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3,3-dimethylbutyl methylphosphonyl thiocholine
-
4-ketoamyltrimethylammonium
binding structure analysis
Acetylcholine
substrate inhibition
bambuterol
a specific and stereoselective inhibitor of butyrylcholinesterase, which is about 8000times faster inhibited than acetylcholinesterase. AChE wild-type enzyme, and mutants F297I/Y337A and F295L/F297I/Y337A show a deviation from linearity, either enzymes are inhibited by racemate or enantiomers, indicating the presence of reversible enzyme-inhibitor complex, overview
choline
product inhibition, binding structure analysis
cycloheptyl methylphosphonyl thiocholine
SP and RP enantiomers
diisopropyl fluorophosphate
nerve agent, binding structure, overview
fasciculin
binds at the mouth of the gorge, decreases the mobility of reporter groups attached to L76C and Y124C, increases the mobility of reporter groups attached to E81C and E84C
-
huperzine
binds at the base of the active site gorge, has no effect on the mobility of reporter groups attached to L76C and Y124C, increases the mobility of reporter groups attached to E81C and E84C
isopropyl methylphosphonyl thiocholine
SP and RP enantiomers
m-(N,N,N-trimethylammonio)-trifluoroacetophenone
binding structure analysis
methamidophos
an organophosphorous-based insecticide, binding structure, overview
sarin
nerve agent, binding structure, overview
succinyldicholine
substrate inhibition, binding structure analysis
TFK+
analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview
TFK0
analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview
VX (nerve agent)
i.e. O-ethyl S-2-isopropylaminoethyl methylphosphonothiolate, nerve agent, binding structure, overview
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
E2020, acetylcholinesterase inhibitor used in treatment of Alzheimer's diaease, inhibition kinetics
1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide
-
-
2,2-dichlorovinyl dimethyl phosphate
-
i.e. DDVP, reversible, detailed kinetic analysis
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
i.e. 2-PAM, reversible, detailed kinetic analysis
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
i.e. HI-6, reversible, detailed kinetic analysis
4-O-methylhonokiol
-
isolated from ethanol extract of Magnolia officinalis. 4-O-methylhonokiol also dose-dependently attenuates the scopolamine-induced increase of AChE activity in the cortex and hippocampus of mice
aflatoxin B1
-
50% inhibition at 0.031 mM by increase of Km-value and decrease of vmax-value. Partial recativation by 2-aldoxime, i.e. 2-PAM, pyridin-2-aldoxime 1-methoiodide
Insulin
-
AChE activity in detergent soluble fraction of scopolamine amnesic mice is inhibited by donepezil, insulin and melatonin with varying extent in different brain regions, whereas AChE activity in salt soluble fraction is not much affected, overview
-
Melatonin
-
AChE activity in detergent soluble fraction of scopolamine amnesic mice is inhibited by donepezil, insulin and melatonin with varying extent in different brain regions, whereas AChE activity in salt soluble fraction is not much affected, overview
methyl (3-{4-[({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}propyl)phosphonofluoridate
-
-
methyl (3-{4-[({[6-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}propyl)phosphonofluoridate
-
-
methyl (4-{4-[({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}butyl)phosphonofluoridate
-
-
methyl (4-{4-[({[6-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}butyl)phosphonofluoridate
-
-
methyl paraoxon
-
reversible binding to a site on acetylcholinesterase distinct from the active site reduces their subsequent capacity to phosphorylate the active site, probably by steric hindrance or allosteric modification of the active site
methyl [3-(4-{[(4-{(E)-[4-(dimethylamino)phenyl]diazenyl}benzoyl)amino]methyl}-1H-1,2,3-triazol-1-yl)propyl]phosphonofluoridate
-
-
methyl [3-(4-{[(pyren-2-ylsulfonyl)amino]methyl}-1H-1,2,3-triazol-1-yl)propyl]phosphonofluoridate
-
-
methyl [4-(4-{[(4-{(E)-[4-(dimethylamino)phenyl]diazenyl}benzoyl)amino]methyl}-1H-1,2,3-triazol-1-yl)butyl]phosphonofluoridate
-
-
methyl [4-(4-{[(pyren-2-ylsulfonyl)amino]methyl}-1H-1,2,3-triazol-1-yl)butyl]phosphonofluoridate
-
-
methyl {3-[4-({[(6-methoxy-2-oxo-2H-chromen-3-yl)carbonyl]amino}methyl)-1H-1,2,3-triazol-1-yl]propyl}phosphonofluoridate
-
-
methyl {4-[4-({[(6-methoxy-2-oxo-2H-chromen-3-yl)carbonyl]amino}methyl)-1H-1,2,3-triazol-1-yl]butyl}phosphonofluoridate
-
-
methylorganophosphonates
-
the Sp-enantiomer is more reactive
-
muscarine
-
treatment with 0.01 mM muscarine leads to a 20% decrease in enzyme activity in SN-56 cells
O-O-dimethyl-O-(2,2-dichlorovinyl)phosphate
-
phosphorylates the active site serine
RP cycloheptyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can only poorly be reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
RP-3,3-dimethylbutyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can only poorly be reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
RP-isopropyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
SP-3,3-dimethylbutyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
SP-cycloheptyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
SP-isopropyl methylphosphonyl thiocholine
-
phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
Tabun
-
an organophosphorous inhibitor
tea polyphenol
-
up to 60% inhibition of enzyme
trifluoroacetophenone
-
inhibits Y124C mutant slower than the wild-type enzyme
fenamiphos
an organophosphorous-based insecticide, binding structure, overview
fenamiphos
an organophosphorus compound and insecticide
BW284c51
-
50% inhibition at 0.000021 mM
BW284c51
-
i.e. 1,5-bis(4-allyldimethyl-ammoniumphenyl)pentane-3-one dibromide, specific inhibition of AChE
donepezil
-
AChE activity in detergent soluble fraction of scopolamine amnesic mice is inhibited by donepezil, insulin and melatonin with varying extent in different brain regions, whereas AChE activity in salt soluble fraction is not much affected, overview
donepezil
-
donepezil concomitantly elevates VEGF expression in intracardiac endothelial cells of wild-type and alpha7 KO mice and further increases choline acetyltransferase protein expression, which is critical for acetylcholine synthesis in endothelial cells
fasciculin
-
-
-
fasciculin
-
inhibits catalysis peripherally by sealing the mouth of the active center gorge
-
galanthamine
-
-
galanthamine
-
a competitive and reversible, specific inhibitor, crosses the blood brain barrier, significantly increases brain cholinergic network activity
paraoxon
-
-
paraoxon
-
26% inhibition at 0.0000001 mM, reversible binding to a site on acetylcholinesterase distinct from the active site reduces their subsequent capacity to phosphorylate the active site
additional information
oxime-based reactivators, such as [(E)-[1-[(4-carbamoylpyridin-1-ium-1-yl)methoxymethyl]pyridin-2-ylidene]methyl]-oxoazanium dichloride, i.e. HI-6, and 1,7-heptylene-bis-N,N0-2-pyridiniumaldoxime dichloride, i.e. Ortho-7, restore the organophosphate-inhibited enzymatic activity by cleaving the phosphorous conjugate, overview. Flipping of the His447 imidazole ring allows the formation of a hydrogen bonding network among the Glu334-His447-Ortho-7 triad, which presumably deprotonates the Ortho-7 oxime hydroxyl group, increases the nucleophilicity of the oxime group, and leads to cleavage of the phosphorous conjugate. Binding structure determination and analysis, higher reactivation rate of HI-6 than Ortho-7, overview
-
additional information
-
oxime-based reactivators, such as [(E)-[1-[(4-carbamoylpyridin-1-ium-1-yl)methoxymethyl]pyridin-2-ylidene]methyl]-oxoazanium dichloride, i.e. HI-6, and 1,7-heptylene-bis-N,N0-2-pyridiniumaldoxime dichloride, i.e. Ortho-7, restore the organophosphate-inhibited enzymatic activity by cleaving the phosphorous conjugate, overview. Flipping of the His447 imidazole ring allows the formation of a hydrogen bonding network among the Glu334-His447-Ortho-7 triad, which presumably deprotonates the Ortho-7 oxime hydroxyl group, increases the nucleophilicity of the oxime group, and leads to cleavage of the phosphorous conjugate. Binding structure determination and analysis, higher reactivation rate of HI-6 than Ortho-7, overview
-
additional information
-
organophosphate inhibitor binding and active site gorge structure, oveview, nucleophilic oximes, i.e. bis-quarternary oximes, aldoximes, and hydroxamates, act as reactivators of the inhibited enzyme and are of therapeutic use, overview
-
additional information
-
blueberry polyphenols, as gallic acid equivalents, directly inhibit AChE to 64-66% reduced activity of the detergent soluble and the salt soluble enzyme, respectively
-
additional information
-
chromophore-linked fluorophosphonate inhibitors show bimolecular inhibition constants ranging from 0.3 * 105 M/min to 10.4 * 105 M/min
-
additional information
-
inhibitory effect on AChE of the ethanol extract of Magnolia officinalis, overview
-
additional information
-
oximes poorly reactivate tabun-inhibited AChE. In silico pharmacophore model for binding affinity of tabun-inhibited AChE from a set of 11 oximes, 9 of which show binding to the inhibited enzyme, overview. Stereoelectronic profiles and three-dimensional quantitative structure-activity relationship pharmacophores using ab initio quantum chemical and pharmacophore generation methods, detailed overview
-
additional information
-
not inhibited by GM6001
-
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0.023
4-ketoamyltrimethylammonium
pH 7.0, 22°C, recombinant wild-type enzyme
1.4
choline
pH 7.0, 22°C, recombinant wild-type enzyme
0.021
succinyldicholine
pH 7.0, 22°C, recombinant wild-type enzyme
0.0000004 - 0.0087
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
0.15 - 1.7
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
0.046 - 0.36
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
additional information
additional information
-
0.0000004
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, Y337A mutant
0.0000005
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, Y337F mutant
0.0000022
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, wild-type enzyme
0.00002
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, Y124Q mutant
0.00002
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, Y72N mutant
0.000027
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, F295L mutant
0.00007
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, F297I mutant
0.00069
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, W86A mutant
0.0032
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, W286A mutant
0.0051
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, D74N mutant
0.0087
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C, Y72N/Y124N/W286R mutant
0.15
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
pH 7.0, 25°C, wild-type
0.28
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
pH 7.0, 25°C, mutant Y72N/Y124Q/W286A
0.59
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
pH 7.0, 25°C, mutant Y337A
0.65
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
pH 7.0, 25°C, mutant F295L/Y337A
1.7
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
-
pH 7.0, 25°C, mutant F297I/Y337A
0.046
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
pH 7.0, 25°C, wild-type
0.087
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
pH 7.0, 25°C, mutant Y337A
0.11
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
pH 7.0, 25°C, mutant F295L/Y337A
0.18
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
pH 7.0, 25°C, mutant F297I/Y337A
0.36
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
-
pH 7.0, 25°C, mutant Y72N/Y124Q/W286A
additional information
additional information
inhibition kinetics, wild-type and mutant enzymes, overview
-
additional information
additional information
-
inhibition kinetics, wild-type and mutant enzymes, overview
-
additional information
additional information
inhibition kinetics of wild-type and knockout mutant enzyme
-
additional information
additional information
-
inhibition kinetics of wild-type and knockout mutant enzyme
-
additional information
additional information
-
inhibition rate constants, overview
-
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E81C
reporter group 5-((((2-acetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid attached to cysteine
E84C
reporter group 5-((((2-acetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid attached to cysteine
F295A/Y337A
mutant retains hydrolytic activity
F296L/F297I/Y337A
site-directed mutagenesis, the mutant shows a 14fold decreased inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
H447I
inhibitor TFK+ binding to the H447I mutant proceeds with a different reaction mechanism from the wild-type enzyme. A water molecule takes over the role of His447 and participates in the bond breaking and forming as a charge relayer. Unlike in the wild-type mAChE case, Glu334, a conserved residue from the catalytic triad, acts as a catalytic base in the reaction
L76C
reporter group 5-((((2-acetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid attached to cysteine
S203A
site-directed mutagenesis of the catalytic site residue, inactive mutant
Y124C
reporter group 5-((((2-acetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid attached to cysteine
Y124Q
site-directed mutagenesis, the mutant shows an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
Y337A
site-directed mutagenesis, the mutant shows an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
Y337A/E202Q/F295A
mutant retains hydrolytic activity
Y337A/F295A/F297A
4fold increased Km
Y337A/F295L/F297I
mutant retains hydrolytic activity
Y337A/F295L/Y338A
no substrate inactivation
Y337A/F338A
mutant retains hydrolytic activity
Y72N/Y124Q/Y337A
site-directed mutagenesis, the mutant shows an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
D74N
-
altered Ki for E2020
E81C
-
kinetics similar to wild-type enzyme
E84C
-
4fold increased Km, 2fold increase in Kd for edrophonium binding, 18fold increase for 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide binding
F295L/F297I/Y337A
-
mutant enzyme can be partially reactivated after phosphonylation
F297I/Y337A
-
mutant enzyme can be partially reactivated after phosphonylation
L76C
-
kinetics similar to wild-type enzyme
W86A
-
altered Ki for E2020
Y124C-acrylodan
-
mutant retains hydrolytic activity
Y124C-benzyl
-
mutant retains hydrolytic activity
Y124C-N(CH3)3+
-
mutant with increased Km
Y124C-NH3+
-
mutant with increased Km
Y124C-SO3-
-
mutant retains hydrolytic activity
Y337F
-
altered Ki for E2020
Y72N/Y124N/W286R
-
altered Ki for E2020
F295L/Y337A
mutant retains hydrolytic activity
F295L/Y337A
site-directed mutagenesis, the mutant an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
F295L/Y337A
site-directed mutagenesis, the mutant shows a 13fold increased inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
F297I/Y337A
increased inhibition by RP-cycloheptyl methylphosphonyl thiocholine
F297I/Y337A
site-directed mutagenesis, the mutant shows an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
A262C
-
kinetics similar to wild-type enzyme, association and dissociation rate of fasciculin similar to wild type enzyme
A262C
-
mutant retains hydrolytic activity
F295L
-
altered Ki for E2020
F295L
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
F295L
-
the mutant shows enhanced reactivation rate by the oximes HI-6 and 2-PAM compared to the wild-type enzyme
F295L/Y337A
-
mutant enzyme can be partially reactivated after phosphonylation
F295L/Y337A
-
the mutant shows 120fold enhanced reactivation rate by the oximes HI-6 and 2-PAM compared to the wild-type enzyme
F297I
-
altered Ki for E2020
F297I
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
F297I
-
the mutant shows enhanced reactivation rate by the oximes HI-6 and 2-PAM compared to the wild-type enzyme
H287C
-
kinetics similar to wild-type enzyme, association and dissociation rate of fasciculin similar to wild type enzyme
H287C
-
mutant retains hydrolytic activity
W286A
-
altered Ki for E2020
W286A
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
Y124C
-
kinetics similar to wild-type enzyme, association and dissociation rate of fasciculin similar to wild type enzyme
Y124C
-
mutant retains hydrolytic activity
Y124Q
-
altered Ki for E2020
Y124Q
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
Y337A
-
altered Ki for E2020
Y337A
-
reactivation of mutant enzyme after phosphonylation with RP-3,3-dimethylbutyl methylphosphonyl thiocholine with 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide is better than reactivation of wild-type enzyme
Y337A
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
Y337A
-
the mutant shows enhanced reactivation rate by the oximes HI-6 and 2-PAM compared to the wild-type enzyme
Y337A/F338A
-
mutant enzyme can be partially reactivated after phosphonylation
Y337A/F338A
-
the mutant shows enhanced reactivation rate by the oximes HI-6 and 2-PAM compared to the wild-type enzyme
Y72N
-
altered Ki for E2020
Y72N
-
analysis of inhibition kinetics for 2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride, 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, and 2,2-dichlorovinyl dimethyl phosphate
additional information
-
stop codon in place of Cys549
additional information
-
neuromuscular transmission during repetitive nerve stimulation is severely depressed in the AChE knockout mice, AChE deficiency phenotype, overview
additional information
-
donepezil accelerates angiogenesis even in alpha7 KO mice with hindlimb ischemia. alpha7 KO mice phenotype, overview
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Bourne, Y.; Taylor, P.; Bougis, P.E.; Marchot, P.
Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly
J. Biol. Chem.
274
2963-2970
1999
Mus musculus
brenda
Marchot, P.; Ravelli, R.B.G.; Raves, M.L.; Bourne, Y.; Vellom, D.C.; Kanter, J.; Camp, S.; Sussman, J.L.; Taylor, P.
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin
Protein Sci.
5
672-679
1996
Mus musculus
brenda
Gomez, J.L.; Moral-Naranjo, M.T.; Compoy, F.J.; Vidal, C.J.
Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart
J. Neurosci. Res.
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1999
Mus musculus
brenda
Kovarik, Z.; Radic, Z.; Berman, H.A.; Simeon-Rudolf, V.; Reiner, E.; Taylor, P.
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates
Biochem. J.
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2003
Mus musculus (P21836), Mus musculus
brenda
Kovarik, Z.; Radic, Z.; Berman, H.A.; Simeon-Rudolf, V.; Reiner, E.; Taylor, P.
Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates
Biochemistry
43
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2004
Mus musculus
brenda
Zatta, P.; Ibn-Lkhayat-Idrissi, M.; Zambenedetti, P.; Kilyen, M.; Kiss, T.
In vivo and in vitro effects of aluminum on the activity of mouse brain acetylcholinesterase
Brain Res. Bull.
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2002
Mus musculus
brenda
Saxena, A.; Fedorko, J.M.; Vinayaka, C.R.; Medhekar, R.; Radic, Z.; Taylor, P.; Lockridge, O.; Doctor, B.P.
Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases
Eur. J. Biochem.
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2003
Mus musculus, Tetronarce californica
brenda
Gomez, J.L.; Nieto-Ceron, S.; Campoy, F.J.; Munoz-Delgado, E.; Vidal, C.J.
Purification and properties of hydrophilic dimers of acetylcholinesterase from mouse erythrocytes
Int. J. Biochem. Cell Biol.
35
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2003
Mus musculus
brenda
Kua, J.; Zhang, Y.; McCammon, J.A.
Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach
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Mus musculus
brenda
Boyd, A.E.; Marnett, A.B.; Wong, L.; Taylor, P.
Probing the active center gorge of acetylcholinesterase by fluorophores linked to substituted cysteines
J. Biol. Chem.
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2000
Mus musculus
brenda
Shi, J.; Boyd, A.E.; Radic, Z.; Taylor, P.
Reversibly bound and covalently attached ligands induce conformational changes in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase
J. Biol. Chem.
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2001
Mus musculus
brenda
Shi, J.; Tai, K.; McCammon, J.A.; Taylor, P.; Johnson, D.A.
Nanosecond dynamics of the mouse acetylcholinesterase Cys69-Cys96 omega loop
J. Biol. Chem.
278
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2003
Mus musculus (P21836), Mus musculus
brenda
Kardos, S.A.; Sultatos, L.G.
Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase
Toxicol. Sci.
58
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2000
Mus musculus
brenda
Kovarik, Z.; Ciban, N.; Radic, Z.; Simeon-Rudolf, V.; Taylor, P.
Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP
Biochem. Biophys. Res. Commun.
342
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2006
Mus musculus
brenda
Ekstrom, F.; Akfur, C.; Tunemalm, A.K.; Lundberg, S.
Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase
Biochemistry
45
74-81
2006
Mus musculus (P21836), Mus musculus
brenda
Kim, H.K.; Kim, M.; Kim, S.; Kim, M; Chung, J.H.
Effects of green tea polyphenol on cognitive and acetylcholinesterase activities
Biosci. Biotechnol. Biochem.
68
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2004
Mus musculus
brenda
Cometa, M.F.; Lorenzini, P.; Fortuna, S.; Volpe, M.T.; Meneguz, A.; Palmery, M.
In vitro inhibitory effect of aflatoxin B1 on acetylcholinesterase activity in mouse brain
Toxicology
206
125-135
2005
Mus musculus
brenda
Hoernberg, A.; Tunemalm, A.K.; Ekstroem, F.
Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state
Biochemistry
46
4815-4825
2007
Mus musculus (P21836), Mus musculus
brenda
Bourne, Y.; Radic, Z.; Sulzenbacher, G.; Kim, E.; Taylor, P.; Marchot, P.
Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding
J. Biol. Chem.
281
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2006
Mus musculus (P21836), Mus musculus
brenda
Ko, S.O.; Kim, T.H.; Lee, H.K.; Lee, J.C.; Cho, E.S.
Temporospatial localization of acetylcholinesterase activity in the dental epithelium during mouse tooth development
Life Sci.
81
1235-1240
2007
Mus musculus
brenda
Taylor, P.; Kovarik, Z.; Reiner, E.; Radic, Z.
Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure
Toxicology
233
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2007
Mus musculus
brenda
Bosak, A.; Gazic, I.; Vinkovic, V.; Kovarik, Z.
Amino acid residues involved in stereoselective inhibition of cholinesterases with bambuterol
Arch. Biochem. Biophys.
471
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2008
Mus musculus (P21836), Mus musculus
brenda
Agrawal, R.; Tyagi, E.; Shukla, R.; Nath, C.
Effect of insulin and melatonin on acetylcholinesterase activity in the brain of amnesic mice
Behav. Brain Res.
189
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2008
Mus musculus
brenda
Papandreou, M.A.; Dimakopoulou, A.; Linardaki, Z.I.; Cordopatis, P.; Klimis-Zacas, D.; Margarity, M.; Lamari, F.N.
Effect of a polyphenol-rich wild blueberry extract on cognitive performance of mice, brain antioxidant markers and acetylcholinesterase activity
Behav. Brain Res.
198
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2009
Mus musculus
brenda
Pavlov, V.A.; Parrish, W.R.; Rosas-Ballina, M.; Ochani, M.; Puerta, M.; Ochani, K.; Chavan, S.; Al-Abed, Y.; Tracey, K.J.
Brain acetylcholinesterase activity controls systemic cytokine levels through the cholinergic anti-inflammatory pathway
Brain Behav. Immun.
23
41-45
2009
Mus musculus
brenda
Vignaud, A.; Fougerousse, F.; Mouisel, E.; Guerchet, N.; Hourde, C.; Bacou, F.; Butler-Browne, G.S.; Chatonnet, A.; Ferry, A.
Genetic inactivation of acetylcholinesterase causes functional and structural impairment of mouse soleus muscles
Cell Tissue Res.
333
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2008
Mus musculus
brenda
Cheng, Y.H.; Cheng, X.L.; Radi?, Z.; McCammon, J.A.
Acetylcholinesterase: mechanisms of covalent inhibition of H447I mutant determined by computational analyses
Chem. Biol. Interact.
175
196-199
2008
Mus musculus (P21836), Mus musculus
brenda
Jazi, R.; Lalonde, R.; Qian, S.; Strazielle, C.
Regional brain evaluation of acetylcholinesterase activity in PS1/A246E transgenic mice
Neurosci. Res.
63
106-114
2009
Mus musculus
brenda
Hoernberg, A.; Artursson, E.; Waerme, R.; Pang, Y.P.; Ekstroem, F.
Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: reactivation involving flipping of the His447 ring to form a reactive Glu334-His447-oxime triad
Biochem. Pharmacol.
79
507-515
2010
Mus musculus (P21836), Mus musculus
brenda
Guo, L.; Suarez, A.I.; Braden, M.R.; Gerdes, J.M.; Thompson, C.M.
Inhibition of acetylcholinesterase by chromophore-linked fluorophosphonates
Bioorg. Med. Chem. Lett.
20
1194-1197
2010
Electrophorus electricus, Mus musculus
brenda
Bhattacharjee, A.K.; Kuca, K.; Musilek, K.; Gordon, R.K.
In silico pharmacophore model for tabun-inhibited acetylcholinesterase reactivators: a study of their stereoelectronic properties
Chem. Res. Toxicol.
23
26-36
2010
Mus musculus
brenda
Kakinuma, Y.; Furihata, M.; Akiyama, T.; Arikawa, M.; Handa, T.; Katare, R.G.; Sato, T.
Donepezil, an acetylcholinesterase inhibitor against Alzheimers dementia, promotes angiogenesis in an ischemic hindlimb model
J. Mol. Cell. Cardiol.
48
680-693
2010
Homo sapiens, Mus musculus
brenda
Lee, Y.K.; Yuk, D.Y.; Kim, T.I.; Kim, Y.H.; Kim, K.T.; Kim, K.H.; Lee, B.J.; Nam, S.Y.; Hong, J.T.
Protective effect of the ethanol extract of Magnolia officinalis and 4-O-methylhonokiol on scopolamine-induced memory impairment and the inhibition of acetylcholinesterase activity
J. Nat. Med.
63
274-282
2009
Mus musculus
brenda
Artursson, E.; Andersson, P.O.; Akfur, C.; Linusson, A.; Boerjegren, S.; Ekstroem, F.
Catalytic-site conformational equilibrium in nerve-agent adducts of acetylcholinesterase: possible implications for the HI-6 antidote substrate specificity
Biochem. Pharmacol.
85
1389-1397
2013
Homo sapiens, Mus musculus (P21836), Mus musculus
brenda
Hicks, D.A.; Makova, N.Z.; Nalivaeva, N.N.; Turner, A.J.
Characterisation of acetylcholinesterase release from neuronal cells
Chem. Biol. Interact.
203
302-308
2013
Mus musculus
brenda