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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)
PaperKaplan_2001_Biochemistry_40_7433
Kovarik_2019_Toxicol.Appl.Pharmacol_372_40
Shafferman_1992_EMBO.J_11_3561
Barak_1994_J.Biol.Chem_269_6296
Ordentlich_1995_J.Biol.Chem_270_2082
Cochran_2011_J.Biol.Chem_286_29718
Artursson_2009_Toxicology_265_108
Kovarik_2013_Chem.Biol.Interact_203_77
Macek Hrvat_2016_Chem.Biol.Interact_259_148
Ariel_1998_Biochem.J_335_95
Kinetic_parameter (12)
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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