: F295A/F338A_human-ACHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|F295A/F338A
Torpedo number|331,288//331//288
Comment|p.F295A/F338A Phe295Ala/Phe338Ala (p.F326A/F369A Phe326Ala/Phe369Ala in primary sequence with 31 amino-acids signal peptide) Acyl pocket 680-fold decreased catalytic activity, orientation of His 447
Kinetic parameters|none

    Title: Lessons from functional analysis of AChE covalent and noncovalent inhibitors for design of AD therapeutic agents
    Barak D, Ordentlich A, Kaplan D, Kronman C, Velan B, Shafferman A
    Ref: Chemico-Biological Interactions, 157-158:219, 2005 : PubMed


    Title: Functional requirements for the optimal catalytic configuration of the AChE active center
    Shafferman A, Barak D, Kaplan D, Ordentlich A, Kronman C, Velan B
    Ref: Chemico-Biological Interactions, 157-158:123, 2005 : PubMed


    Title: The aromatic trapping of the catalytic histidine is essential for efficient catalysis in acetylcholinesterase
    Barak D, Kaplan D, Ordentlich A, Ariel N, Velan B, Shafferman A
    Ref: Biochemistry, 41:8245, 2002 : 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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