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Mutation Report for: W86E_human-ACHE

Name Class
W86E_human-ACHEGene_locushuman-ACHE
Torpedo_number84
AA_ChangeW86E
Mode_of_mutationSite directed mutagenesis
ModificationCholine binding site
Signal transduction
SummaryCholine binding site;cation-aromatic interaction, 660 fold decrease affinity for ACTh no effect on uncharged substrate;Ordentlich_1995_J.Biol.Chem_270_2082;Shafferman_1995_5th.ChE.Meeting.Madras__189
Signal transduction;Y133 maintains the correct orientation of W86;Ordentlich_1995_J.Biol.Chem_270_2082;Shafferman_1995_5th.ChE.Meeting.Madras__189
PaperShafferman_1992_EMBO.J_11_3561
Ordentlich_1995_J.Biol.Chem_270_2082
Shafferman_1995_5th.ChE.Meeting.Madras__189
Kinetic_parameterAcetylthiocholine_W86E_human-ACHE
3,3-dimethylbutylthioacetate_W86E_human-ACHE
Edrophonium_W86E_human-ACHE
Propidium_W86E_human-ACHE
Decamethonium_W86E_human-ACHE
Commentp.W86E Trp86Glu (p.W117E Trp117Glu in primary sequence with 31 amino-acids signal peptide) Choline binding site;cation-aromatic interaction, 660 fold decrease affinity for ACTh no effect on uncharged substrate; Y133 maintains the correct orientation of W86
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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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