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Mutation Report for: D74E_human-ACHE

D74E_human-ACHE
Gene_Locus|human-ACHE
Mode of mutation|Site directed mutagenesis
Amino Acid change|D74E
Torpedo number|72
Summary|
Comment|p.D74E Asp74Glu (p.D105E Asp105Glu in primary sequence with 31 amino-acids signal peptide) Peripheral Anionic Site/signal transduction/allosteric modulation. Affects conformation of active site and PAS; no effect in VX stereoselectivity; Unable to facilitate HI-6-mediated reactivation of tabun-hAChE
Kinetic parameters|Acetylthiocholine_D74E_human-ACHE,
BW284C51_D74E_human-ACHE,
Decamethonium_D74E_human-ACHE,
Edrophonium_D74E_human-ACHE,
Propidium_D74E_human-ACHE


References:
    Title: Reactivation of tabun-hAChE investigated by structurally analogous oximes and mutagenesis
    Artursson E, Akfur C, Hornberg A, Worek F, Ekstrom F
    Ref: Toxicology, 265:108, 2009 : PubMed

            

    Title: The role of AChE active site gorge in determining stereoselectivity of charged and noncharged VX enantiomers
    Ordentlich A, Barak D, Sod-Moriah G, Kaplan D, Mizrahi D, Segall Y, Kronman C, Karton Y, Lazar A and Shafferman A <2 more author(s)>
    Ref: Chemico-Biological Interactions, 157-158:191, 2005 : PubMed

            

    Title: Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center
    Shafferman A, Velan B, Ordentlich A, Kronman C, Grosfeld H, Leitner M, Flashner Y, Cohen S, Barak D, Ariel N
    Ref: EMBO Journal, 11:3561, 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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