Torpedo_number Report for: 199

drome-ACHE

Mutation	Type	Evaluation system	Effect	Reference
E275A	sdm	Insecticide sensitivity		Boublik_2002_Protein.Eng_15_43
E275Q	sdm	Insecticide sensitivity		Boublik_2002_Protein.Eng_15_43
E275G	sdm	Binding of Triton X-100 studies	no effect on Triton X-100 binding	Marcel_2000_J.Biol.Chem_275_11603

human-ACHE : (kinetic parameters)

Mutation	Kin.	Type	Evaluation system	Effect	Reference
E202Q/ F338A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202Q/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202Q/ F295L/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202Q/ F297I/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202A	kin	sdm	Catalysis	Decrease in catalytic and bimolecular constant, identical effect on charge and uncharged substrate, affects acylation-deacylation steps and not the noncovalent complex formation	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202A	kin	sdm	H-bond network	Decrease in catalytic and bimolecular constant, identical effect on charge and uncharged substrate, affects acylation-deacylation steps and not the noncovalent complex formation	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202A	kin	sdm	Substrate inhibition	E202 mutant not inhibited at high substrate concentration	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202A	kin	sdm	Acylation,Phosphorylation	low effect on inhibition by DFP and DEFP but high for Paraoxon	Ordentlich_1995_5th.ChE.Meeting.Madras__221, Ordentlich_1996_J.Biol.Chem_271_11953, Shafferman_1996_Biochem.J_318_833
E202A	kin	sdm	Aging	E202 contributes to the aging process by stabilizing the imidazolium His447	Shafferman_1996_Biochem.J_318_833
E202Q	kin	sdm	Catalysis	Decrease in catalytic and bimolecular constant, identical effect on charge and uncharged substrate, affects acylation-deacylation steps and not the noncovalent complex formation	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202Q	kin	sdm	Substrate inhibition	E202 mutant not inhibited at high substrate concentration	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202Q	kin	sdm	Acylation,Phosphorylation	low effect on inhibition by DFP and DEFP but high for Paraoxon	Ordentlich_1995_5th.ChE.Meeting.Madras__221, Ordentlich_1996_J.Biol.Chem_271_11953, Shafferman_1996_Biochem.J_318_833
E202Q	kin	sdm	Aging	E202 contributes to the aging process by stabilizing the imidazolium His447	Shafferman_1996_Biochem.J_318_833
E202Q	kin	sdm	Heat and pressure stability	strengthened heat or pressure stability	Clery-Barraud_2002_Eur.J.Biochem_269_4297
E202Q	kin	sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202D	kin	sdm	Catalysis	Decrease in catalytic and bimolecular constant, identical effect on charge and uncharged substrate, affects acylation-deacylation steps and not the noncovalent complex formation	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202D	kin	sdm	Substrate inhibition	E202 mutant not inhibited at high substrate concentration	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Shafferman_1995_5th.ChE.Meeting.Madras__189, Shafferman_1996_Biochem.J_318_833
E202D	kin	sdm	Acylation,Phosphorylation	low effect on inhibition by DFP and DEFP but high for Paraoxon	Ordentlich_1995_5th.ChE.Meeting.Madras__221, Ordentlich_1996_J.Biol.Chem_271_11953, Shafferman_1996_Biochem.J_318_833
E202D	kin	sdm	Aging	E202 contributes to the aging process by stabilizing the imidazolium His447	Shafferman_1996_Biochem.J_318_833

human-BCHE

Mutation	Type	Evaluation system	Effect	Reference
E197Q	sdm	Phosphotriesterase activity	Slow aging dealkylation	Millard_1998_Biochemistry_37_237
E197Q	sdm	Substrate activation	strongly reduced substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
E197Q	sdm	Aging	E197Q increases half-life of aging by DFP 60 times	Masson_1997_Biochem.J_327_601
E197C	sdm	OP-resistance		Zhang_2012_J.Pharmacol.Exp.Ther_343_673
E197Q/ F329S	sdm	Aging	E197Q/F329S increases half-life of aging by DFP 54 times	Masson_1997_Biochem.J_327_601
E197D	sdm	Aging	Resistance to penetration of water D70 and E197 function like check valves for water	Masson_1999_Chem.Biol.Interact_119-120_17
E197D	sdm	Substrate activation	moderatly reduced substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
E197D	sdm	Aging	E197D increases half-life of aging by DFP 5.8 times	Masson_1997_Biochem.J_327_601
G117H/ E197Q	sdm	Search for phosphotriesterase activity	Phosphotriesterase activity	Millard_1998_Biochemistry_37_237
E197G	sdm	Succinylthiocholine binding	Higner Km	Masson_1997_Biochemistry_36_2266
E197G	sdm	Substrate activation	substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
E197G	sdm	Aging	E197G increases half-life of aging by DFP 155 times	Masson_1997_Biochem.J_327_601

human-CES1

Mutation	Kin.	Type	Evaluation system	Effect	Reference
E220G		nat	Natural mutant	decreased activity on enalapril clopidogrel and sacubitril	Wang_2017_Drug.Metab.Dispos_45_1149

luccu-E3aest7

Mutation	Type	Evaluation system	Effect	Reference
E217M	sdm	OP-resistance	search for OP hydrolase and MCE activities	Heidari_2004_Insect.Biochem.Mol.Biol_34_353
E217M	sdm	Pyrethroids hydrolysis	search for Pyrethroids hydrolysis activities	Heidari_2005_Insect.Biochem.Mol.Biol_35_597
E217M	sdm	Pyrethroids hydrolysis	Hydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterases	Devonshire_2007_Insect.Biochem.Mol.Biol_37_891

mouse-ACHE

Mutation	Type	Evaluation system	Effect	Reference
E202Q	sdm	Electrostatic	influence TFK inhibition but not ionic strength dependance	Radic_1997_J.Biol.Chem_272_23265
E202Q	sdm	Aging	decreased the affinity of soman for AChE, slowed the reactivation of soman-inhibited AChE by HI-6, and decreased the aging of mutant AChE	Saxena_1997_Biochem.Pharmacol_54_269
D74N/ E202Q/ E450Q	sdm	Electrostatic	influence TFK inhibition but not ionic strength dependance	Radic_1997_J.Biol.Chem_272_23265
D74N/ E202Q	sdm	Electrostatic	influence TFK inhibition but not ionic strength dependance	Radic_1997_J.Biol.Chem_272_23265

torca-ACHE

Mutation	Type	Evaluation system	Effect	Reference
E199D	sdm	Acylation	lower activity reduction in kcat but not Km substrate inhibition eliminated	Gibney_1990_Proc.Natl.Acad.Sci.U.S.A_87_7546, Radic_1992_Biochemistry_31_9760
E199D	sdm	Phosphorylation	Decreased affinity for reversible inhibitors and reduced rates of phosphorylation carbamylation	Gibney_1990_Proc.Natl.Acad.Sci.U.S.A_87_7546, Radic_1992_Biochemistry_31_9760
E199Q	sdm	Acylation	increases Km and Kss and reduces kcat	Gibney_1990_Proc.Natl.Acad.Sci.U.S.A_87_7546, Radic_1992_Biochemistry_31_9760, Saxena_1993_Biochem.Biophys.Res.Commun_197_343
E199Q	sdm	Acylation,Phosphorylation	Decreased affinity for reversible inhibitors and reduced rates of phosphorylation carbamylation	Gibney_1990_Proc.Natl.Acad.Sci.U.S.A_87_7546, Radic_1992_Biochemistry_31_9760, Saxena_1993_Biochem.Biophys.Res.Commun_197_343
E199Q	sdm	Acylation,Phosphorylation	resistant to aging	Saxena_1993_Biochem.Biophys.Res.Commun_197_343
E199Q	sdm	Huperzine A	3-fold increase in KI value for the binding of Huperzine A	Saxena_1994_Protein.Sci_3_1770
E199H	sdm	Acylation,Phosphorylation	very low activity	Gibney_1990_Proc.Natl.Acad.Sci.U.S.A_87_7546

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