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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Rattus norvegicus and UniProt Accession P37136
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3.1.1.7 acetylcholinesteraseIUBMB Comments
Acts on a variety of acetic esters; also catalyses transacetylations.
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Word Map
- 3.1.1.7
-
cholinergic
- alzheimer
- nerve
- butyrylcholinesterase
-
organophosphate
-
pesticide
- hippocampus
-
neurotoxicity
- dementia
- erythrocyte
- deficit
-
organophosphorus
-
insecticide
-
muscarinic
- donepezil
- synaptic
-
neuroprotective
- cerebral
- acetyltransferase
- fiber
-
maze
- cortical
-
innervation
-
poison
- cholinesterases
-
nicotinic
-
neurotransmitter
- neuromuscular
- neurodegenerative
- atropine
- axon
- oxime
- carbamate
-
chat
-
histochemistry
-
amyloid
-
morris
-
neurochemical
-
monoamine
- synapses
-
intoxication
- chlorpyrifos
- striatum
-
neurotransmission
-
postsynaptic
- forebrain
- carboxylesterase
-
antidote
-
parasympathetic
- biotechnology
- synthesis
- analysis
- pharmacology
- medicine
- diagnostics
-
anticholinergic
- environmental protection
- drug development
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ache, acetylcholinesterase, acetylcholine esterase, acetyl cholinesterase, hache, eeache, ache1, huache, tcache, membrane-bound acetylcholinesterase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AcCholE
-
-
-
-
acetyl beta-methylcholinesterase
-
-
-
-
acetylcholine esterase
-
-
-
-
acetylcholine hydrolase
-
-
-
-
acetylthiocholinesterase
-
-
-
-
AChE
choline esterase I
-
-
-
-
cholinesterase
-
-
-
-
esterase, acetyl choline
-
-
-
-
true cholinesterase
-
-
-
-
AChE
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
transacetylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylcholine acetylhydrolase
Acts on a variety of acetic esters; also catalyses transacetylations.
CAS REGISTRY NUMBER
COMMENTARY
9000-81-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetylcholine + H2O
?
-
inactivation of transmitter substance operating in cholinergic neurotransmission
-
-
?
acetylcholine + H2O
choline + acetate
-
-
-
-
?
S-acetylthiocholine + H2O
acetate + thiocholine
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
S-acetylthiocholine iodide + H2O
acetate + thiocholine iodide
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
acetylthiocholine + H2O
thiocholine + acetate
activity of AChE is determined by Ellman's method using acetylthiocholine iodide as a substrate
-
-
?
acetylthiocholine + H2O
thiocholine + acetate
-
-
-
-
?
acetylthiocholine iodide + H2O
acetate + thiocholine iodide
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
additional information
?
-
-
AChE is an acetylcholine-hydrolyzing enzyme and is implicated in cognitive functions and probably plays important roles in neurodegenerative disorders, including Alzheimer's disease
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetylcholine + H2O
?
-
inactivation of transmitter substance operating in cholinergic neurotransmission
-
-
?
acetylcholine + H2O
choline + acetate
-
-
-
-
?
additional information
?
-
-
AChE is an acetylcholine-hydrolyzing enzyme and is implicated in cognitive functions and probably plays important roles in neurodegenerative disorders, including Alzheimer's disease
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
compound C547
a fast-binding inhibitor of mixed-type and a very potent and selective reversible inhibitor of AChE, shows a high level of pharmacological selectivity in inhibiting acetylcholinesterase as compared to butyrylcholinesterase (EC 3.1.1.8)
DL-homocysteine thiolactone
inhibits the enzyme in cardiac tissue of male rats
(E)-2-(4-[(diethylamino)methyl]benzylidene)-5,6-dimethoxy-2,3-dihydroinden-1-one
-
i.e. BZYX, an indanone derivative, and a dual-binding-site AChE inhibitor. BZYX also shows high neuroprotection from H2O2-induced apoptosis in PC12 cells and prevents loss of membrane potential, determination with fluorescent 5,5',6,6'-tetrachloro-1,1',3,3'-tetraethylbenzimidazol-carbocyanine iodide, i.e. JC-1, overview
(E)-3-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
-
-
(E)-3-(3-(1-benzylpiperidin-4-yloxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
-
-
(E)-3-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
-
-
(E)-3-(4-(1-benzylpiperidin-4-yloxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
-
-
1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide
-
i.e. BW284c51, complete inhibition
10-N-demethyl-10-N-(10-(4-(piperidin-1-ylmethyl)-phenoxy)decan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(12-(4-(piperidin-1-ylmethyl)-phenoxy)dodecan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(2-(4-(piperidin-1-ylmethyl)phenoxy)ethan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(3-(4-(piperidin-1-ylmethyl)phenoxy)propan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(1-benzylpiperidin-4-yloxy)-butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(3-(1-morpholinoethyl)phenoxy)butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(4-((diethylamino)methyl)-phenoxy)butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(4-(morpholinomethyl)phenoxy)butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(4-(piperidin-1-ylmethyl)phenoxy)butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(4-(4-(pyrrolidine-1-carbonyl)-phenoxy)butan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(5-(4-(piperidin-1-ylmethyl)phenoxy)pentan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(1-benzylpiperidin-4-yloxy)-hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(3-(1-morpholinoethyl)phenoxy)hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(4-((diethylamino)methyl)-phenoxy)hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(4-(morpholinomethyl)phenoxy)hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(4-(piperidin-1-ylmethyl)phenoxy)hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(6-(4-(pyrrolidine-1-carbonyl)-phenoxy)hexan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(8-(4-(piperidin-1-ylmethyl)phenoxy)octan-1-yl)-galanthamine
-
-
10-N-demethyl-10-N-(9-(4-(piperidin-1-ylmethyl)phenoxy)nonan-1-yl)-galanthamine
-
-
2-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
-
-
2-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxychroman-4-one
-
-
2-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
-
-
2-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxychroman-4-one
-
-
2-(4-(3-(diethylamino)propanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
-
displays neuroprotective effect against H2O2-induced cell death
2-(4-(3-(ethyl(methyl)amino)propanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
-
-
2-(4-(4-(ethyl(methyl)amino)butanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
-
-
3-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
-
-
3-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
-
-
4,4-difluoro-8-(propan-2-yl)-N-(2,3,4-trifluorophenyl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
4,4-difluoro-8-(propan-2-yl)-N-propyl-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
4,4-difluoro-N,8-di(propan-2-yl)-1,3,4,5-tetrahydro-2Hpyrido[4,3-b]indole-2-carboxamide
-
-
4,4-difluoro-N-(2-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
4,4-difluoro-N-(3-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
4,4-difluoro-N-(4-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
chitooligosaccharides
-
90-COSs and 50-COSs are prepared from 90% and 50% deacetylated chitosan, cellular AChE activity is decreased with increasing concentration of 90-MMWCOS chitooligosaccharides in PC12 cell lines, the 90-COSs exhibit more potent AChE inhibitory activities compared to 50-COSs, while 90-MMWCOS, 1-5 kDa, in the 90COSs show the highest activity, overview
interferon-beta
-
mechanisms of action of IFN-b is through the inhibition of AChE activity, overview
-
N-(2,4-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2,4-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2,5-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2,6-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2-chlorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2-cyanophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2-methoxyphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(2-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3,4-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3,4-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3,5-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3-chlorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3-ethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(3-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(4-methoxyphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-(4-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-cyclopentyl-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
N-ethyl-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
-
-
pilocarpine
-
pilocarpine induction of status epilepticus leads to enzyme inhibition during seizures in the rat brain, overview
serpentine
-
isolated from aqueous extracts of Catharanthus roseus roots, competitive blockade of muscarinic receptors with high efficiency
Ethidium bromide
-
uncompetitive inhibition at concentrations of 0.00625-0.1 mM in all brain regions except for the cerebellum where the inhibition is of a mixed-type
additional information
DL-homocysteine and DL-homocysteine thiolactone inhibit the activity of enzyme AChE in rat cardiac tissue, but increase the activity of antioxidant enzymes, overview
-
additional information
-
no inhibition by oxotremorine, effects of inhibitors on muscarinic acetylcholine receptors, overview
-
additional information
-
acetylcholinesterase activity remains unaffected by the two drugs simvastatin and atorvastatin, that reduce brain lathosterol and cholesterol synthesis rate but do not reduce cholesterol levels, overview
-
additional information
-
design, synthesis and evaluation of galanthamine derivatives as acetylcholinesterase inhibitors, overview
-
additional information
-
molecular modelling and inhibitor docking, overview. No inhibition by 3-(1-benzylpiperidin-4-yloxy)benzaldehyde, 3-((1-benzylpiperidin-4-yl)methoxy)benzaldehyde, 4-(1-benzylpiperidin-4-yloxy)benzaldehyde, {(E)-3-(3-(1-benzylpiperidin-4-yloxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one, and (E)-3-(3-((1-benzylpiperidin-4-yl)nethoxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
-
additional information
-
no inhibition and blockade of muscarinic receptors by serpentine precursor ajmaline at 0.08 mM, weak by catharanthine at over 0.01 mM, but both compounds inhibit nicotinic receptors in a reversible but non-competitive manner, a more potent nicotinic antagonist is tubocurarine
-
additional information
-
synthesis of difluoropyrido[4,3-b]indoles and evaluation as acetylcholinesterase inhibitors, anti-amnesic effect of synthesized compounds against scopolamine-induced memory loss, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
intraperitoneal administration of 1 mg/kg/day for 14 days, increase in enzyme activity by 53%, no change of total antioxidant status
Cd2+
-
intraperitoneal administration of 1 mg/kg/day for 14 days, increase in enzyme activity by 46% and decrease of total antioxidant status
Guanidinoacetate
-
accumulates in guanidinoacetate methyltransferase deficiency, and increases the enzyme activity in the striatum and affecting memory acquisition, consolidation and retrieval of stepdown inhibitory avoidance task in rats, overview
L-cysteine
-
intraperitoneal administration of 7 mg/kg/day for 14 days, increase in enzyme activity by 185% and increase of total antioxidant status. L-cysteine given before a toxic dose of cadmium results in increase of enzyme activity up to 85%, a total antioxidant status similar to the control values, and survival of the treated animals
Zn2+
-
intraperitoneal administration of 1 mg/kg/day for 14 days, increase in enzyme activity by 18%, no change of total antioxidant status
additional information
-
acetylcholinesterase activity remains unaffected by the two drugs simvastatin and atorvastatin, that reduce brain lathosterol and cholesterol synthesis rate but do not reduce cholesterol levels, overview
-
additional information
-
beta-amyloid peptides Abeta25-35 induce AChE protein expression in PC12 cell lines
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
acetylthiocholine iodide
-
pH 8, 37°C, brain, soluble form, component I
0.05
acetylthiocholine iodide
-
pH 8, 37°C, brain, membrane-bound form, component I
0.063
acetylthiocholine iodide
-
pH 8, 37°C, erythrocyte, membrane-bound form, component I
0.26
acetylthiocholine iodide
-
pH 8, 37°C, erythrocyte, membrane-bound form, component II
0.3
acetylthiocholine iodide
-
pH 8, 37°C, brain, soluble form, component II
0.55
acetylthiocholine iodide
-
pH 8, 37°C, brain, membrane-bound form, component II
1.535
acetylthiocholine iodide
-
pH 8, 37°C, erythrocyte, membrane-bound form, component III
additional information
additional information
Michaelis-Menten kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
tissue-dependent inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000058
(E)-2-(4-[(diethylamino)methyl]benzylidene)-5,6-dimethoxy-2,3-dihydroinden-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0242
(E)-3-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0204
(E)-3-(4-(1-benzylpiperidin-4-yloxy)phenyl)-1-(2-hydroxy-4,5-dimethoxyphenyl)prop-2-en-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000612
10-N-demethyl-10-N-(10-(4-(piperidin-1-ylmethyl)-phenoxy)decan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000581
10-N-demethyl-10-N-(12-(4-(piperidin-1-ylmethyl)-phenoxy)dodecan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000245
10-N-demethyl-10-N-(2-(4-(piperidin-1-ylmethyl)phenoxy)ethan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000018
10-N-demethyl-10-N-(3-(4-(piperidin-1-ylmethyl)phenoxy)propan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000306
10-N-demethyl-10-N-(4-(1-benzylpiperidin-4-yloxy)-butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000941
10-N-demethyl-10-N-(4-(3-(1-morpholinoethyl)phenoxy)butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000146
10-N-demethyl-10-N-(4-(4-((diethylamino)methyl)-phenoxy)butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000991
10-N-demethyl-10-N-(4-(4-(morpholinomethyl)phenoxy)butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000124
10-N-demethyl-10-N-(4-(4-(piperidin-1-ylmethyl)phenoxy)butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000538
10-N-demethyl-10-N-(4-(4-(pyrrolidine-1-carbonyl)-phenoxy)butan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000065
10-N-demethyl-10-N-(5-(4-(piperidin-1-ylmethyl)phenoxy)pentan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000222
10-N-demethyl-10-N-(6-(1-benzylpiperidin-4-yloxy)-hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000154
10-N-demethyl-10-N-(6-(3-(1-morpholinoethyl)phenoxy)hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000089
10-N-demethyl-10-N-(6-(4-((diethylamino)methyl)-phenoxy)hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000113
10-N-demethyl-10-N-(6-(4-(morpholinomethyl)phenoxy)hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000056
10-N-demethyl-10-N-(6-(4-(piperidin-1-ylmethyl)phenoxy)hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.000122
10-N-demethyl-10-N-(6-(4-(pyrrolidine-1-carbonyl)-phenoxy)hexan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000347
10-N-demethyl-10-N-(8-(4-(piperidin-1-ylmethyl)phenoxy)octan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0000881
10-N-demethyl-10-N-(9-(4-(piperidin-1-ylmethyl)phenoxy)nonan-1-yl)-galanthamine
Rattus norvegicus
-
pH 7.4, 37°C
0.0086
2-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0304
2-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxychroman-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0066
2-(3-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0127
2-(3-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxychroman-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00209
2-(3-(2-(diethylamino)ethyl)phenoxy)-5,6-dimethoxyindan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00071
2-(3-(2-(ethyl(methyl)amino)ethyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00237
2-(3-(3-(diethylamino)propanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00028
2-(4(2-(diethylamino)acetyl)phenoxy)-5,6-dimethoxyindan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0137
2-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.011
2-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxychroman-4-one
Rattus norvegicus
-
-
0.0041
2-(4-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0076
2-(4-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxychroman-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000421
2-(4-(2-(diethylamino)ethyl)phenoxy)-5,6-dimethoxyindan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000316
2-(4-(2-(ethyl(methyl)amino)acetyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000516
2-(4-(2-(ethyl(methyl)amino)ethyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000078
2-(4-(3-(diethylamino)propanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000277
2-(4-(3-(diethylamino)propyl)phenoxy)-5,6-dimethoxyindan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000185
2-(4-(3-(ethyl(methyl)amino)propanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000406
2-(4-(4-(diethylamino)butanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000481
2-(4-(4-(diethylamino)butyl)phenoxy)-5,6-dimethoxyindan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000376
2-(4-(4-(ethyl(methyl)amino)butanoyl)phenoxy)-5,6-dimethoxy-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00163
3-(3-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00129
3-(3-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00072
3-(4-((1-benzylpiperidin-4-yl)methoxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000093
3-(4-(1-benzylpiperidin-4-yloxy)phenyl)-6,7-dimethoxy-4H-chromen-4-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000476
4,4-difluoro-8-(propan-2-yl)-N-(2,3,4-trifluorophenyl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000967
4,4-difluoro-8-(propan-2-yl)-N-propyl-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001052
4,4-difluoro-N,8-di(propan-2-yl)-1,3,4,5-tetrahydro-2Hpyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000563
4,4-difluoro-N-(2-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000527
4,4-difluoro-N-(3-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000515
4,4-difluoro-N-(4-fluorophenyl)-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.00155
5,6-dimethoxy-2-(3-(2-(piperidin-1-yl)ethyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00177
5,6-dimethoxy-2-(3-(2-(pyrrolidin-1-yl)ethyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000832
5,6-dimethoxy-2-(3-(3-(pyrrolidin-1-yl)propanoyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000364
5,6-dimethoxy-2-(4-(2-(piperidin-1-yl)acetyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000502
5,6-dimethoxy-2-(4-(2-(piperidin-1-yl)ethyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00024
5,6-dimethoxy-2-(4-(2-(pyrrolidin-1-yl)acetyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000373
5,6-dimethoxy-2-(4-(2-(pyrrolidin-1-yl)ethyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0000173
5,6-dimethoxy-2-(4-(3-(piperidin-1-yl)propanoyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00064
5,6-dimethoxy-2-(4-(3-(piperidin-1-yl)propyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.00000416
5,6-dimethoxy-2-(4-(3-(pyrrolidin-1-yl)propanoyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000209
5,6-dimethoxy-2-(4-(3-(pyrrolidin-1-yl)propyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000529
5,6-dimethoxy-2-(4-(4-(piperidin-1-yl)butanoyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000062
5,6-dimethoxy-2-(4-(4-(pyrrolidin-1-yl)butanoyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.000415
5,6-dimethoxy-2-(4-(4-(pyrrolidin-1-yl)butyl)phenoxy)-indan-1-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0184
7,8-dihydro-[1,3]dioxolo[4,5-g]isoquinoline
Rattus norvegicus
-
pH and temperature not specified in the publication
0.05
isocorydine
Rattus norvegicus
-
IC50 above 0.05 mM, pH and temperature not specified in the publication
0.0000508
N-(2,4-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001686
N-(2,4-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000494
N-(2,5-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000483
N-(2,6-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001739
N-(2-chlorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000653
N-(2-cyanophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000987
N-(2-methoxyphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001039
N-(2-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000499
N-(3,4-difluorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001739
N-(3,4-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001684
N-(3,5-dimethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001682
N-(3-chlorophenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001024
N-(3-ethylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001156
N-(3-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001039
N-(4-methoxyphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001023
N-(4-methylphenyl)-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000991
N-cyclopentyl-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0001014
N-ethyl-4,4-difluoro-8-(propan-2-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indole-2-carboxamide
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0000462
neostigmine
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication
0.0413
tetrahydropalmatine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.05
thalifoline
Rattus norvegicus
-
IC50 above 0.05 mM, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
tissue-dependent activity with and without pilocarpine treatment, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
dependence of the kinetic characteristics of integral membrane enzyme acetylcholinesterase (AChE) and structural and functional state of the membrane on the duration of mild hypothermia, by external cooling to 30°C, microviscosity of erythrocyte membranes is measured, detailed overview. The erythrocyte AChE of a homoiothermic animal is very sensitive to alterations in body temperature. Activity of the enzyme increases essentially immediately after a decrease in body temperature to 30°C and is followed with alterations in its kinetic characteristic
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
114150, 114159, 114160, 114184, 653349, 653994, 654021, 663813, 665849, 666241, 679180, 680122, 682110, 682128, 682902, 693989, 695151, 709296, 729516, 749758
additional information
additional information
acetylcholinesterase (AChE) is located on the outer surfaces of postsynaptic membranes of cholinergic synapses in a synaptic cleft. On the other hand, AChE is expressed in non-cholinergic neurons, located in various sites of brain. AChE can be seen not only in neural and muscular tissues, but in a number of non-excitable tissues free of cholinergic innervation, such as testes, endothelial cells, hemopoetic and osteogenic cells, and various tumors. Besides, it can be found at the outer surface of the erythrocyte membrane
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
AChE is located on the outer surfaces of postsynaptic membranes of cholinergic synapses in a synaptic cleft
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
compound C547 and pyridostigmine bromide show efficiency to reduce muscle weakness symptoms and ability to activate contractions of urinary bladder in a rat model of autoimmune myasthenia gravis (MG). At a dose effectively reducing MG symptoms, C547 does not affect activity of rat urinary bladder, while at equipotent dose, pyridostigmine causes a significant increase in tonus and force of spontaneous contractions of bladder wall. In contrast, almost complete inhibition of butyrylcholinesterase (BChE, EC 3.1.1.8) does not affect either the force of contractions or tonus of EAMG rat bladders in vivo
malfunction
negative effects of acute hyperhomocysteinemia induced by DL-homocysteine or DL-homocysteine thiolactone on serum biochemical parameters, plasma antioxidant enzyme and cardiac acetylcholinesterase activities in the rat
physiological function
acetylcholinesterase (AChE) is a key enzyme of cholinergic neurotransmission. The enzyme is located on the outer surfaces of postsynaptic membranes of cholinergic synapses, and its function is regulation of time profiles of neurotransmitter acetylcholine (ACh) concentration in a synaptic cleft. On the other hand, AChE is expressed in non-cholinergic neurons, located in various sites of brain, where no other markers of cholinergic neurotransmission (acetylcholine transferase, high-affinity choline uptake system, etc.) can be found. Therefore, the enzyme has some neuromodulatory functions not involving its catalytic activity. AChE can be seen not only in neural and muscular tissues, but in a number of non-excitable tissues free of cholinergic innervation, such as testes, endothelial cells, hemopoetic and osteogenic cells, and various tumors. Besides, it can be found at the outer surface of the erythrocyte membrane. A rat erythrocyte contains 700-800 molecules of AChE in form of dimers anchored by phosphatidylinositol in an outer membrane layer. A lot of data point to a vital role of AChE in erythrocyte oxygen transport and in the mobilization of nitrogen oxide metabolism in the erythrocytes. Erythrocyte AChE is hardly needed for regulation of the levels of circulating acetylcholine, as the amount of tissue and circulating cholinesterases is more than sufficient to degrade free acetylcholine
physiological function
both AChE and BChE (EC 3.1.1.8) are involved in cholinergic modulation of rat urinary bladder contractions
additional information
dependence of the kinetic characteristics of integral membrane enzyme acetylcholinesterase (AChE) and structural and functional state of the membrane on the duration of mild hypothermia, by external cooling to 30°C, microviscosity of erythrocyte membranes is measured, detailed overview. The erythrocyte AChE of a homoiothermic animal is very sensitive to alterations in body temperature. Activity of the enzyme increases essentially immediately after a decrease in body temperature to 30°C and is followed with alterations in its kinetic characteristic
additional information
molecular mechanisms of the changes in the thermal stability of erythrocyte AChE, overview. H2O2 can play a regulatory role in the functioning of AChE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACES_RAT
614
0
68196
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
-
membrane-bound enzyme from ethanol- and sucrose-treated rats is more stable at temperatures between 10°C and 50°C than the enzyme from untreated rats
additional information
kinetics of thermal denaturation of acetylcholinesterase of the rat red blood cell membrane during moderate hypothermia, thermostability of acetylcholinesterase of rat erythrocyte membranes in the norm and moderate hypothermia, detailed overview. Kinetics of the thermal denaturation of acetylcholinesterase are nonlinear and correspond to a model that involves two-step denaturation, fast and slow, of the enzyme's native form. The rate constants of the fast phase, k1, are much higher than those of the slow phase, k2, while the energy of the fast phase activation is lower by only 19.4% compared to that of the slow one. Short-term moderate hypothermia increases k1 and decreases the index of relative activity of the intermediate form of acetylcholinesterase (parameter beta), leading to significant lowering of the activation energies of both stages, parameter beta becomes more temperature-dependent. The prolongation of hypothermia up to 3 h mainly contributes to a decrease in k1 and k2 relative to short-term hypothermia and the activation energy of denaturation increases. The structure of acetylcholinesterase is labilized at the initial stages of the development of the hypothermic state and stabilized during prolonged hypothermia. Molecular mechanisms of the changes in the thermal stability of erythrocyte AChE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cerebellum, cerebrum, and hypothalamus, by ammonium sulfate fractionation, gel filtration, and dialysis, to homogeneity
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
analysis of reactivation of enzyme by various oximes after inhibition by sarin. Comparison of human, pig and rat enzyme. Higher affinity of oximes 1,1'-butane-1,4-diylbis(2-((Z)-(hydroxyimino)methyl)pyridinium),i.e. K033, and 4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride, i.e. HI-6, for the intact enzymes than obidoxime and pralidoxime
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
incubation of brain homogenates with galactose, galactose 1-phosphate and/or galactitol at concentrations typical for classical galactosaemia or galactokinase deficiency galactosaemia. Enzyme activity is significantly higher in hypothalamus compared with frontal cortex and hippocampus. Frontal cortex and hippocampus enzyme are significantly inhibited by galactose derivatives, whereas hypothalamus enyme activity remains unaltered
medicine
-
whole-body hypothermia increases the degree of substrate inhibition of enzyme, its maximum rate and its Km-value
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vigny, M.; Gisiger, V.; Massoulie, J.
Nonspecific cholinesterase and acetylcholinesterase in rat tissues: molecular forms, structural and catalytic properties, and significance of the two enzymes
Proc. Natl. Acad. Sci. USA
75
2588-2592
1978
Rattus norvegicus
Tunnicliff, G.; Tsukada, Y.; Barbeau, A.
Some properties of acetylcholinesterase from rat retina
Can. J. Biochem.
54
389-392
1976
Rattus norvegicus
Rakonczay, Z.; Mallol, J.; Schenk, H.; Vincendon, G.; Zanetta, J.P.
Purification and properties of the membrane-bound acetylcholinesterase from adult rat brain
Biochim. Biophys. Acta
657
243-256
1981
Rattus norvegicus
Brodbeck, U.
Multiple molecular forms of acetylcholinesterase and their possible role in the degradation of neurohormones
Colloq. Ges. Biol. Chem. Mosbach
36
22-32
1985
Bos taurus, Gallus gallus, Rattus norvegicus, Torpedo sp.
-
Ott, P.
Membrane acetylcholinesterases: purification, molecular properties and interactions with amphiphilic environments
Biochim. Biophys. Acta
822
375-392
1985
Bos taurus, Gallus gallus, Homo sapiens, Rattus norvegicus, Torpedo sp.
Khandkar, M.A.; Mukherjee, E.; Parmar, D.V.; Katyare, S.S.
Alloxan-diabetes alters kinetic properties of the membrane-bound form, but not of the soluble form, of acetylcholinesterase in rat brain
Biochem. J.
307
647-649
1995
Rattus norvegicus
Boeck, A.T.; Schopfer, L.M.; Lockridge, O.
DNA sequence of butyrylcholinesterase from the rat: expression of the protein and characterization of the properties of rat butyrylcholinesterase
Biochem. Pharmacol.
63
2101-2110
2002
Rattus norvegicus
Ruano, M.J.; Sanchez-Martin, M.M.; Alonso, J.M.; Hueso, P.
Changes of acetylcholinesterase activity in brain areas and liver of sucrose- and ethanol-fed rats
Neurochem. Res.
25
461-470
2000
Rattus norvegicus
Rosenfeld, C.; Kousba, A.; Sultatos, L.G.
Interactions of rat brain acetylcholinesterase with the detergent Triton X-100 and the organophosphate paraoxon
Toxicol. Sci.
63
208-213
2001
Rattus norvegicus
Dave, K.R.; Syal, A.R.; Katyare, S.S.
Tissue cholinesterases. A comparative study of their kinetic properties
Z. Naturforsch. C
55
100-108
2000
Homo sapiens, Rattus norvegicus
Carageorgiou, H.; Tzotzes, V.; Sideris, A.; Zarros, A.; Tsakiris, S.
Cadmium effects on brain acetylcholinesterase activity and antioxidant status of adult rats: modulation by zinc, calcium and L-cysteine co-administration
Basic Clin. Pharmacol. Toxicol.
97
320-324
2005
Rattus norvegicus
Klichkhanov, N.K.; Meilanov, I.S.
Effect of hypothermia on kinetic characteristics of acetylcholine esterase in rat erythrocyte membranes
Bull. Exp. Biol. Med.
138
47-49
2004
Rattus norvegicus
Kuca, K.; Cabal, J.; Kassa, J.
In vitro reactivation of sarin-inhibited brain acetylcholinesterase from different species by various oximes
J. Enzyme Inhib. Med. Chem.
20
227-232
2005
Homo sapiens, Rattus norvegicus, Sus scrofa
Marinou, K.; Tsakiris, S.; Tsopanakis, C.; Schulpis, K.H.; Behrakis, P.
Suckling rat brain regional distribution of acetylcholinesterase activity in galactosaemia in vitro
Metab. Brain Dis.
20
227-236
2005
Rattus norvegicus
Mazzanti, C.M.; Spanevello, R.M.; Obregon, A.; Pereira, L.B.; Streher, C.A.; Ahmed, M.; Mazzanti, A.; Graca, D.L.; Morsch, V.M.; Schetinger, M.R.
Ethidium bromide inhibits rat brain acetylcholinesterase activity in vitro
Chem. Biol. Interact.
162
121-127
2006
Rattus norvegicus
Roy, R.; Chaudhuri, A.N.
Differential acetylcholinesterase activity in rat cerebrum, cerebellum and hypothalamus
Indian J. Exp. Biol.
44
381-386
2006
Rattus norvegicus
Mazzanti, C.M.; Spanevello, R.M.; Pereira, L.B.; Goncalves, J.F.; Kaizer, R.; Correa, M.; Ahmed, M.; Mazzanti, A.; Festugatto, R.; Graca, D.L.; Morsch, V.M.; Schetinger, M.R.
Acetylcholinesterase activity in rats experimentally demyelinated with ethidium bromide and treated with interferon beta
Neurochem. Res.
31
1027-1034
2006
Rattus norvegicus
Freitas, R.M.; Sousa, F.C.; Viana, G.S.; Fonteles, M.M.
Acetylcholinesterase activities in hippocampus, frontal cortex and striatum of Wistar rats after pilocarpine-induced status epilepticus
Neurosci. Lett.
399
76-78
2006
Rattus norvegicus
Kobayashi, H.; Suzuki, T.; Sakamoto, M.; Hashimoto, W.; Kashiwada, K.; Sato, I.; Akahori, F.; Satoh, T.
Brain regional acetylcholinesterase activity and muscarinic acetylcholine receptors in rats after repeated administration of cholinesterase inhibitors and its withdrawal
Toxicol. Appl. Pharmacol.
219
151-161
2007
Rattus norvegicus
Shen, Y.; Sheng, R.; Zhang, J.; He, Q.; Yang, B.; Hu, Y.
2-Phenoxy-indan-1-one derivatives as acetylcholinesterase inhibitors: a study on the importance of modifications at the side chain on the activity
Bioorg. Med. Chem.
16
7646-7653
2008
Rattus norvegicus
Lee, S.H.; Park, J.S.; Kim, S.K.; Ahn, C.B.; Je, J.Y.
Chitooligosaccharides suppress the level of protein expression and acetylcholinesterase activity induced by Abeta25-35 in PC12 cells
Bioorg. Med. Chem. Lett.
19
860-862
2009
Rattus norvegicus
Jia, P.; Sheng, R.; Zhang, J.; Fang, L.; He, Q.; Yang, B.; Hu, Y.
Design, synthesis and evaluation of galanthamine derivatives as acetylcholinesterase inhibitors
Eur. J. Med. Chem.
44
772-784
2008
Rattus norvegicus
Zugno, A.I.; Pereira, L.O.; Mattos, C.; Scherer, E.B.; Netto, C.A.; Wyse, A.T.
Guanidinoacetate administration increases acetylcholinesterase activity in striatum of rats and impairs retention of an inhibitory avoidance task
Metab. Brain Dis.
23
189-198
2008
Rattus norvegicus
Cibickova, L.; Radomir, H.; Stanislav, M.; Norbert, C.; Helena, Z.; Daniel, J.; Alena, T.; Eva, B.; Vladimir, P.
The influence of simvastatin, atorvastatin and high-cholesterol diet on acetylcholinesterase activity, amyloid beta and cholesterol synthesis in rat brain
Steroids
74
13-19
2009
Rattus norvegicus
Zhang, J.; Zhu, D.; Sheng, R.; Wu, H.; Hu, Y.; Wang, F.; Cai, T.; Yang, B.; He, Q.
BZYX, a novel acetylcholinesterase inhibitor, significantly improved chemicals-induced learning and memory impairments on rodents and protected PC12 cells from apoptosis induced by hydrogen peroxide
Eur. J. Pharmacol.
613
1-9
2009
Rattus norvegicus
Shen, Y.; Zhang, J.; Sheng, R.; Dong, X.; He, Q.; Yang, B.; Hu, Y.
Synthesis and biological evaluation of novel flavonoid derivatives as dual binding acetylcholinesterase inhibitors
J. Enzyme Inhib. Med. Chem.
24
372-380
2009
Rattus norvegicus
Pereira, D.M.; Ferreres, F.; Oliveira, J.M.; Gaspar, L.; Faria, J.; Valentao, P.; Sottomayor, M.; Andrade, P.B.
Pharmacological effects of Catharanthus roseus root alkaloids in acetylcholinesterase inhibition and cholinergic neurotransmission
Phytomedicine
17
646-652
2009
Electrophorus electricus, Rattus norvegicus
Hung, T.M.; Dang, N.H.; Kim, J.C.; Jang, H.S.; Ryoo, S.W.; Lee, J.H.; Choi, J.S.; Bae, K.; Min, B.S.
Alkaloids from roots of Stephania rotunda and their cholinesterase inhibitory activity
Planta Med.
76
1762-1764
2010
Rattus norvegicus
Sergutina, A.V.; Rakhmanova, V.I.
Brain acetylcholinesterase activity in Wistar and August rats with low and high motor activity (a cytochemical study)
Bull. Exp. Biol. Med.
157
450-453
2014
Rattus norvegicus
Worek, F.; Aurbek, N.; Wille, T.; Eyer, P.; Thiermann, H.
Kinetic analysis of interactions of paraoxon and oximes with human, Rhesus monkey, swine, rabbit, rat and guinea pig acetylcholinesterase
Toxicol. Lett.
200
19-23
2011
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Kornjaca, D.; Zivkovic, V.; Krstic, D.; Colovic, M.; Duric, M.; Stankovic, S.; Mutavdzin, S.; Jakovljevic, V.; Duric, D.
The effects of acute hyperhomocysteinemia induced by DL-homocysteine or DL-homocysteine thiolactone on serum biochemical parameters, plasma antioxidant enzyme and cardiac acetylcholinesterase activities in the rat
Arch. Biol. Sci.
70
241-248
2018
Rattus norvegicus (P37136), Rattus norvegicus Wistar (P37136)
-
Madaiah, M.; Jayanna, B.K.; Manu, A.S.; Prashanth, M.K.; Revanasiddappa, H.D.; Veeresh, B.
Synthesis, characterization, and evaluation of difluoropyrido[4,3-b]indoles as potential agents for acetylcholinesterase and antiamnesic activity
Arch. Pharm.
350
e1600303
2017
Rattus norvegicus
Klichkhanov, N.; Dzhafarova, A.; Al-Rabeei, M.
Kinetic characteristics of acetylcholinesterase and structural-functional state of rat erythrocyte membranes at moderate hypothermia
Biochemistry (Moscow) Suppl. Ser. A Membr. Cell Biol.
11
275-286
2017
Rattus norvegicus (P37136), Rattus norvegicus Wistar (P37136)
-
Klichkhanov, N.; Dzhafarova, A.
The kinetics of thermal denaturation of acetylcholinesterase of the rat red blood cell membrane during moderate hypothermia
Biophysics
63
526-536
2018
Rattus norvegicus (P37136), Rattus norvegicus Wistar (P37136)
-
Petrov, K.A.; Kharlamova, A.D.; Lenina, O.A.; Nurtdinov, A.R.; Sitdykova, M.E.; Ilyin, V.I.; Zueva, I.V.; Nikolsky, E.E.
Specific inhibition of acetylcholinesterase as an approach to decrease muscarinic side effects during myasthenia gravis treatment
Sci. Rep.
8
304
2018
Homo sapiens (P22303), Homo sapiens, Rattus norvegicus (P37136)
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