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Mutation Report for: Y337A_human-ACHE

Name Class
Y337A_human-ACHEGene_locushuman-ACHE
Torpedo_number330
AA_ChangeY337A
Mode_of_mutationSite directed mutagenesis
ModificationSignal transduction
Substrate inhibition
Oxime interaction
Acyl specificity
Summary (5)
Paper (10)
Kinetic_parameterEdrophonium_Y337A_human-ACHE
Paranitrophenylacetate_Y337A_human-ACHE
S-N-Propylthioacetate_Y337A_human-ACHE
3,3-dimethylbutylthioacetate_Y337A_human-ACHE
Acetylthiocholine_Y337A_human-ACHE
Hexamethonium_Y337A_human-ACHE
BW284C51_Y337A_human-ACHE
Propidium_Y337A_human-ACHE
Decamethonium_Y337A_human-ACHE
Tacrine_Y337A_human-ACHE
HuperzineA_Y337A_human-ACHE
Butyrylthiocholine_Y337A_human-ACHE
Commentp.Y337A Tyr337Ala (p.Y368A Tyr368Ala in primary sequence with 31 amino-acids signal peptide);Decrease in catalytic and apparent bimolecular constant Substrate inhibition;absence of substrate inhibition; Acyl specificity;replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE; Oxime interaction; reactivation of tabun-inhibited human AChE. Unable to facilitate HI-6-mediated reactivation of tabun-hAChE; The phosphoramidated-hAChE choline-binding site mutant Y337A showed three-times enhanced reactivation capacity with non-triazole imidazole containing aldoximes than with 2PAM

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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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