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Mutation Report for: E202A_human-ACHE

Name Class
E202A_human-ACHEGene_locushuman-ACHE
Torpedo_number199
AA_ChangeE202A
Mode_of_mutationSite directed mutagenesis
ModificationAcylation,Phosphorylation
Substrate inhibition
Aging
H-bond network
Summary (5)
Paper (8)
Kinetic_parameter (7)
Commentp.E202A Glu202Ala (p.E233A Glu233Ala in primary sequence with 31 amino-acids signal peptide) Catalysis;Decrease in catalytic and bimolecular constant, identical effect on charge and uncharged substrate, affects acylation-deacylation steps and not the noncovalent complex formation; H-bond network; not inhibited at high substrate concentration; Acylation,Phosphorylation;low effect on inhibition by DFP and DEFP but high for Paraoxon; Aging:E202 contributes to the aging process by stabilizing the imidazolium His447

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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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