Torpedo_number Report for: 330

brafl-ACHE2

Mutation	Kin.	Type	Evaluation system	Effect	Reference
Y352A		sdm	Acyl specificity		Pezzementi_2003_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_136_813

bunfa-ACHE

Mutation	Type	Evaluation system	Effect	Reference
Y330G	sdm	Substrate activation	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y330G	sdm	Signal transduction	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y330A	sdm	Substrate activation	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y330A	sdm	Signal transduction	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y330W	sdm	Substrate activation	Substrate activation at low inhibition at high	Masson_2002_Biochim.Biophys.Acta_1594_313
Y330W	sdm	Signal transduction	Substrate activation at low inhibition at high	Masson_2002_Biochim.Biophys.Acta_1594_313

drome-ACHE

Mutation	Type	Evaluation system	Effect	Reference
Y408A	sdm	Insecticide sensitivity		Boublik_2002_Protein.Eng_15_43
Y408F	sdm	Insecticide sensitivity		Boublik_2002_Protein.Eng_15_43
Y408F	sdm	Binding of Triton X-100 studies	mutation mimic the torpedo enzyme, no effect	Marcel_2000_J.Biol.Chem_275_11603
Y408F	sdm	OP biosensors	OP biosensors sensitivity increased 12 fold	Villatte_1998_Biosens.Bioelectron_13_157

human-ACHE : (kinetic parameters)

Mutation	Kin.	Type	Evaluation system	Effect	Reference
F295L/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
F297I/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
E202Q/ Y337A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
D134H/ 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
F295L/ Y337A/ F338A		sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
F295L/ F297V/ Y337A	kin	sdm	Acyl specificity	replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE	Kaplan_2001_Biochemistry_40_7433, Barak_2005_Chem.Biol.Interact_157-158_219
Y72N/ Y124Q/ W286A/ F295L/ F297W/ Y337A		sdm	Acyl specificity	replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE	Kaplan_2001_Biochemistry_40_7433
Y337A/ F338A		sdm	Acyl specificity		Shafferman_2005_Chem.Biol.Interact_157-158_123
Y337A/ F338A		sdm	Oxime interaction	non-aging catalytic bioscavenger	Cochran_2011_J.Biol.Chem_286_29718
Y72N/ Y124Q/ W286A/ F295L/ F297V/ Y337A/ V407F		sdm	Acyl specificity	Acyl pocket V407F does not increase kcat of the hexamutant	Barak_2002_Biochemistry_41_8245
Y337A	kin	sdm	Signal transduction	Decrease in catalytic and apparent bimolecular constant	Shafferman_1992_EMBO.J_11_3561, Barak_1994_J.Biol.Chem_269_6296, Ordentlich_1995_J.Biol.Chem_270_2082
Y337A	kin	sdm	Substrate inhibition	absence of substrate inhibition	Shafferman_1992_EMBO.J_11_3561, Barak_1994_J.Biol.Chem_269_6296, Ordentlich_1995_J.Biol.Chem_270_2082
Y337A	kin	sdm	Oxime interaction		Cochran_2011_J.Biol.Chem_286_29718
Y337A	kin	sdm	Acyl specificity	replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE	Kaplan_2001_Biochemistry_40_7433
Y337A	kin	sdm	oxime interaction	reactivation of tabun-inhibited human AChE. Unable to facilitate HI-6-mediated reactivation of tabun-hAChE	Artursson_2009_Toxicology_265_108
Y337G		sdm	Substrate activation	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y337G		sdm	Signal transduction	Substrate activation at low and high Ph	Masson_2002_Biochim.Biophys.Acta_1594_313
Y337W		sdm	Substrate activation	Substrate activation at low Ph inhibition at high	Masson_2002_Biochim.Biophys.Acta_1594_313
Y337W		sdm	Signal transduction	Substrate activation at low Ph inhibition at high	Masson_2002_Biochim.Biophys.Acta_1594_313
Y337F	kin	sdm	Signal transduction	very low effect on catalysis and inhibition	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Ordentlich_1993_J.Biol.Chem_268_17083, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Ashani_1994_Mol.Pharmacol_45_555, Barak_1994_J.Biol.Chem_269_6296, Ordentlich_1995_J.Biol.Chem_270_2082
Y337F	kin	sdm	Substrate inhibition	identical to wild type	Shafferman_1992_EMBO.J_11_3561, Shafferman_1992_4th.ChE.Meeting.Eilat__165, Ordentlich_1993_J.Biol.Chem_268_17083, Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097, Ashani_1994_Mol.Pharmacol_45_555, Barak_1994_J.Biol.Chem_269_6296, Ordentlich_1995_J.Biol.Chem_270_2082
Y337F	kin	sdm	oxime interaction	reactivation of tabun-inhibited human AChE. Unable to facilitate HI-6-mediated reactivation of tabun-hAChE. Induced a 2-2.5-fold enhancement of the bimolecular rate constant for K027 and HLo-7	Artursson_2009_Toxicology_265_108
Y72N/ Y124Q/ W286A/ F295L/ F297V/ Y337A	kin	sdm	Acyl specificity	replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE	Kaplan_2001_Biochemistry_40_7433

human-BCHE

Mutation	Type	Evaluation system	Effect	Reference
A328C	sdm	Active mutant		Lushchekina_2016_Chem.Biol.Interact_259_223
A328D	nat	Silent variant	Natural mutant	Gatke_2007_Pharmacogenet.Genomics_17_995
A328Y	sdm	Cocaine hydrolysis	4-fold improvement in catalytic efficiency kcat/Km	Xie_1999_Mol.Pharmacol_55_83
A328Y	sdm	Binding of inhibitors	smaller dimension of the active-site gorge	Saxena_1999_Chem.Biol.Interact_119-120_61
A328Y	sdm	Substrate activation	substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
A328Y	sdm	Aricept~Donepezil~E2020 inhibition	small increase Ki vs WT	Saxena_2003_Eur.J.Biochem_270_4447
A328W	sdm	Cocaine hydrolysis	hydrolyzed cocaine 15-fold faster compared with wild-type BChE	Duysen_2002_J.Pharmacol.Exp.Ther_302_751
A328W/ Y332A	sdm	Cocaine hydrolysis	CocE 40-fold increased kcat and low increase in Km	Sun_2002_Mol.Pharmacol_62_220
A328W/ Y332A/ Y419S	sdm	Cocaine hydrolysis	no activity	Hamza_2005_J.Phys.Chem.B_109_4776
A328W/ Y332G	sdm	Cocaine hydrolysis	Catalytic efficiency slightly higher than A328W/Y332A	Hamza_2005_J.Phys.Chem_109_4776
A199S/ F227A/ P285A/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	4400-fold improved catalytic efficiency against-cocaine E9	Zheng_2014_Nat.Commun_5_3457
A199S/ F227A/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	2000-fold improved catalytic efficiency against-cocaine E9	Zheng_2008_J.Am.Chem.Soc_130_12148
A199S/ F227A/ S287G/ A328W/ Y332G/ F364C/ M532C	sdm	Cocaine hydrolysis	improved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bonds	Fang_2014_Chem.Biol.Interact_214C_18
A199S/ F227A/ S287G/ A328W/ Y332G/ V377C/ A516C	sdm	Cocaine hydrolysis	improved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bonds	Fang_2014_Chem.Biol.Interact_214C_18
A199S/ F227A/ S287G/ A328W/ Y332G/ N535C	sdm	Cocaine hydrolysis	improved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bonds	Fang_2014_Chem.Biol.Interact_214C_18
A199S/ F227A/ S287G/ A328W/ Y332G/ F329V	sdm	Cocaine hydrolysis	E11	Zheng_2010_Biochemistry_49_9113
A199S/ F227L/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	1000-fold improved catalytic efficiency against-cocaine E	Zheng_2010_Biochemistry_49_9113
A199S/ F227A/ S287G/ A328W/ E441D	sdm	Cocaine hydrolysis	improved catalytic efficiency against-cocaine E	Xue_2011_Mol.Pharmacol_79_290
A199S/ F227I/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	1000-fold improved catalytic efficiency against-cocaine E	Zheng_2010_Biochemistry_49_9113
A199S/ F227V/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	1000-fold improved catalytic efficiency against-cocaine E	Zheng_2010_Biochemistry_49_9113
F227A/ S287G/ A328W/ Y332M	sdm	Cocaine hydrolysis	AME359 CocH, 34-fold improved catalytic efficiency against (-)-cocaine	Pancook_2003_FASEB.J_17_A565
A199S/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	CocH1 456-fold improved catalytic efficiency against (-)-cocaine	Pan_2005_Proc.Natl.Acad.Sci.U.S.A_102_16656
A199S/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis	Selectively blocks cocaine toxicity and reinstatement of drug seeking in rats (mutant fused to albumin TV-1380)	Brimijoin_2008_Neuropsychopharmacology_33_2715
A199S/ S287G/ A328W/ Y332G	sdm	Cocaine hydrolysis		Yang_2010_Chem.Biol.Interact_187_148
A199S/ S287G/ A328W/ Y332G/ L286I	sdm	Cocaine hydrolysis	E10	Zheng_2010_Biochemistry_49_9113
A328F	sdm	Binding of inhibitors	smaller dimension of the active-site gorge	Saxena_1999_Chem.Biol.Interact_119-120_61
A328F	sdm	Substrate activation	substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
A328F	sdm	Aricept~Donepezil~E2020 inhibition	10-fold increase Ki vs WT	Saxena_2003_Eur.J.Biochem_270_4447
A328F	sdm	Cationic triarylmethane dyes		Biberoglu_2011_Arch.Biochem.Biophys_511_64
A328G	sdm	Substrate activation	substrate activation	Masson_2001_Biochim.Biophys.Acta_1544_166
A328G	sdm	Aging	A328G decreases half-life of aging by DFP 0.9 times	Masson_1997_Biochem.J_327_601
A328G/ F329S	sdm	Aging	A328G/F329S increases half-life of aging by DFP 4.2 times	Masson_1997_Biochem.J_327_601

human-NLGN4X

Mutation	Kin.	Type	Evaluation system	Effect	Reference
K378R		nat	Natural mutation	Portuguese caucasian male mild autism	Yan_2005_Mol.Psychiatry_10_329

luccu-E3aest7

Mutation	Type	Evaluation system	Effect	Reference
F354W	sdm	OP-resistance	search for OP hydrolase and MCE activities	Heidari_2004_Insect.Biochem.Mol.Biol_34_353
F354W	sdm	Pyrethroids hydrolysis	search for Pyrethroids hydrolysis activities	Heidari_2005_Insect.Biochem.Mol.Biol_35_597
F354W	sdm	Pyrethroids hydrolysis	Hydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterases	Devonshire_2007_Insect.Biochem.Mol.Biol_37_891
F354L	sdm	OP-resistance	search for OP hydrolase and MCE activities	Heidari_2004_Insect.Biochem.Mol.Biol_34_353
F354L	sdm	Pyrethroids hydrolysis	search for Pyrethroids hydrolysis activities	Heidari_2005_Insect.Biochem.Mol.Biol_35_597
F354L	sdm	Pyrethroids hydrolysis	Hydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterases	Devonshire_2007_Insect.Biochem.Mol.Biol_37_891

mouse-ACHE : (kinetic parameters)

Mutation	Kin.	Type	Evaluation system	Effect	Reference
Y337A/ F338A		sdm	Oxime interaction	non-aging catalytic bioscavenger	Kovarik_2004_Biochemistry_43_3222
Y337A	kin	sdm	Signal transduction	responsible for the 1800 fold difference in Ki for ethopropazine AChE/BChE	Radic_1993_Biochemistry_32_12074, Radic_1994_J.Biol.Chem_269_11233, Saxena_1994_Protein.Sci_3_1770
Y337A	kin	sdm	Aricept~Donepezil~E2020 inhibition	decrease Ki vs WT	Saxena_2003_Eur.J.Biochem_270_4447
Y337A	kin	sdm	Oxime interaction	enlargement of the active site of the gorge	Kovarik_2006_Biochem.Biophys.Res.Commun_342_973, Kovarik_2007_Toxicology_233_79
Y337A	kin	sdm	Oxime interaction		Kovarik_2004_Biochemistry_43_3222
F295L/ Y337A		sdm	Oxime interaction	enlargement of the active site of the gorge	Kovarik_2006_Biochem.Biophys.Res.Commun_342_973, Kovarik_2007_Toxicology_233_79
F295L/ Y337A		sdm	Acyl specificity	enlargement of the active site of the gorge	Kovarik_2006_Biochem.Biophys.Res.Commun_342_973, Kovarik_2007_Toxicology_233_79
F295L/ Y337A		sdm	Oxime interaction		Kovarik_2004_Biochemistry_43_3222
F297I/ Y337A		sdm	Oxime interaction	enlargement of the active site of the gorge	Kovarik_2006_Biochem.Biophys.Res.Commun_342_973, Kovarik_2007_Toxicology_233_79
F297I/ Y337A		sdm	Oxime interaction		Kovarik_2004_Biochemistry_43_3222
F295L/ F297I/ Y337A		sdm	oxime interaction	enlargement of the active site of the gorge	Kovarik_2006_Biochem.Biophys.Res.Commun_342_973
F295L/ F297I/ Y337A		sdm	Oxime interaction		Kovarik_2004_Biochemistry_43_3222
Y337F	kin	sdm	Signal transduction	less effect than Y337A on occlusion of ethopropazine binding site	Radic_1993_Biochemistry_32_12074, Saxena_1994_Protein.Sci_3_1770
Y337F	kin	sdm	Substrate inhibition	less effect than Y337A on occlusion of ethopropazine binding site	Radic_1993_Biochemistry_32_12074, Saxena_1994_Protein.Sci_3_1770
Y337F	kin	sdm	Aricept~Donepezil~E2020 inhibition	decrease Ki vs WT	Saxena_2003_Eur.J.Biochem_270_4447

mouse-BCHE

Mutation	Kin.	Type	Evaluation system	Effect	Reference
A199S/ F227A/ S287G/ A328W/ Y332G		sdm	Cocaine hydrolysis		Chen_2015_Biochem.J_466_243

musdo-EST23aes07

Mutation	Kin.	Type	Evaluation system	Effect	Reference
L354F		nat	OP-resistance		Zhang_2018_Sci.Rep_8_224
L354F		nat	OP-resistance		Zhang_2010_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_156_6

nillu-ACHE1

Mutation	Kin.	Type	Evaluation system	Effect	Reference
F/ Y330S		nat	OP-resistance	associated in carbofuran resistant strain (CAS)	Kwon_2012_Pestic.Biochem.Physiol_103_94

nipbr-ACHEB

Mutation	Type	Evaluation system	Reference
F345A	sdm	Insecticide sensitivity	Schulze_2005_Anal.Chem_77_5823
F345Y	sdm	Insecticide sensitivity	Schulze_2005_Anal.Chem_77_5823
M301A/ F345A	sdm	Insecticide sensitivity	Schulze_2005_Anal.Chem_77_5823
M301A/ F345Y	sdm	Insecticide sensitivity	Schulze_2005_Anal.Chem_77_5823

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