Torpedo_number

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Torpedo_number Report for: 330

brafl-ACHE2
MutationKin.TypeEvaluation systemEffectReference
Y352A sdmAcyl specificityPezzementi_2003_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_136_813

bunfa-ACHE
MutationKin.TypeEvaluation systemEffectReference
Y330G sdmSubstrate activationSubstrate activation at low and high Ph Masson_2002_Biochim.Biophys.Acta_1594_313
Y330G sdmSignal transductionSubstrate activation at low and high Ph Masson_2002_Biochim.Biophys.Acta_1594_313
Y330A sdmSubstrate activationSubstrate activation at low and high Ph Masson_2002_Biochim.Biophys.Acta_1594_313
Y330A sdmSignal transductionSubstrate activation at low and high Ph Masson_2002_Biochim.Biophys.Acta_1594_313
Y330W sdmSubstrate activationSubstrate activation at low inhibition at highMasson_2002_Biochim.Biophys.Acta_1594_313
Y330W sdmSignal transductionSubstrate activation at low inhibition at highMasson_2002_Biochim.Biophys.Acta_1594_313

drome-ACHE
MutationKin.TypeEvaluation systemEffectReference
Y408A sdmInsecticide sensitivityBoublik_2002_Protein.Eng_15_43
Y408F sdmInsecticide sensitivityBoublik_2002_Protein.Eng_15_43
Y408F sdmBinding of Triton X-100 studiesmutation mimic the torpedo enzyme, no effectMarcel_2000_J.Biol.Chem_275_11603
Y408F sdmOP biosensorsOP biosensors sensitivity increased 12 foldVillatte_1998_Biosens.Bioelectron_13_157

human-ACHE : (kinetic parameters)
MutationKin.TypeEvaluation systemEffectReference
F295L/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
F297I/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
E202Q/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
D134H/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
E202Q/
F295L/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
E202Q/
F297I/
Y337A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
F295L/
Y337A/
F338A
 sdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
F295L/
F297V/
Y337A
kinsdmAcyl specificityreplacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHEKaplan_2001_Biochemistry_40_7433,
Barak_2005_Chem.Biol.Interact_157-158_219
Y72N/
Y124Q/
W286A/
F295L/
F297W/
Y337A
 sdmAcyl specificityreplacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHEKaplan_2001_Biochemistry_40_7433
Y337A/
F338A
 sdmAcyl specificityShafferman_2005_Chem.Biol.Interact_157-158_123
Y337A/
F338A
 sdmOxime interactionnon-aging catalytic bioscavengerCochran_2011_J.Biol.Chem_286_29718
Y72N/
Y124Q/
W286A/
F295L/
F297V/
Y337A/
V407F
 sdmAcyl specificity Acyl pocket V407F does not increase kcat of the hexamutantBarak_2002_Biochemistry_41_8245
Y337AkinsdmSignal transductionDecrease 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
Y337AkinsdmSubstrate inhibitionabsence of substrate inhibitionShafferman_1992_EMBO.J_11_3561,
Barak_1994_J.Biol.Chem_269_6296,
Ordentlich_1995_J.Biol.Chem_270_2082
Y337AkinsdmOxime interactionCochran_2011_J.Biol.Chem_286_29718
Y337AkinsdmAcyl specificityreplacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHEKaplan_2001_Biochemistry_40_7433
Y337Akinsdmoxime interactionreactivation of tabun-inhibited human AChE. Unable to facilitate HI-6-mediated reactivation of tabun-hAChEArtursson_2009_Toxicology_265_108
Y337G sdmSubstrate activationSubstrate activation at low and high PhMasson_2002_Biochim.Biophys.Acta_1594_313
Y337G sdmSignal transductionSubstrate activation at low and high PhMasson_2002_Biochim.Biophys.Acta_1594_313
Y337W sdmSubstrate activationSubstrate activation at low Ph inhibition at highMasson_2002_Biochim.Biophys.Acta_1594_313
Y337W sdmSignal transductionSubstrate activation at low Ph inhibition at highMasson_2002_Biochim.Biophys.Acta_1594_313
Y337FkinsdmSignal transductionvery low effect on catalysis and inhibitionShafferman_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
Y337FkinsdmSubstrate inhibitionidentical to wild typeShafferman_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
Y337Fkinsdmoxime interactionreactivation 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-7Artursson_2009_Toxicology_265_108
Y72N/
Y124Q/
W286A/
F295L/
F297V/
Y337A
kinsdmAcyl specificityreplacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHEKaplan_2001_Biochemistry_40_7433

human-BCHE
MutationKin.TypeEvaluation systemEffectReference
A328C sdmActive mutantLushchekina_2016_Chem.Biol.Interact_259_223
A328D natSilent variantNatural mutantGatke_2007_Pharmacogenet.Genomics_17_995
A328Y sdmCocaine hydrolysis4-fold improvement in catalytic efficiency kcat/KmXie_1999_Mol.Pharmacol_55_83
A328Y sdmBinding of inhibitorssmaller dimension of the active-site gorgeSaxena_1999_Chem.Biol.Interact_119-120_61
A328Y sdmSubstrate activationsubstrate activationMasson_2001_Biochim.Biophys.Acta_1544_166
A328Y sdmAricept~Donepezil~E2020 inhibitionsmall increase Ki vs WTSaxena_2003_Eur.J.Biochem_270_4447
A328W sdmCocaine hydrolysishydrolyzed cocaine 15-fold faster compared with wild-type BChEDuysen_2002_J.Pharmacol.Exp.Ther_302_751
A328W/
Y332A
 sdmCocaine hydrolysisCocE 40-fold increased kcat and low increase in KmSun_2002_Mol.Pharmacol_62_220
A328W/
Y332A/
Y419S
 sdmCocaine hydrolysisno activityHamza_2005_J.Phys.Chem.B_109_4776
A328W/
Y332G
 sdmCocaine hydrolysisCatalytic efficiency slightly higher than A328W/Y332AHamza_2005_J.Phys.Chem_109_4776
A199S/
F227S/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 2790-fold improved catalytic efficiency against (-)-cocaine Zheng_2023_J.Phys.Chem.B__
A199S/
F227A/
P285A/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 4400-fold improved catalytic efficiency against-cocaine E9 Zheng_2014_Nat.Commun_5_3457
A199S/
F227A/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 2000-fold improved catalytic efficiency against-cocaine E9 Zheng_2008_J.Am.Chem.Soc_130_12148
A199S/
F227A/
S287G/
A328W/
Y332G/
F364C/
M532C
 sdmCocaine hydrolysisimproved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bondsFang_2014_Chem.Biol.Interact_214C_18
A199S/
F227A/
S287G/
A328W/
Y332G/
V377C/
A516C
 sdmCocaine hydrolysisimproved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bondsFang_2014_Chem.Biol.Interact_214C_18
A199S/
F227A/
S287G/
A328W/
Y332G/
N535C
 sdmCocaine hydrolysisimproved catalytic efficiency against-cocaine and increased biological half-life with new cross-subunit SS bondsFang_2014_Chem.Biol.Interact_214C_18
A199S/
F227A/
S287G/
A328W/
Y332G/
F329V
 sdmCocaine hydrolysis E11 Zheng_2010_Biochemistry_49_9113
A199S/
F227L/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 1000-fold improved catalytic efficiency against-cocaine E Zheng_2010_Biochemistry_49_9113
A199S/
F227A/
S287G/
A328W/
E441D
 sdmCocaine hydrolysis improved catalytic efficiency against-cocaine E Xue_2011_Mol.Pharmacol_79_290
A199S/
F227I/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 1000-fold improved catalytic efficiency against-cocaine E Zheng_2010_Biochemistry_49_9113
A199S/
F227V/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis 1000-fold improved catalytic efficiency against-cocaine E Zheng_2010_Biochemistry_49_9113
F227A/
S287G/
A328W/
Y332M
 sdmCocaine hydrolysisAME359 CocH, 34-fold improved catalytic efficiency against (-)-cocaine Pancook_2003_FASEB.J_17_A565
A199S/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysisCocH1 456-fold improved catalytic efficiency against (-)-cocaine Pan_2005_Proc.Natl.Acad.Sci.U.S.A_102_16656
A199S/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysisSelectively 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
 sdmCocaine hydrolysisYang_2010_Chem.Biol.Interact_187_148
A199S/
S287G/
A328W/
Y332G/
L286I
 sdmCocaine hydrolysisE10Zheng_2010_Biochemistry_49_9113
A328F sdmBinding of inhibitorssmaller dimension of the active-site gorgeSaxena_1999_Chem.Biol.Interact_119-120_61
A328F sdmSubstrate activationsubstrate activationMasson_2001_Biochim.Biophys.Acta_1544_166
A328F sdmAricept~Donepezil~E2020 inhibition10-fold increase Ki vs WTSaxena_2003_Eur.J.Biochem_270_4447
A328F sdmCationic triarylmethane dyesBiberoglu_2011_Arch.Biochem.Biophys_511_64
A328G sdmSubstrate activationsubstrate activationMasson_2001_Biochim.Biophys.Acta_1544_166
A328G sdmAgingA328G decreases half-life of aging by DFP 0.9 timesMasson_1997_Biochem.J_327_601
A328G/
F329S
 sdmAgingA328G/F329S increases half-life of aging by DFP 4.2 timesMasson_1997_Biochem.J_327_601

human-NLGN4X
MutationKin.TypeEvaluation systemEffectReference
K378R natNatural mutationPortuguese caucasian male mild autism Yan_2005_Mol.Psychiatry_10_329

luccu-E3aest7
MutationKin.TypeEvaluation systemEffectReference
F354W sdmOP-resistancesearch for OP hydrolase and MCE activities Heidari_2004_Insect.Biochem.Mol.Biol_34_353
F354W sdmPyrethroids hydrolysissearch for Pyrethroids hydrolysis activities Heidari_2005_Insect.Biochem.Mol.Biol_35_597
F354W sdmPyrethroids hydrolysisHydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterasesDevonshire_2007_Insect.Biochem.Mol.Biol_37_891
F354L sdmOP-resistancesearch for OP hydrolase and MCE activities Heidari_2004_Insect.Biochem.Mol.Biol_34_353
F354L sdmPyrethroids hydrolysissearch for Pyrethroids hydrolysis activities Heidari_2005_Insect.Biochem.Mol.Biol_35_597
F354L sdmPyrethroids hydrolysisHydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterasesDevonshire_2007_Insect.Biochem.Mol.Biol_37_891

mouse-ACHE : (kinetic parameters)
MutationKin.TypeEvaluation systemEffectReference
Y337A/
F338A
 sdmOxime interactionnon-aging catalytic bioscavengerKovarik_2004_Biochemistry_43_3222
Y337AkinsdmSignal transductionresponsible for the 1800 fold difference in Ki for ethopropazine AChE/BChERadic_1993_Biochemistry_32_12074,
Radic_1994_J.Biol.Chem_269_11233,
Saxena_1994_Protein.Sci_3_1770
Y337AkinsdmAricept~Donepezil~E2020 inhibitiondecrease Ki vs WTSaxena_2003_Eur.J.Biochem_270_4447
Y337AkinsdmOxime interactionenlargement of the active site of the gorgeKovarik_2006_Biochem.Biophys.Res.Commun_342_973,
Kovarik_2007_Toxicology_233_79
Y337AkinsdmOxime interactionKovarik_2004_Biochemistry_43_3222
F295L/
Y337A
 sdmOxime interactionenlargement of the active site of the gorgeKovarik_2006_Biochem.Biophys.Res.Commun_342_973,
Kovarik_2007_Toxicology_233_79
F295L/
Y337A
 sdmAcyl specificityenlargement of the active site of the gorgeKovarik_2006_Biochem.Biophys.Res.Commun_342_973,
Kovarik_2007_Toxicology_233_79
F295L/
Y337A
 sdmOxime interactionKovarik_2004_Biochemistry_43_3222
F297I/
Y337A
 sdmOxime interactionenlargement of the active site of the gorgeKovarik_2006_Biochem.Biophys.Res.Commun_342_973,
Kovarik_2007_Toxicology_233_79
F297I/
Y337A
 sdmOxime interactionKovarik_2004_Biochemistry_43_3222
F295L/
F297I/
Y337A
 sdmoxime interactionenlargement of the active site of the gorgeKovarik_2006_Biochem.Biophys.Res.Commun_342_973
F295L/
F297I/
Y337A
 sdmOxime interactionKovarik_2004_Biochemistry_43_3222
Y337FkinsdmSignal transductionless effect than Y337A on occlusion of ethopropazine binding siteRadic_1993_Biochemistry_32_12074,
Saxena_1994_Protein.Sci_3_1770
Y337FkinsdmSubstrate inhibitionless effect than Y337A on occlusion of ethopropazine binding siteRadic_1993_Biochemistry_32_12074,
Saxena_1994_Protein.Sci_3_1770
Y337FkinsdmAricept~Donepezil~E2020 inhibitiondecrease Ki vs WTSaxena_2003_Eur.J.Biochem_270_4447

mouse-BCHE
MutationKin.TypeEvaluation systemEffectReference
A199S/
F227A/
S287G/
A328W/
Y332G
 sdmCocaine hydrolysis Chen_2015_Biochem.J_466_243

musdo-EST23aes07
MutationKin.TypeEvaluation systemEffectReference
L354F natOP-resistanceZhang_2018_Sci.Rep_8_224
L354F natOP-resistanceZhang_2010_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_156_6

nillu-ACHE1
MutationKin.TypeEvaluation systemEffectReference
F/
Y330S
 natOP-resistance associated in carbofuran resistant strain (CAS)Kwon_2012_Pestic.Biochem.Physiol_103_94

nipbr-ACHEB
MutationKin.TypeEvaluation systemEffectReference
F345A sdmInsecticide sensitivitySchulze_2005_Anal.Chem_77_5823
F345Y sdmInsecticide sensitivitySchulze_2005_Anal.Chem_77_5823
M301A/
F345A
 sdmInsecticide sensitivitySchulze_2005_Anal.Chem_77_5823
M301A/
F345Y
 sdmInsecticide sensitivitySchulze_2005_Anal.Chem_77_5823

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