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Mutation Report for: F295L/F297V_human-ACHE

Name Class
Torpedo_number (3)
Mode_of_mutationSite directed mutagenesis
ModificationAcyl specificity
SummaryAcyl specificity;Acyl pocket, Increases hydrolysis of BTC;Ordentlich_1993_J.Biol.Chem_268_17083;Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097;Ashani_1994_Mol.Pharmacol_45_555
OP-specificity;increases reactivity towards DFP DEFP and paraoxon;Ordentlich_1996_J.Biol.Chem_271_11953'
OP-specificity;decrease in stereoselectivity;Ordentlich_2004_Biochemistry_43_11255
Acyl specificity;replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE;Kaplan_2001_Biochemistry_40_7433
Paper (6)
Kinetic_parameter (6)
Commentp.F295L/F297V Phe295Leu/Phe297Val (p.F326L/F328V Phe326Leu/Phe328Valin primary sequence with 31 amino-acids signal peptide) Acyl pocket, Increases hydrolysis of BTC OP-specificity: increases reactivity towards DFP DEFP and paraoxon;replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE

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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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