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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.7 acetylcholinesterase
IUBMB Comments
Acts on a variety of acetic esters; also catalyses transacetylations.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ache, acetylcholinesterase, acetylcholine esterase, acetyl cholinesterase, hache, eeache, ache1, huache, tcache, membrane-bound acetylcholinesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AcCholE
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acetyl beta-methylcholinesterase
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acetylcholine esterase
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acetylcholine hydrolase
acetylcholinesterase
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acetylthiocholinesterase
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-
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choline esterase I
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cholinesterase
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esterase, acetyl choline
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membrane-bound acetylcholinesterase
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true cholinesterase
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-
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-
additional information
-
the enzyme belongs to the superfamily of alpha/beta-hydrolase fold proteins
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetylcholine + H2O = choline + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
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transacetylation
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylcholine acetylhydrolase
Acts on a variety of acetic esters; also catalyses transacetylations.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-81-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1-dimethyl-4-acetylthiomethylpiperidinium + H2O
?
show the reaction diagram
i.e. MATP+, paper spray mass spectrometry is used to monitor the activity of acetylcholinesterase, both in-solution and on modified hydrophobic paper surface. Hydrophobic paper surfaces are prepared using vaporized trichloro(3,3,3-trifluoropropyl)silane. In both approaches, mixtures of diluted human whole blood with and without inhibitor ethyl ((2-[bis(propan-2-yl)amino]ethyl)sulfanyl)(methyl)phosphonate (VX) are mixed with a non-endogenous AChE specific substrate, 1,1-dimethyl-4-acetylthiomethylpiperidinium (MATP+). Formation of the cleaved MATP+ product is monitored over time and compared to MATP+ to determine relative AChE activity. This on-substrate assay is effective at determining AChE activity and identifying the toxicant, while determination of AChE activity in-solution proceeds at a slower rate. Method evaluation, overview
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
-
a chromogenic substrate for detection of erythrocyte acetylcholinesterase activity
-
-
?
2,6-dichloro-3'-methylindophenylacetate + H2O
2,6-dichloro-3'-methylindophenol + acetate
show the reaction diagram
-
weak substrate
-
?
2,6-dichlorophenolindophenol acetate + H2O
2,6-dichlorophenolindophenol + acetate
show the reaction diagram
2,6-dichlorophenolindophenol acetate computational molecular docking study using the enzyme's crystal structure, PDB ID 4YE7
-
-
?
2,6-dichlorophenolindophenylacetate + H2O
2,6-dichlorophenolindophenol + acetate
show the reaction diagram
-
-
-
?
2-methoxyacetylthiocholine + H2O
thiocholine + 2-methoxyacetate
show the reaction diagram
-
recombinant enzyme shows about 12% activity compared to acetylthiocholine
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-
?
3',5'-dichloro-2'-methylindophenylacetate + H2O
3',5'-dichloro-2'-methylindophenol + acetate
show the reaction diagram
-
weak substrate
-
?
3',5'-dichlorophenolindophenylacetate + H2O
3',5'-dichlorophenolindophenol + acetate
show the reaction diagram
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weak substrate
-
?
3-(acetamido)-N,N,N-trimethylanilinium + H2O
?
show the reaction diagram
-
slow hydrolysis
-
-
?
3-(acetamido)-N,N,N-trimethylanilinum + H2O
?
show the reaction diagram
-
ATMA
-
?
3-methylbutyrylthiocholine + H2O
thiocholine + 3-methylbutyrate
show the reaction diagram
-
recombinant enzyme shows about 1% activity compared to acetylthiocholine
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-
?
6-monoacetylmorphine + H2O
morphine + acetate
show the reaction diagram
-
-
-
?
acetyl-beta-methylcholine + H2O
methylcholine + acetate
show the reaction diagram
-
-
-
?
acetyl-beta-methylthiocholine + H2O
beta-methylthiocholine + acetate
show the reaction diagram
-
-
-
?
acetyl-homo-thiocholine + H2O
?
show the reaction diagram
-
recombinant enzyme shows less than 10% activity compared to acetylthiocholine
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?
acetylcholine + H2O
acetate + choline
show the reaction diagram
acetylcholine + H2O
choline + acetate
show the reaction diagram
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
acetylthiocholine chloride + H2O
acetate + thiocholine chloride
show the reaction diagram
-
-
-
-
?
acetylthiocholine iodide + H2O
acetate + thiocholine iodide
show the reaction diagram
acetylthiocholine iodide + H2O
thiocholine + acetate
show the reaction diagram
-
-
-
-
?
acetylthiocholine iodide + H2O
thiocholine iodide + acetate
show the reaction diagram
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-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
show the reaction diagram
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?
benzoylthiocholine + H2O
thiocholine + benzoate
show the reaction diagram
-
recombinant enzyme shows about 1% activity compared to acetylthiocholine
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-
?
butyrylthiocholine + H2O
thiocholine + butyrate
show the reaction diagram
carbachol + H2O
?
show the reaction diagram
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slow hydrolysis
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?
cyclopentylcarbonylthiocholine + H2O
thiocholine + cyclopentanecarboxylate
show the reaction diagram
-
recombinant enzyme shows about 4% activity compared to acetylthiocholine
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?
cyclopropylcarbonylthiocholine + H2O
thiocholine + cyclopropanecarboxylate
show the reaction diagram
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recombinant enzyme shows about 4% activity compared to acetylthiocholine
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?
diisopropyl phosphofluoridate + H2O
?
show the reaction diagram
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mutant G117H, no activity with the wild-type enzyme
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?
echothiophate + H2O
?
show the reaction diagram
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mutant G117H, no activity with the wild-type enzyme
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?
heroin + H2O
6-monoacetylmorphine + acetate
show the reaction diagram
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?
hexanoylthiocholine + H2O
thiocholine + hexanoate
show the reaction diagram
-
recombinant enzyme shows about 6% activity compared to acetylthiocholine
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?
indophenylacetate + H2O
indophenol + acetate
show the reaction diagram
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-
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?
isobutyrylthiocholine + H2O
thiocholine + isobutyrate
show the reaction diagram
-
recombinant enzyme shows about 2% activity compared to acetylthiocholine
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?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
show the reaction diagram
-
mutant G117H, no activity with the wild-type enzyme
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?
pentanoylthiocholine + H2O
thiocholine + pentanoate
show the reaction diagram
-
recombinant enzyme shows about 5% activity compared to acetylthiocholine
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?
phenylacetylthiocholine + H2O
thiocholine + phenylacetate
show the reaction diagram
-
recombinant enzyme shows about 7% activity compared to acetylthiocholine
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?
pivaloylthiocholine + H2O
thiocholine + pivalate
show the reaction diagram
-
recombinant enzyme shows about 5% activity compared to acetylthiocholine
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?
propionylthiocholine + H2O
thiocholine + propionate
show the reaction diagram
S-acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
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?
S-acetylthiocholine iodide + H2O
acetate + thiocholine iodide
show the reaction diagram
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
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-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetylcholine + H2O
acetate + choline
show the reaction diagram
acetylcholine + H2O
choline + acetate
show the reaction diagram
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
-
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?
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
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?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
AchE is not affected by Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-haemanthamine
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(+)-tabun
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(-)-huperzine A
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(-)-tabun
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-nitro-N'-[(R)-1-phenylethyl]isophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-[methyl(methylsulfonyl)-amino]-N'-[(R)-1-(4-fluorophenyl)ethyl]isophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-[methyl(methylsulfonyl)amino]-N-[(R)-1-phenylethyl]isophthalamide
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shows inhibitory effects on beta amyloid production of amyloid precursor protein-transfected HEK293 cells and mild protective effect against hydrogen peroxide-induced cell injury
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropyl-5-nitroisophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropyl-5-[methyl(methylsulfonyl)amino]isophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropylisophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-nitroisophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-isophthalamide
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(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-phenylethyl]isophthalamide
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(3,4-dimethoxyphenyl)-(4-([(2-dimethylaminoethyl)-methylamino]methyl)phenyl)-methanone
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(3,4-dimethoxyphenyl)-(4-([(2-methoxybenzyl)methylamino]methyl)phenyl)-methanone
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(3,4-dimethoxyphenyl)-(4-([methyl-(3-methylbenzyl)amino]methyl)phenyl)methanone
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(3,4-dimethoxyphenyl)-(4-([methyl-(3-nitrobenzyl)amino]methyl)phenyl)methanone
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(3,4-dimethoxyphenyl)-(4-morpholin-4-ylmethylphenyl)methanone
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(3,4-dimethoxyphenyl)-(4-[(methylprop-2-ynylamino)-methyl]phenyl)methanone
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(3,4-dimethoxyphenyl)-{4-[(ethylpropylamino)methyl]phenyl}methanone
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(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl (2-methylphenyl)carbamate
-
50% inhibition at 10 nM
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 760 nM
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl ethylcarbamate
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50% inhibition at 94 nM
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl methylcarbamate
-
50% inhibition at 28 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl (2-methylphenyl)carbamate
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50% inhibition at 13 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl (4-isopropylphenyl)carbamate
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50% inhibition at 3860 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl ethylcarbamate
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50% inhibition at 82 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl methylcarbamate
-
50% inhibition at 27 nM
(4-([benzyl-(2-dimethylaminoethyl)amino]methyl)-phenyl)-(3,4-dimethoxyphenyl)methanone
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(4-([benzyl-(2-hydroxyethyl)amino]methyl)phenyl)-(3,4-dimethoxyphenyl)methanone
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(4-bromobenzoyl)phosphoramidic dichloride
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(4-chlorobenzoyl)phosphoramidic dichloride
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(4-methylbenzoyl)phosphoramidic dichloride
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(4-[(benzylethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
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(4-[(benzylmethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
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(4-[(benzylmethylamino)methyl]phenyl)-(3-fluoro-4-methoxyphenyl)methanone
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(4-[(benzylmethylamino)methyl]phenyl)-(4-methoxyphenyl)methanone
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(4-[(benzylmethylamino)methyl]phenyl)naphthalen-2-yl-methanone
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(4-[3-(benzylmethylamino)propenyl]phenyl)-(3,4-dimethoxyphenyl)methanone
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(7R,11R)-huprine 19
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(7S,11S)-huprine W
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(7S,9R)-ar-turmerol
-
a synthetic bisabolane-type sesquiterpenoid derivative
(7S,9R)-dihydro-arturmerol
-
a synthetic bisabolane-type sesquiterpenoid derivative
(7S,9S)-arturmerol
-
a synthetic bisabolane-type sesquiterpenoid derivative
(7S,9S)-dihydro-ar-turmerol
-
a synthetic bisabolane-type sesquiterpenoid derivative
(E)-1-(4-carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)but-2-ene
-
(R)-(+)-fenoxon sulfoxide
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(R)-(+)-fenthion sulfoxide
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(R)-bambuterol monocarbamate
inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(R)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate
i.e. (R)-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(rac) fenoxon sulfoxide
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(rac) fenthion sulfoxide
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(RS)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate
i.e. rac-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(S)-(-)-fenoxon sulfoxide
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(S)-(-)-fenthion sulfoxide
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(S)-ar-curcumene
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a synthetic bisabolane-type sesquiterpenoid derivative
(S)-ar-turmerone
-
sesquiterpenoid, a competitive inhibitor
(S)-bambuterol monocarbamate
inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(S)-dihydro-ar-curcumene
-
a synthetic bisabolane-type sesquiterpenoid derivative
(S)-dihydro-ar-turmerone
-
a sesquiterpenoid, a noncompetitive inhibitor
(S)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate
i.e. (S)-bambuterol, inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(S-(2-diethylamino)isobutyl)methylphosphonothioate
-
i.e. VR, detailed analysis of inhibition kinetics
1,1'-(ethane-1,1-diyldifuran-5,2-diyl)bis(trifluoroethanone)
-
-
1,1'-heptane-1,7-diylbis{2-[(E)-(hydroxyimino)methyl]pyridinium}
-
reversible inhibition, 0.000385 mM reduces the activity to 76%; reversible inhibition, reduces the activity to 89% and 44% at concentrations of 0.0000385 mM and 0.000385 mM, respectively
1,1'-nonane-1,9-diylbis{2-[(E)-(hydroxyimino)methyl]pyridinium}
-
reversible inhibition, enzyme activity is inhibited to 64% and 15% at 0.0000385 mM and 0.000385 mM, respectively
1,3-bis(4-vinylbenzyl)benzylbenzimidazolium
-
1,3-bis(N-propylphthalimide)benzylbenzimidazolium
-
1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide
-
i.e. BW284c51
1,5-bis(4-allyldimethylammoniumphenyl)pentan-3-one dibromide
i.e. BW284c51
1,5-bis(allyldimethylammoniumphenyl)pentan-3-one dibromide
-
-
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(4,6-dimethylpyrimidin-2-yl)-3-(4-methyl-3-nitrophenyl)guanidine
-
-
1-(4-amino-3-chloro-5-iodo-phenyl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(4-amino-3-iodo-phenyl)-3-(1-benzyl-4-piperidyl)propan-1-one
-
1-(4-amino-3-iodo-phenyl)-3-(1-butyl-4-piperidyl)propan-1-one
-
1-(4-amino-3-iodo-phenyl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(4-amino-3-iodo-phenyl)-3-[1-(cyclopentylmethyl)-4-piperidyl]propan-1-one
-
1-(4-amino-5-chloro-2-methoxyphenyl)-3-(1-butyl-4-piperidinyl)-1-propanone
i.e. RS67333
1-(4-amino-5-chloro-3-iodo-2-methoxy-phenyl)-3-(1-benzyl-4-piperidyl)propan-1-one
-
1-(4-amino-5-chloro-3-iodo-2-methoxy-phenyl)-3-[1-(cyclohexylmethyl)-4-piperidyl] propan-1-one
-
1-(4-cyclopentyl-6-methylpyrimidin-2-yl)-3-(2,4-dimethylphenyl)guanidine
-
-
1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium)butane
-
1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium)propane
-
1-(4-vinylbenzyl)-3-(2,3,5,6-tetramethylbenzyl)-imidazolidinium
-
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)-imidazolidinium
-
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
-
1-(4-vinylbenzyl)-3-(2-methylbenzyl)-imidazolidinium
-
1-(4-vinylbenzyl)-3-(2-methylbenzyl)benzimidazolium
-
1-(4-vinylbenzyl)-3-(3-methylbenzyl)-imidazolidinium
-
1-(4-vinylbenzyl)-3-(4-methylbenzyl)-imidazolidinium
-
1-(4-vinylbenzyl)-3-(4-methylbenzyl)benzimidazolium
-
1-(4-vinylbenzyl)-3-benzylbenzimidazolium
-
1-(4-vinylbenzyl)-3-benzylimidazolidinium
-
1-(4-vinylbenzyl)-3-methylbenzimidazolium
-
1-(4-vinylbenzyl)benzimidazole
-
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(hydroxymethyl)-5-methyloctahydro-2H-quinolizinium
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
1-(N-propylphthalimide)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
-
1-(N-propylphthalimide)-3-(3-methylbenzyl)benzimidazolium
-
1-(N-propylphthalimide)-3-(4-methylbenzyl)benzimidazolium
-
1-(N-propylphthalimide)-3-naphthalenemethylbenzimidazolium
-
1-(N-propylphthalimide)benzoimidazole
-
1-benzyl-2-chloro-3-(2,3-dihydro-benzo[1,4]-dioxin-2-ylmethyl)imidazolidine
-
1-butanoyl-3-(2,6-dimethylphenyl)thiourea
-
1-butanoyl-3-(3-methoxyphenyl)thiourea
-
1-butanoyl-3-(4-chlorophenyl)thiourea
-
1-butanoyl-3-benzylthiourea
-
1-dodecyl-1H-pyrrole-2,5-dione
-
-
1-ethyl-2-[(E)-(1-ethylquinolin-2(1H)-ylidene)methyl]quinolinium
-
-
1-ethyl-2-[(Z)-(1-ethyl[1]benzothieno[3,2-d][1,3]thiazol-2(1H)-ylidene)methyl]quinolinium
-
-
1-ethyl-6-methyl-2-[(1-methyl-1,2-dihydro[1]benzofuro[3,2-d][1,3]thiazol-2-yl)methyl]quinolinium
-
-
1-methyl-3-(3-(methylamino)cyclohexyl)pyridinium
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
1-methyl-3-(methylcarbamoyl)-1,4-dihydroquinolin-5-yl dimethylcarbamate
-
-
1-methyl-3-(morpholin-4-ylcarbonyl)-1,4-dihydroquinolin-5-yl dimethylcarbamate
-
-
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl (2-methylphenyl)carbamate
-
50% inhibition at 56 nM
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 4300 nM
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl ethylcarbamate
-
50% inhibition at 830 nM
1-naphthyl phenothiazine carbamate
-
-
1-O-acetyllycorine
-
-
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-[5-[(1E)-1-hydrazinylideneethyl]-2-methoxybenzyl]piperidine
-
-
1-[5-[(1H-benzimidazol-2-ylsulfanyl)methyl]furan-2-yl]-2,2,2-trifluoroethanone
-
-
1-[7-chloro-2-(trimethylsilyl)-1H-inden-5-yl]-3-[1-(cyclohexylmethyl)piperidin-4-yl]propan-1-one
-
1-[7-chloro-4-methoxy-2-(trimethylsilyl)-1H-inden-5-yl]-3-[1-(cyclohexylmethyl)piperidin-4-yl]propan-1-one
-
1-[[(3-acetylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
-
-
1-[[(3-butanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
-
-
1-[[(3-decanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
-
-
1-[[(3-heptanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
-
-
1-[[(3-hexanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
-
-
10-(2,2-dimethylpropanoyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 4.7
10-(chloroacetyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 7.3
10-(cyclobutylcarbonyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 11.6
10-(cyclopropylcarbonyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 1.9
10-(methoxyacetyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 0.8
10-acetyl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 1.1
10-butyryl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 1.9
10-hydroxy-infractopicrin
-
isolated from Cortinarius infractus, inhibits acetylcholinesterase, but does not inhibit butyrylcholinesterase
10-isobutyryl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 2.7
10-O-methylhostasine
-
a benzylphenethylamine alkaloid from Hosta plantaginea
10-propionyl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC3.1.1.7 is 1.8
11-hydroxygalantamine
-
-
2'-ethylphenylgeneserine N-oxide
-
50% inhibition at 125 nM
2,2'-[[(E)-1,2-diphenylethene-1,2-diyl]bis(benzene-4,1-diyloxy)]diethanesulfonate
-
-
2,3,4-trimethylpyrimido[2,1-a]isoquinolin-5-ium
-
-
2,3-dimethoxy-6-methyl-9H-xanthen-9-one
-
-
2,6-dichlorophenolindophenol
causes substrate inhibition at concentrations above 0.25 mM
2-(1-piperidinyl)ethyl phenothiazine carbamate
-
-
2-(1-pyrrolidinyl)ethyl phenothiazine carbamate
-
-
2-(2-methyl-1H-imidazol-1-yl)-1-[2-(trifluoromethyl)-4a,10a-dihydro-10H-phenothiazin-10-yl]ethanone
-
-
2-(3-methylphenyl)-4H-chromen-4-one
-
-
2-(3-[2-bromo-3-(2,3,5,6-tetramethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
-
2-(3-[2-bromo-3-(2,4,6-trimethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
-
2-(3-[2-bromo-3-(2-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
-
2-(3-[2-bromo-3-(3-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
-
2-(3-[2-bromo-3-(4-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
-
2-(4-methylphenyl)-4H-chromen-4-one
-
-
2-(4-morpholino)ethyl phenothiazine carbamate
-
-
2-(6-oxo-7,11-diazatricyclo(7.3.1.0 2,7)tridec-11-yl)ethyl acetate
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
2-(N,N-diethylamino)ethyl phenothiazine carbamate
-
-
2-(N,N-dimethylamino)ethyl phenothiazine carbamate
-
-
2-amino-3-[2-oxo-2-[phenyl(propan-2-yl)amino]ethyl]-1,3-thiazol-3-ium
-
-
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,3,5,6-tetramethylbenzyl)imidazolidine
-
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,4,6-trimethylbenzyl)imidazolidine
-
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2-methylbenzyl)imidazolidine
-
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(3-methylbenzyl)imidazolidine
-
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(4-methylbenzyl)imidazolidine
-
2-chloro-5-methyl-1,3,2-benzodioxaphosphole 2-oxide
-
50% inhibition at 0.48 mM, detailed kinetic analysis
2-chloro-5-methyl-2,3-dihydro-1H-1,3,2-benzodiazaphosphole 2-oxide
-
50% inhibition at 1.54 mM, detailed kinetic analysis
2-chlorophenyl phenothiazine carbamate
-
-
2-methoxyphenyl phenothiazine carbamate
-
-
2-methylphenyl phenothiazine carbamate
-
-
2-naphthyl phenothiazine carbamate
-
-
2-t-butylphenyl phenothiazine carbamate
-
-
2-[(1-[2-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]ethyl]piperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
-
-
2-[(1-[3-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]propyl]piperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
-
-
2-[(2-acetyl-6,6-dimethyl-4-phenyl-5,6-dihydro-2H-1,2-oxazin-3-yl)methyl]-1H-isoindole-1,3(2H)-dione
-
-
2-[(E)-(hydroxyimino)methyl]-1-[[(3-nonanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
-
-
2-[(E)-(hydroxyimino)methyl]-1-[[(3-octanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
-
-
2-[(E)-(hydroxyimino)methyl]-1-[[(3-pentanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
-
-
2-[(E)-(hydroxyimino)methyl]-1-[[(3-propanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
-
-
2-[(E)-(hydroxyimino)methyl]-1-[[(3-undecanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
-
-
2-[3-(3-benzyl-2-bromo-imidazolidin-1-yl)-propyl]isoindole-1,3-dione
-
2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-diethylethanamine
-
-
2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-dimethylethanamine
-
-
2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-diethylethanamine
-
-
2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-dimethylethanamine
-
-
2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]-imidazole
-
-
2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]-imidazole
-
-
2-[5-methyl-3-(trifluoromethyl)-1H-pyrazol-1-yl]-N-[3-nitro-5-(pyridin-3-yloxy)phenyl]acetamide
-
-
2-[[(4S)-6,6-dimethyl-4-phenyl-5,6-dihydro-4H-1,2-oxazin-3-yl]methyl]-1H-isoindole-1,3(2H)-dione
-
-
3,3'-((1,5-dioxopentane-1,5-diyl)bis(iminocyclohexane-3,1-diyl))bis(1-methylpyridinium)
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
-
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-(1-butylpiperidin-4-yl)-1-[2-(trimethylsilyl)-1H-inden-5-yl]propan-1-one
-
3-(1-phenoxypiperidin-4-yl)-1-[2-(trimethylsilyl)-1H-inden-5-yl]propan-1-one
-
3-(3-methylphenyl)-2H-chromen-2-one
-
-
3-(4-methylphenyl)-2H-chromen-2-one
-
-
3-(6-oxo-6-(8-oxooctahydro-2H-2,6-methanopyrido(1,2-a)(1,5)diazocin-3(4H)-yl)hexanoyl)decahydro-8H-1,5-methanopyrido(1,2-a)(1,5)diazocin-8-one
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
3-(dimethylcarbamoyl)-1-methyl-1,4-dihydroquinolin-5-yl dimethylcarbamate
-
-
3-(dimethylcarbamoyl)-5-[(dimethylcarbamoyl)oxy]-1-methylquinolinium
-
-
3-(N,N-diethylamino)propyl phenothiazine carbamate
-
-
3-(N,N-dimethylamino) phenyl phenothiazine carbamate
-
binding by residues F329 and Y332, structure, overview
3-([7-[methyl(3-[[(methylamino)oxy]carbonyl]benzyl)amino]heptyl]oxy)-9H-xanthen-9-one
-
-
3-chlorophenyl phenothiazine carbamate
-
-
3-ethyl-2-[(1E)-2-(phenylamino)but-1-en-1-yl]naphtho[2,3-d][1,3]oxazol-3-ium
-
-
3-ethyl-2-[(E)-(1-ethyl-6-methoxyquinolin-2(1H)-ylidene)methyl]-5-methoxy-1,3-benzothiazol-3-ium
-
-
3-ethyl-2-[(E)-(1-ethyl-6-methylquinolin-2(1H)-ylidene)methyl]-5-hydroxy-1,3-benzothiazol-3-ium
-
-
3-ethyl-2-[(E)-(1-ethylquinolin-2(1H)-ylidene)methyl]-5-iodo-1,3-benzothiazol-3-ium
-
-
3-methoxy-6-methyl-9H-xanthen-9-one
-
-
3-methoxyphenyl phenothiazine carbamate
-
-
3-methyl-2-(4-methylphenyl)-4H-chromen-4-one
-
-
3-methylphenyl phenothiazine carbamate
-
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
-
3-[1-(cyclohexylmethyl)piperidin-4-yl]-1-[2-(trimethylsilyl)-1H-inden-5-yl]propan-1-one
-
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
3-[1-(cyclopentylmethyl)piperidin-4-yl]-1-[2-(trimethylsilyl)-1H-inden-5-yl]propan-1-one
-
3-[10-(benzylmethylamino)decyloxy]xanthen-9-one
-
-
3-[11-(benzylmethylamino)undecyloxy]xanthen-9-one
-
-
3-[12-(benzylmethylamino)dodecyloxy]xanthen-9-one
-
-
3-[3-(benzylmethylamino)propoxy]xanthen-9-one
-
-
3-[3-[(2-methoxybenzyl)methylamino]propoxy]-xanthen-9-one
-
-
3-[4-(benzylmethylamino)butoxy]xanthen-9-one
-
-
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[4-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]butyl]propanamide
-
-
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[5-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]pentyl]propanamide
-
-
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[6-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]hexyl]propanamide
-
-
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[7-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]heptyl]propanamide
-
-
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[8-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]octyl]propanamide
-
-
3-[5-(benzylmethylamino)pentyloxy]xanthen-9-one
-
-
3-[6-(benzylmethylamino)hexyloxy]xanthen-9-one
-
-
3-[7-(benzylmethylamino)-heptyloxy]xanthen-9-one
-
-
3-[7-(benzylmethylamino)heptyloxy]-6-methoxyxanthen-9-one
-
-
3-[7-[(2,3-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
-
-
3-[7-[(2,5-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
-
-
3-[7-[(2-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
-
-
3-[7-[(2-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
-
-
3-[7-[(3-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
-
-
3-[7-[(3-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
-
-
3-[7-[(4-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
-
-
3-[7-[(4-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
-
-
3-[7-[ethyl-(2-methoxybenzyl)amino]heptyloxy]-xanthen-9-one
-
-
3-[7-[methyl-(2,3,4-trimethoxybenzyl)amino]-heptyloxy]xanthen-9-one
-
-
3-[7-[methyl-(2-methylbenzyl)amino]-heptyloxy]-xanthen-9-one
-
-
3-[7-[methyl-(2-nitrobenzyl)amino]heptyloxy]-xanthen-9-one
-
-
3-[8-(benzylmethylamino)octyloxy]xanthen-9-one
-
-
3-[9-(benzylmethylamino)nonyloxy]xanthen-9-one
-
-
3-[omega-(benzylmethylamino)alkoxy]xanthen-9-ones
-
structure-activity relationships, overview
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl (2-methylphenyl)carbamate
-
50% inhibition at 23 nM
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 2650 nM
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl ethylcarbamate
-
50% inhibition at 360 nM
4-(1H-benzimidazol-2-yl)phenol
-
-
4-(5-chloro-1H-benzimidazol-2-yl)phenol
-
-
4-(5-methyl-1H-benzimidazol-2-yl)phenol
-
-
4-amino-3-chloro-5-iodobenzoic acid
-
4-amino-3-iodobenzoic acid
-
4-amino-5-chloro-3-iodo-2-methoxybenzoic acid
-
4-biphenyl phenothiazine carbamate
-
-
4-bromo-N-[di(morpholin-4-yl)phosphoryl]benzamide
-
-
4-carbamoyl-1-(3-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
-
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
-
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
-
4-carbamoyl-1-(4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
-
4-carbamoyl-1-[(2E)-4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)but-2-en-1-yl]pyridinium
-
4-carbamoyl-1-[(2E)-4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)but-2-en-1-yl]pyridinium
-
4-chloro-N-[di(morpholin-4-yl)phosphoryl]benzamide
-
-
4-chlorophenyl phenothiazine carbamate
-
-
4-methoxy-1H-indole-5-carboxylic acid
-
4-methoxyphenyl phenothiazine carbamate
-
-
4-methylphenyl phenothiazine carbamate
-
-
4-t-butylphenyl phenothiazine carbamate
-
-
4-[2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
-
-
4-[2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
-
-
4-[2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
-
-
5(6)-chloro-2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
-
-
5(6)-chloro-2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
-
-
5(6)-methyl-2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
-
-
5(6)-methyl-2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
-
-
5,6-dimethoxy-2-([1-[2-(1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]piperidin-4-yl]methyl)-2,3-dihydro-1H-inden-1-one
-
-
5,6-dimethoxy-2-([1-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]piperidin-4-yl]methyl)-2,3-dihydro-1H-inden-1-one
-
-
5-(4-chlorophenyl)-N-[10-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]decyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
-
5-(4-chlorophenyl)-N-[6-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]hexyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
-
5-(4-chlorophenyl)-N-[7-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]heptyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
-
5-(4-chlorophenyl)-N-[8-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]octyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
-
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
-
5-[(dimethylcarbamoyl)oxy]-1-methyl-3-(methylcarbamoyl)quinolinium
-
-
5-[(dimethylcarbamoyl)oxy]-1-methyl-3-(morpholin-4-ylcarbonyl)quinolinium
-
-
5-[(dimethylcarbamoyl)oxy]-3-(ethoxycarbonyl)-1-methylquinolinium
-
-
5-[(dimethylcarbamoyl)oxy]-3-(methoxycarbonyl)-1-methylquinolinium
-
-
5-[(E)-(dimethylhydrazinylidene)methyl]-1-(4-methoxy-3-nitrobenzyl)-1H-imidazole
-
-
5-[(ethylcarbamoyl)oxy]-3-(methoxycarbonyl)-1-methylquinolinium
-
-
6,7-dimethoxy-2-(3-methylphenyl)-4H-chromen-4-one
-
-
6,7-dimethoxy-3-(3-methylphenyl)-2H-chromen-2-one
-
-
6,7-dimethoxy-3-(4-methylphenyl)-2H-chromen-2-one
-
-
6-chloro-N-(2-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]ethyl)-1,2,3,4-tetrahydroacridin-9-amine
-
-
6-chloro-N-(3-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]propyl)-1,2,3,4-tetrahydroacridin-9-amine
-
-
6-chlorotacrine
-
-
6-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
-
-
6-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
-
-
6-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
-
-
6-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
-
-
6-methoxytacrine
-
mixed competitive-uncompetitive inhibition
6-[7-(benzylmethylamino)heptyloxy]-2,3-dimethoxyxanthen-9-one
-
-
7-deoxy-trans-dihydronarciclasine
-
-
7-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
-
-
7-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
-
-
7-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
-
-
7-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
-
-
7-methyloctahydro-2H-quinolizin-1-yl (7-methyloctahydro-2H-quinolizin-1-yl)methyl butanedioate
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
7-[(dimethylcarbamoyl)oxy]-3-(ethoxycarbonyl)-1-methylquinolinium
-
-
8-demethoxy-10-O-methylhostasine
-
a benzylphenethylamine alkaloid from Hosta plantaginea
8-demethoxyhostasine
-
benzylphenethylamine alkaloid from Hosta plantaginea
8-methoxyflindersine
-
an alkaloid isolated from Waltheria brachypetala
9-(3-bromo-5-ethoxy-4-hydroxyphenyl)-3,3,6,6-tetramethyl-3,4,5,6,7,9-hexahydro-1H-xanthene-1,8(2H)-dione
-
-
9-amino-1,2,3,4-tetrahydroacridin-1-ol
-
-
9-aminoacridine
-
-
9-O-demethyl-7-O-methyllycorenine
-
a benzylphenethylamine alkaloid from Hosta plantaginea
acetylthiocholine
acetylthiocholine iodide
-
above 5 mM
AH233683
-
-
Aldicarb
-
-
aldicarb-sulfone
-
-
aldicarb-sulfoxide
-
-
alpha-amyrin
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves as a mixture of alpha- and beta amyrin
amberboin
a sesquiterpene lactone from extract of Volutaria abyssinica, inhibition mechanism
aminocarb
-
-
AP2238
-
-
Aspartame
-
and its metabolites, inhibitory above 2.8 mg per kg body weight
assoanine
-
-
azamethiphos
-
-
bambuterol
-
50% inhibition at 0.03 mM
bendiocarb
-
-
benzoyl phosphoramidic dichloride
-
-
benzoylphosphoramidic dichloride
-
-
beta-amyrin
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves as a mixture of alpha- and beta amyrin
bisnorcymserine
-
50% inhibition at mM
bromchlophos
-
-
butocarboxim
-
-
butoxycarboxim
-
-
butyl carbamate
-
-
butylsarin
-
detailed analysis of inhibition kinetics
butyrylthiocholine
-
BW284c51
calenduladiol
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves. 31.2% inhibition at 0.5 mM
carbanolate
-
-
Carbaryl
-
-
carbofuran
-
-
chlorfenvinphos
-
-
Chloroquine
-
mixed type, 33% inhibition at 0.022 mM, 67% inhibition at 0.193 mM
chlorpyrifos
-
-
chlorpyrifos oxon
choline
-
-
cis-rosmarinic acid
-
from extracts of Melissa officinalis leaves
compound C547
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)
coumaphos-oxon
-
-
Crotoxyphos
-
-
cryptotanshinone
mixed non-competitive inhibitor
cyclopentyl phenothiazine carbamate
-
-
cyclophostin
-
cyclosarin
cymserine
-
inhibition in the nanomolar range
decamethonium
demeton-S-methyl
-
-
diazoxon
-
second order rate constant for inhibition is 420000 per M and min
dichlorvos
-
-
dicrotophos
-
-
diethyltabun
-
detailed analysis of inhibition kinetics
dihydrotanshinone
mixed non-competitive inhibitor
diisopropyl fluorophosphate
inhibition, aging, and reactivation kinetics
diisopropyl phosphorofluoridate
-
-
diisopropylfluorophosphate
dimethyl (2-acetyl-6,6-dimethyl-4-phenyl-5,6-dihydro-2H-1,2-oxazin-3-yl)propanedioate
-
-
dimethyl [(10R)-10-(4-methoxyphenyl)-7-oxa-8-azaspiro[4.5]dec-8-en-9-yl]propanedioate
-
-
dimethyl [(1S,4S,4'R)-4'-phenyl-4'H-spiro[bicyclo[2.1.1]hexane-5,5'-[1,2]oxazin]-3'-yl]propanedioate
-
-
dimethyl [(4R)-4,6,6-trimethyl-5,6-dihydro-4H-1,2-oxazin-3-yl]propanedioate
-
-
dimethyl [(4S)-4-(4-methoxyphenyl)-6,6-dimethyl-5,6-dihydro-4H-1,2-oxazin-3-yl]propanedioate
-
-
dimethyl [(9R)-9-phenyl-6-oxa-7-azaspiro[3.5]non-7-en-8-yl]propanedioate
-
-
dimethyl [2-acetyl-4-(4-chlorophenyl)-6,6-dimethyl-5,6-dihydro-2H-1,2-oxazin-3-yl]propanedioate
-
-
dioxacarb
-
-
disodium calenduladiol disulfate
-
a semisynthetic derivative of calenduladiol, elicits higher AChE inhibition than this with 94.1% inhibition at 0.5 mM
donecopride
synthesized from donepezil and RS67333, shows a double mechanism of action and good bioavailability, docking into the active-site gorge of hAChE. Replacement of the benzene ring of the compound by an indole residue should increase the interaction of the ligand with the peripheral anionic site (PAS), thus resulting in increased inhibition of beta-amyloid aggregation
donepezil
donepizil
-
-
Echothiophate
-
99% inhibition of detergent-soluble enzyme activity at 0.001 mM, does not inhibit the soluble enzyme
edrophonium
epinorgalantamine
-
-
eptastigmine
ethiofencarb
-
-
ethopropazine
ethyl 3-(4-amino-3-chloro-5-iodo-phenyl)-3-oxo-propanoate
-
ethyl 3-(4-amino-3-iodo-phenyl)-3-oxo-propanoate
-
ethyl 3-(4-amino-5-chloro-3-iodo-2-methoxy-phenyl)-3-oxo-propanoate
-
ethyl 3-(4-methoxy-1H-indol-5-yl)-3-oxo-propanoate
-
ethyl 5-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
-
-
ethyl 7-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
-
-
ethyl carbamate
-
-
ethyl N,N-di-isopropylphosphorofluoridate
-
-
ethyl N,N-di-n-propylphosphoamidocyanidate
-
-
ethyl N,N-diethylphosphorofluoridate
-
-
ethyl N-ethylphosphorofluoridate
-
-
ethyl N-methylphosphorofluoridate
-
-
ethyl N-n-propylphosphorofluoridate
-
-
ethyl((2-[bis(propan-2-yl)amino]ethyl)sulfanyl)-(methyl)phosphinate
VX, stereospecific inhibition of the enzyme by VX and subsequent reactivation by HI-6, structural analysis, overview
ethylsarin
famphur-O
-
-
faradiol
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves
fasciculin
-
-
-
fenamiphos
fenobucarb
-
-
fenoxon
-
-
fenthion
-
-
fospirate
-
-
FP-biotin
-
i.e. 10-(fluoroethoxyphosphinyl)-N-(biotinamidopentyl)decanamide, second order rate constant for inhibition is 18000000 per M and min
galantamine
galanthamine
heliantriol B2
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves
heptenophos
-
-
heptylene-bis-tacrine
-
-
hostasine
-
a benzylphenethylamine alkaloid from Hosta plantaginea
huperzine
-
inhibition in the nanomolar range
huperzine A
infractopicrin
-
isolated from Cortinarius infractus, inhibits acetylcholinesterase, but does not inhibit butyrylcholinesterase
iso-butylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
iso-ompa
-
50% inhibition at 0.034 mM
iso-pentylsarin
-
-
isoprocarb
-
-
L-aspartate
-
inhibitory above 2.8 mM
L-phenylalanine
-
inhibitory above 0.14 mM
leptophos
-
lipidiol
a sesquiterpene lactone from extract of Volutaria abyssinica, inhibition mechanism
lupeol
-
a pentacyclic triterpene, isolated the ethanolic extract of Chuquiraga erinacea D. Don. subsp. erinacea leaves
malaoxon
-
-
malathion
-
-
Melissa officinalis leaf extract
-
most of the fractions show inhibitory activity and are more potent than the extract due to antagonistic and synergistic effects between various constituents within the plant extract, mass spectrometric analysis of the inhibitory extract fractions, overview
-
metamidophos
-
easy reactivation by oximes
methamidophos
methanol
-
inhibitory above 0.14 mM
methiocarb
-
-
methomyl
-
-
methotrexate
-
-
methyl 4-amino-5-chloro-3-iodo-2-methoxybenzoate
-
methyl 4-methoxy-1H-indole-5-carboxylate
-
methyl 5-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
-
-
methyl 5-[(ethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
-
-
methyl 7-chloro-4-methoxy-1H-indole-5-carboxylate
-
methyl [(10R)-10-phenyl-7-oxa-8-azaspiro[4.5]dec-8-en-9-yl]acetate
-
-
methyl [(1S,4S,4'R)-4'-phenyl-4'H-spiro[bicyclo[2.1.1]hexane-5,5'-[1,2]oxazin]-3'-yl]acetate
-
-
methyl [(4S)-4-(4-methoxyphenyl)-6,6-dimethyl-5,6-dihydro-4H-1,2-oxazin-3-yl]acetate
-
-
methylsarin
methylsulfomethylate-O-ethyl-S-2-ethylmercaptoethyl methylthiophosphanate
-
Gd-42, selective inhibitor for acetylcholine esterase
metrifonate
mevinphos
-
-
mexacarbate
-
-
MMB-4
-
-
Monocrotophos
-
-
N'-[(1E)-1-(4-hydroxyphenyl)ethylidene]-2-(2-nitrophenoxy)acetohydrazide
-
-
N,N'-bis(3-pyridin-3-ylcyclohexyl)pentanediamide
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
N,N,N,N',N',N'-hexamethylbutane-1,4-diaminium
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
N,N,N-trimethyl-10-(methylsulfonylthio)decan-1-aminium bromide
-
i.e. AMTS10, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-11-(methylsulfonylthio)undecan-1-aminium bromide
-
i.e. AMTS11, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-12-(methylsulfonylthio)dodecan-1-aminium bromide
-
i.e. AMTS12, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-13-(methylsulfonylthio)tridecan-1-aminium bromide
-
i.e. AMTS13, causes a degree of apparently irreversible of the AChE activity in erythrocytes. AMTS13 at 0.006 mM leads to 43% inhibition after 1 h, 70% after 6 h, and 78% after 16 h
N,N,N-trimethyl-14-(methylsulfonylthio)tetradecan-1-aminium bromide
-
i.e. AMTS14, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-15-(methylsulfonylthio)pentadecan-1-aminium bromide
-
i.e. AMTS15, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-16-(methylsulfonylthio)hexadecan-1-aminium bromide
-
i.e. AMTS16, causes a degree of apparently irreversible of the AChE activity in erythrocytes
N,N,N-trimethyl-7-(methylsulfonylthio)heptan-1-aminium bromide
-
i.e. AMTS7, causes weak and purely reversible inhibition of AChE activity in erythrocytes
N,N,N-trimethyl-8-(methylsulfonylthio)octan-1-aminium bromide
-
i.e. AMTS8, causes weak and purely reversible inhibition of AChE activity in erythrocytes
N,N,N-trimethyl-9-(methylsulfonylthio)nonan-1-aminium bromide
-
i.e. AMTS9, causes weak and purely reversible inhibition of AChE activity in erythrocytes
N,N,N-trimethylmethanaminium
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
N,N-diethyl-2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethanamine
-
-
N,N-dimethyl phosphoramidic acid bis-(4-chlorophenyl) ester
-
binding activity and lipophilicity, overview
N,N-dimethyl phosphoramidic acid bis-(4-methylphenyl) ester
-
binding activity and lipophilicity, overview
N,N-dimethyl phosphoramidic acid bis-phenyl ester
-
binding activity and lipophilicity, overview
N,N-dimethyl-2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethanamine
-
-
N-((4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]carbamoyl-5-hydroxy-2-methyloct-4-yl)-5-[methyl(methylsulfonyl)amino]-N'-[(R)-1-phenyl ethyl]isophthalamide
-
48.7% inhibition at 0.025 mM
N-((4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]carbamoyl-5-hydroxy-2-methyloct-4-yl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]isophthalamide
-
47.5% inhibition at 0.025 mM
N-((4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]ethylcarbamoyl-5-hydroxy-2-methyloctan-4-yl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]isophthalamide
-
23.8% inhibition at 0.025 mM
N-((4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]methylcarbamoyl-5-hydroxy-2-methyloct-4-yl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]isophthalamide
-
45.9% inhibition at 0.025 mM
N-((4S,5S,7R)-2-[7-(4-benzylpiperazin-1-yl)]carbamoyl-5-hydroxy-2-methyloct-4-yl)-5-[methyl(methylsulfonyl)amino]-N'-[(R)-1-phenylethyl]isophthalamide
-
5.2% inhibition at 0.025 mM
N-(1,3-thiazol-5-ylcarbamothioyl)butanamide
-
N-(2-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]ethyl)-1,2,3,4-tetrahydroacridin-9-amine
-
-
N-(3-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]propyl)-1,2,3,4-tetrahydroacridin-9-amine
-
-
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethyl-carbamoyl-3-hydroxy-1-phenylbut-2-yl)-5-[methyl-(methylsulfonyl)amino]-N'-[(R)-1-phenylethyl]isophthalamide
-
-
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethylcarbamoyl-3-hydroxy-1-phenylbut-2-yl)-N',N'-dipropyl-5-nitroisophthalamide
-
-
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethylcarbamoyl-3-hydroxy-1-phenylbut-2-yl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]iso phthalamide
-
-
N-benzoyl N',N'-(tert-butybenzyl) phosphoramidic chloride
-
26% reactivation of enzyme activity by pralidoxime, 4% by obidoxime
N-benzoyl N',N'-(tert-butybenzyl) thiophosphoramidic chloride
-
22% reactivation of enzyme activity by pralidoxime, 3% by obidoxime
n-butylsarin
N-methyl,N-alkyl carbamates
-
AChE inhibition is mainly determined by the size of the N-alkyl substituent and to a lesser extent by the nature of the leaving group, Ki was highest when the alkyl is methyl, hexyl, cyclohexyl, or an aromatic substituent and lowest when it is ethyl, ki depends on a delicate balance between the length of the residue and its degree of freedom of rotation, overview
-
N-methyl-3-pyridin-3-ylcyclohexanamine
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
N-methyl-N-(3-carbamoyloxyphenyl)methyl-amino inhibitor
-
-
N-methylwaltherione
-
an alkaloid isolated from Waltheria brachypetala
n-pentylsarin
-
-
n-propylsarin
N-[(2,3-dichlorophenyl)carbamothioyl]butanamide
-
N-[(2,4,6-trimethylphenyl)carbamothioyl]butanamide
-
N-[(2,4-dichlorophenyl)carbamothioyl]butanamide
-
N-[(2,6-dichloro-4-fluorophenyl)carbamothioyl]butanamide
-
N-[(2-methoxyphenyl)carbamothioyl]butanamide
-
N-[(3-nitrophenyl)carbamothioyl]butanamide
-
N-[(4-methoxyphenyl)carbamothioyl]butanamide
-
N-[(4-methylphenyl)carbamothioyl]butanamide
-
N-[(4-nitrophenyl)carbamothioyl]butanamide
-
N-[2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]-N-isopropylpropan-2-amine
-
-
N-[2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]-N-isopropylpropan-2-amine
-
-
N-[di(morpholin-4-yl)phosphoryl]-4-methylbenzamide
-
-
N-[di(morpholin-4-yl)phosphoryl]benzamide
-
-
neo-pentylsarin
-
-
neostigmine
neostigmine methyl sulfate
-
norsanguinine
-
-
O-ethyl S-(2-(diisopropylamino)ethyl) methylphosphonothioate
-
i.e. VX, detailed analysis of inhibition kinetics
O-ethyl S-2-N,N-diisopropylaminoethyl methylphosphonothiolate
-
reactivation of sarin-inhibited acetylcholinesterase by oximes, 2-PAM, MMB4, HI-6, HLo-7, and ICD-585, overview
O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate
VX
O-ethyl-O-(4-nitrophenyl)-phenylphosphonothioate
-
-
O-ethyl-S-pentyl methylthiophosphonate
-
LG-64
O-ethyl-S-[2-(diisopropylamino)-ethyl]-methylphosphonothioate
O-isobutyl S-2-N,N-diethylaminoethyl methylphosphonothiolate
-
reactivation of sarin-inhibited acetylcholinesterase by oximes, 2-PAM, MMB4, HI-6, HLo-7, and ICD-585, overview
O-pinacolyl methylphosphonofluoridate
i.e. soman
obidoxime
-
-
octahydro-2H-quinolizin-1-yl octahydro-2H-quinolizin-1-ylmethyl butanedioate
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
octahydro-2H-quinolizin-1-ylmethanol
-
pKi-values and comparison with inhibitory effect on horse and Berrytheutis magister butyrylcholinesterase EC 3.1.1.8
omethoate
-
-
organophosphorus compounds
-
determination of reactivation efficiency with oxims, e.g. obixime, 2-PAM, HI 6, HLö 7, and MMB-4, reactivation kinetics, overview, structure-activity relationship for inhibition and spontaneous reactivation, overview
-
oxydemeton methyl
-
-
paraoxon
paraoxon-ethyl
paraoxon-methyl
-
detailed analysis of inhibition kinetics
paraoxonethyl
diethyl-O-4-nitrophenylphosphate, paraoxon, PXE
parathion
-
-
phenothiazine
-
phenserine
phenyl phenothiazine carbamate
-
-
phenylcoumarin
-
-
phenylethylcymserine
-
50% inhibition at 0.03 mM
Phosphamidon
-
-
physostigmine
pirimicarb
-
-
pralidoxime
primaquine
-
mixed type, 33% inhibition at 0.038 mM, 67% inhibition at 0.247 mM
profenofos
-
-
promecarb
-
-
propidium
propidium iodide
-
-
propionylthiocholine
-
propoxur
-
-
propyl phenothiazine carbamate
-
-
pyridostigmine
quinidine
-
-
Quinine
-
mixed type, 33% inhibition at 3.2 mM, 67% inhibition at 7.5 mM
R-DEPP
O,S-diethylphenylphosphonothioate, stereospecific inhibition kinetics and stereospecificity of the chiral nerve agent derivative O,S-diethylphenylphosphonothioate. Chemical modification by DEPP, a measurable amount of the enzyme-phosphonate adduct does not undergo aging
rac-bambuterol monocarbamate
inhibition kinetics of human acetylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
rivastigmine
rosmarinic acid derivative
-
from extracts of Melissa officinalis leaves
-
russian VX
-
-
S-DEPP
O,S-diethylphenylphosphonothioate, stereospecific inhibition kinetics and stereospecificity of the chiral nerve agent derivative O,S-diethylphenylphosphonothioate. Chemical modification by DEPP, a measurable amount of the enzyme-phosphonate adduct does not undergo aging. Pralidoxime, a common rescue agent, affects a modest recovery of eqBChE from treatment with S-DEPP. S-DEPP inhibition is practically irreversible. Kinetic analysis of S-DEPP with cholinesterases
sanguinine
-
-
sarin
sec-pentylsarin
-
-
t-butyl phenothiazine carbamate
-
-
Tabun
tacrine
tert-butyl 4-[3-(4-amino-3-chloro-5-iodo-phenyl)-3-oxopropyl]piperidine-1-carboxylate
-
tert-butyl 4-[3-(4-amino-3-iodo-phenyl)-3-oxo-propyl]piperidine-1-carboxylate
-
tert-butyl 4-[3-(4-amino-5-chloro-3-iodo-2-methoxyphenyl)-3-oxo-propyl]piperidine-1-carboxylate
-
tert-butyl 4-[3-(4-methoxy-1H-indol-5-yl)-3-oxo-propyl]piperidine-1-carboxylate
-
tetra(monoisopropyl)diphosphortetramide
irreversible
tetrachlorvinphos
-
-
tetraethylpyrophosphate
-
-
Tetramethyl ammonium
-
-
thioflavin T
thiomethylcyclosarin
-
thiomethylsarin
-
thiomethylsoman
-
trans-rosmarinic acid
-
from extracts of Melissa officinalis leaves
trimedoxime
-
ungeremine
-
-
VX (nerve agent)
waltherine
-
an alkaloid isolated from Waltheria brachypetala, 51.4% inhibition at 0.1 mg/ml
waltherione-A
-
an alkaloid isolated from Waltheria brachypetala, Waltheria douradinha, Melochia chamaedrys, and Melochia odorata leaves
waltherione-B
-
an alkaloid isolated from Waltheria brachypetala
xanthostigmine
[4-(3,4-dihydro-1H-isoquinolin-2-ylmethyl)phenyl]-(3,4-dimethoxyphenyl)methanone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,1'-(pentane-1,5-diyl)bis(3-(2-(hydroxyimino)acetamido)pyridinium) dibromide
-
-
1,1'-butane-1,4-diylbis(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium)
-
-
1,1'-ethane-1,2-diylbis(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium)
-
-
1,1'-heptane-1,7-diylbis(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium)
-
-
1,1'-propane-1,3-diylbis(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium)
-
-
2-(hydroxyiminomethyl)-1-methylpyridinium chloride
-
-
2-hydroxypyridylamidoxime
-
poisoned AChE reactivator
2-PAM
3-[[(2Z)-2-(hydroxyimino)acetyl]amino]-1-[2-(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium-1-yl)benzyl]pyridinium
-
-
3-[[(2Z)-2-(hydroxyimino)acetyl]amino]-1-[3-(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium-1-yl)benzyl]pyridinium
-
-
3-[[(2Z)-2-(hydroxyimino)acetyl]amino]-1-[4-(3-[[(2Z)-2-(hydroxyimino)acetyl]amino]pyridinium-1-yl)benzyl]pyridinium
-
-
acetylthiocholine
-
substrate activiation below 1 mM is only seen in W86F mutant but not in wild-type or D74G mutant
H2O2
-
1 mM inhibits, 0.001 mM increases activity 2fold
HLo-7
-
i.e. 1-[[[4-(aminocarbonyl)pyridinio]-methoxy]methyl]-2,4-bis-[(hydroxylimino)methyl] pyridinium dimethanesulfonate, an oxime that reactivates nerve-agent-inhibited AChE
ICD-585
-
i.e. 1-(2-hydroxyiminomethyl-1-pyridinium)-1'-(4-carboxy-aminopyridinium)-trimethylene hydrochloride, an oxime that reactivates nerve-agent-inhibited AChE
MMB4
-
i.e. 1,1'-trimethylene bis(4-hydroxyimino methyl) pyridinium dichloride, an oxime that reactivates nerve-agent-inhibited AChE
N,N'-4-xylene-bis-[(2,2'-hydroxyiminomethyl)pyridinium] dibromide
-
most potent reactivator for enzyme inhibited by sarin (45% regeneration at 1 mM within 10 min)
N,N'-4-xylene-bis[(3,3'-hydroxyiminomethyl)-pyridinium] dibromide
-
33% reactivation of enzyme inhibited by sarin at 1 mM within 10 min
obidoxime
pralidoxime
-
poisoned AChE reactivator
presenilin 1
-
i.e. PS1, the transmembrane protein plays a critical role in the gamma-secretase processing of the amyloid precursor protein to generate the beta-amyloid peptide, which accumulates in plaques in the pathogenesis of Alzheimer’s disease. The PS1-A246E pathogenic mutation expressed in transgenic mice leads to decreased AChE activity and alteration of AChE glycosylation, accessibility to its peripheral binding site, and the peripheral binding site, which may reflect a shift in protein conformation and disturbed AChE maturation
-
TMB-4
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
2,6-dichlorophenolindophenol
recombinant enzyme, pH and temperature not specified in the publication
0.047
3-(acetamido)-N,N,N-trimethylanilinum
-
pH 8
0.259
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
0.09
acetyl thiocholine
-
pH 8, 27°C, attachment of polyethylene glycol side chains to lysine residues does not alter the Km value
0.0714 - 0.1215
Acetylcholine
0.025 - 30.64
acetylthiocholine
0.055 - 0.983
acetylthiocholine iodide
0.1785
butyrylthiocholine
-
recombinant enzyme, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
2.17
heroin
recombinant enzyme, pH 7.4, 37°C
0.15 - 0.156
propionylthiocholine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
118
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
6500
acetyl thiocholine
-
pH 8, 27°C, attachment of polyethylene glycol side chains to lysine residues does not alter the Kcat value
7.18
acetylthiocholine
recombinant enzyme, pH 8.0, 22°C
35
heroin
recombinant enzyme, pH 7.4, 37°C
3.72
propionylthiocholine
recombinant enzyme, pH 8.0, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
455.47
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
65.3
acetylthiocholine
recombinant enzyme, pH 8.0, 22°C
16.13
heroin
recombinant enzyme, pH 7.4, 37°C
24.8
propionylthiocholine
recombinant enzyme, pH 8.0, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000032
(-)-huperzine A
pH 8.0, 22°C
0.0012
(R)-(+)-fenoxon sulfoxide
-
pH 7.5, 25°C, recombinant enzyme
0.0043
(rac) fenoxon sulfoxide
-
pH 7.5, 25°C, recombinant enzyme
0.0407
(S)-(-)-fenoxon sulfoxide
-
pH 7.5, 25°C, recombinant enzyme
0.882
(S)-ar-turmerone
-
-
0.0000335
1,3-bis(4-vinylbenzyl)benzylbenzimidazolium
pH 8.0, 37°C
0.0000325
1,3-bis(N-propylphthalimide)benzylbenzimidazolium
pH 8.0, 37°C
0.000008
1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide
-
pH 8, 27°C
0.000003
1,5-bis(4-allyldimethylammoniumphenyl)pentan-3-one dibromide
pH 8.0, 22°C
0.00002342
1-(4-vinylbenzyl)-3-(2,3,5,6-tetramethylbenzyl)-imidazolidinium
pH and temperature not specified in the publication
0.00003322
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)-imidazolidinium
pH and temperature not specified in the publication
0.0000564
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
pH 8.0, 37°C
0.00005205
1-(4-vinylbenzyl)-3-(2-methylbenzyl)-imidazolidinium
pH and temperature not specified in the publication
0.0000726
1-(4-vinylbenzyl)-3-(2-methylbenzyl)benzimidazolium
pH 8.0, 37°C
0.00004665
1-(4-vinylbenzyl)-3-(3-methylbenzyl)-imidazolidinium
pH and temperature not specified in the publication
0.00002478
1-(4-vinylbenzyl)-3-(4-methylbenzyl)-imidazolidinium
pH and temperature not specified in the publication
0.0000508
1-(4-vinylbenzyl)-3-(4-methylbenzyl)benzimidazolium
pH 8.0, 37°C
0.0000461
1-(4-vinylbenzyl)-3-benzylbenzimidazolium
pH 8.0, 37°C
0.00004421
1-(4-vinylbenzyl)-3-benzylimidazolidinium
pH and temperature not specified in the publication
0.0000476
1-(4-vinylbenzyl)-3-methylbenzimidazolium
pH 8.0, 37°C
0.0000672
1-(4-vinylbenzyl)benzimidazole
pH 8.0, 37°C
0.0000763
1-(N-propylphthalimide)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
pH 8.0, 37°C
0.0000289
1-(N-propylphthalimide)-3-(3-methylbenzyl)benzimidazolium
pH 8.0, 37°C
0.0000494
1-(N-propylphthalimide)-3-(4-methylbenzyl)benzimidazolium
pH 8.0, 37°C
0.000019
1-(N-propylphthalimide)-3-naphthalenemethylbenzimidazolium
pH 8.0, 37°C
0.0000416
1-(N-propylphthalimide)benzoimidazole
pH 8.0, 37°C
0.00005008
1-benzyl-2-chloro-3-(2,3-dihydro-benzo[1,4]-dioxin-2-ylmethyl)imidazolidine
pH and temperature not specified in the publication
0.0295
10-(2,2-dimethylpropanoyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0798
10-(chloroacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0556
10-(cyclobutylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0448
10-(cyclopropylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0241
10-(methoxyacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0389
10-acetyl-10H-phenothiazine
-
pH 8.0, 23°C
0.0304
10-butyryl-10H-phenothiazine
-
pH 8.0, 23°C
0.0362
10-isobutyryl-10H-phenothiazine
-
pH 8.0, 23°C
0.0467
10-propionyl-10H-phenothiazine
-
pH 8.0, 23°C
0.00001762
2-(3-[2-bromo-3-(2,3,5,6-tetramethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
pH and temperature not specified in the publication
0.00002774
2-(3-[2-bromo-3-(2,4,6-trimethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
pH and temperature not specified in the publication
0.0000303
2-(3-[2-bromo-3-(2-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
pH and temperature not specified in the publication
0.00002455
2-(3-[2-bromo-3-(3-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
pH and temperature not specified in the publication
0.0000286
2-(3-[2-bromo-3-(4-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
pH and temperature not specified in the publication
0.00003053
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,3,5,6-tetramethylbenzyl)imidazolidine
pH and temperature not specified in the publication
0.00003432
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,4,6-trimethylbenzyl)imidazolidine
pH and temperature not specified in the publication
0.00003233
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2-methylbenzyl)imidazolidine
pH and temperature not specified in the publication
0.00006204
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(3-methylbenzyl)imidazolidine
pH and temperature not specified in the publication
0.00004904
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(4-methylbenzyl)imidazolidine
pH and temperature not specified in the publication
1.2
2-chloro-5-methyl-1,3,2-benzodioxaphosphole 2-oxide
-
25°C, pH 7.8
0.00002419
2-[3-(3-benzyl-2-bromo-imidazolidin-1-yl)-propyl]isoindole-1,3-dione
pH and temperature not specified in the publication
0.042
4-carbamoyl-1-(3-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
pH 7.4, 25°C
0.012
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
pH 7.4, 25°C
0.021
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
pH 7.4, 25°C
0.036
4-carbamoyl-1-(4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
pH 7.4, 25°C
0.022
4-carbamoyl-1-[(2E)-4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)but-2-en-1-yl]pyridinium
pH 7.4, 25°C
0.024
4-carbamoyl-1-[(2E)-4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)but-2-en-1-yl]pyridinium
pH 7.4, 25°C
0.025
asoxime
pH 7.4, 25°C
0.00673
cryptotanshinone
pH and temperature not specified in the publication
0.0022
decamethonium
pH 8.0, 22°C
0.00064
dihydrotanshinone
pH and temperature not specified in the publication
0.00036 - 0.0008
edrophonium
0.0653
ethopropazine
pH 8.0, 22°C
0.8
fasciculin
-
pH 8, 27°C
-
0.0017
fenoxon
-
pH 7.5, 25°C, recombinant enzyme
0.0143
fenthion
-
pH 7.5, 25°C, recombinant enzyme
0.0232
N-benzoyl N',N'-(tert-butybenzyl) phosphoramidic chloride
-
pH 7.4, 25°C
0.0442
N-benzoyl N',N'-(tert-butybenzyl) thiophosphoramidic chloride
-
pH 7.4, 25°C
0.045
O-ethyl-O-(4-nitrophenyl)-phenylphosphonothioate
-
pH 7.4
0.18
pralidoxime
pH 7.4, 25°C
0.00049 - 0.001
propidium
0.15
R-DEPP
pH 8.0, 25°C
0.008
S-DEPP
pH 8.0, 25°C
0.000037 - 0.0001746
tacrine
0.0046
tetra(monoisopropyl)diphosphortetramide
pH 8.0, 22°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.452
(+)-haemanthamine
Homo sapiens
-
-
0.00253
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-nitro-N'-[(R)-1-phenylethyl]isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00135
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-[methyl(methylsulfonyl)-amino]-N'-[(R)-1-(4-fluorophenyl)ethyl]isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00183 - 0.0987
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-5-[methyl(methylsulfonyl)amino]-N-[(R)-1-phenylethyl]isophthalamide
0.00127
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropyl-5-nitroisophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00105
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropyl-5-[methyl(methylsulfonyl)amino]isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00228
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N',N'-dipropylisophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00209
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-nitroisophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.0117
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00306
(1S,2R)-N-(1-benzyl-2-hydroxy-3-(S)-[2-(1-benzylpiperidin-4-yl)ethylamino]-propyl)-N'-[(R)-1-phenylethyl]isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.0024
(3,4-dimethoxyphenyl)-(4-([(2-dimethylaminoethyl)-methylamino]methyl)phenyl)-methanone
Homo sapiens
-
pH 8.0, 37°C
0.0037
(3,4-dimethoxyphenyl)-(4-([(2-methoxybenzyl)methylamino]methyl)phenyl)-methanone
Homo sapiens
-
pH 8.0, 37°C
0.0017
(3,4-dimethoxyphenyl)-(4-([methyl-(3-methylbenzyl)amino]methyl)phenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0043
(3,4-dimethoxyphenyl)-(4-([methyl-(3-nitrobenzyl)amino]methyl)phenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.345
(3,4-dimethoxyphenyl)-(4-morpholin-4-ylmethylphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0368
(3,4-dimethoxyphenyl)-(4-[(ethylpropylamino)methyl]phenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0272
(3,4-dimethoxyphenyl)-(4-[(methylprop-2-ynylamino)-methyl]phenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0086
(4-([benzyl-(2-dimethylaminoethyl)amino]methyl)-phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0014
(4-([benzyl-(2-hydroxyethyl)amino]methyl)phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.385
(4-bromobenzoyl)phosphoramidic dichloride
Homo sapiens
-
pH 7.4, 37°C
0.087
(4-chlorobenzoyl)phosphoramidic dichloride
Homo sapiens
-
pH 7.4, 37°C
4.15
(4-methylbenzoyl)phosphoramidic dichloride
Homo sapiens
-
pH 7.4, 37°C
0.0006
(4-[(benzylethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.00046
(4-[(benzylmethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0016
(4-[(benzylmethylamino)methyl]phenyl)-(3-fluoro-4-methoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0018
(4-[(benzylmethylamino)methyl]phenyl)-(4-methoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0196
(4-[(benzylmethylamino)methyl]phenyl)naphthalen-2-yl-methanone
Homo sapiens
-
pH 8.0, 37°C
0.0021
(4-[3-(benzylmethylamino)propenyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0069
(R)-(+)-fenoxon sulfoxide
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
1
(R)-(+)-fenthion sulfoxide
Homo sapiens
-
above, pH 7.5, 25°C, recombinant enzyme
0.023
(rac) fenoxon sulfoxide
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
1
(rac) fenthion sulfoxide
Homo sapiens
-
above, pH 7.5, 25°C, recombinant enzyme
1
(S)-(+)-fenthion sulfoxide
Homo sapiens
-
above, pH 7.5, 25°C, recombinant enzyme
0.23
(S)-(-)-fenoxon sulfoxide
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
0.1911
(S)-ar-turmerone
Homo sapiens
-
-
0.0815
(S)-dihydro-ar-turmerone
Homo sapiens
-
-
0.000219
1,1'-(ethane-1,1-diyldifuran-5,2-diyl)bis(trifluoroethanone)
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.0000604
1,3-bis(4-vinylbenzyl)benzylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000348
1,3-bis(N-propylphthalimide)benzylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0002606
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.000133
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.01
1-(4,6-dimethylpyrimidin-2-yl)-3-(4-methyl-3-nitrophenyl)guanidine
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.01
1-(4-cyclopentyl-6-methylpyrimidin-2-yl)-3-(2,4-dimethylphenyl)guanidine
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00004422
1-(4-vinylbenzyl)-3-(2,3,5,6-tetramethylbenzyl)-imidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.00004046
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)-imidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.0000755
1-(4-vinylbenzyl)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.00004629
1-(4-vinylbenzyl)-3-(2-methylbenzyl)-imidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.0000832
1-(4-vinylbenzyl)-3-(2-methylbenzyl)benzimidazolium
Homo sapiens
pH 8.0, 37°C
0.00004565
1-(4-vinylbenzyl)-3-(3-methylbenzyl)-imidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.00004249
1-(4-vinylbenzyl)-3-(4-methylbenzyl)-imidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.0000739
1-(4-vinylbenzyl)-3-(4-methylbenzyl)benzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000739
1-(4-vinylbenzyl)-3-benzylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.00005593
1-(4-vinylbenzyl)-3-benzylimidazolidinium
Homo sapiens
pH and temperature not specified in the publication
0.0000454
1-(4-vinylbenzyl)-3-methylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0001178
1-(4-vinylbenzyl)benzimidazole
Homo sapiens
pH 8.0, 37°C
0.0000288
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.0000844
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.0000914
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.0000621
1-(N-propylphthalimide)-3-(2,4,6-trimethylbenzyl)benzylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000318
1-(N-propylphthalimide)-3-(3-methylbenzyl)benzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000688
1-(N-propylphthalimide)-3-(4-methylbenzyl)benzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000561
1-(N-propylphthalimide)-3-naphthalenemethylbenzimidazolium
Homo sapiens
pH 8.0, 37°C
0.0000883
1-(N-propylphthalimide)benzoimidazole
Homo sapiens
pH 8.0, 37°C
0.00004753
1-benzyl-2-chloro-3-(2,3-dihydro-benzo[1,4]-dioxin-2-ylmethyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.00892
1-butanoyl-3-(2,6-dimethylphenyl)thiourea
Homo sapiens
pH 7.7, 37°C
0.0343
1-butanoyl-3-(3-methoxyphenyl)thiourea
Homo sapiens
pH 7.7, 37°C
0.0117
1-butanoyl-3-(4-chlorophenyl)thiourea
Homo sapiens
pH 7.7, 37°C
0.1325
1-butanoyl-3-benzylthiourea
Homo sapiens
pH 7.7, 37°C
0.007716
1-ethyl-2-[(E)-(1-ethylquinolin-2(1H)-ylidene)methyl]quinolinium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.002924
1-ethyl-2-[(Z)-(1-ethyl[1]benzothieno[3,2-d][1,3]thiazol-2(1H)-ylidene)methyl]quinolinium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000897
1-ethyl-6-methyl-2-[(1-methyl-1,2-dihydro[1]benzofuro[3,2-d][1,3]thiazol-2-yl)methyl]quinolinium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
1
1-methyl-3-(methylcarbamoyl)-1,4-dihydroquinolin-5-yl dimethylcarbamate
Homo sapiens
-
above
1
1-methyl-3-(morpholin-4-ylcarbonyl)-1,4-dihydroquinolin-5-yl dimethylcarbamate
Homo sapiens
-
above
0.00096
1-O-acetyllycorine
Homo sapiens
-
-
0.000559
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Homo sapiens
pH 8.0, 25°C
0.01
1-[5-[(1E)-1-hydrazinylideneethyl]-2-methoxybenzyl]piperidine
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000115
1-[5-[(1H-benzimidazol-2-ylsulfanyl)methyl]furan-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.2206
1-[[(3-acetylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.1649
1-[[(3-butanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0087
1-[[(3-decanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0555
1-[[(3-heptanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0828
1-[[(3-hexanoylpyridinium-1-yl)methoxy]methyl]-2-[(E)-(hydroxyimino)methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0127
10-hydroxy-infractopicrin
Homo sapiens
-
-
0.00161
11-hydroxygalantamine
Homo sapiens
-
-
0.01
2,3,4-trimethylpyrimido[2,1-a]isoquinolin-5-ium
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00000156
2,3-dimethoxy-6-methyl-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.01
2-(2-methyl-1H-imidazol-1-yl)-1-[2-(trifluoromethyl)-4a,10a-dihydro-10H-phenothiazin-10-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00000052
2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.00002898
2-(3-[2-bromo-3-(2,3,5,6-tetramethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.00003116
2-(3-[2-bromo-3-(2,4,6-trimethylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.00004394
2-(3-[2-bromo-3-(2-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.00004378
2-(3-[2-bromo-3-(3-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.00004081
2-(3-[2-bromo-3-(4-methylbenzyl)imidazolidin-1-yl]-propyl)-isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.00000073
2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.01
2-amino-3-[2-oxo-2-[phenyl(propan-2-yl)amino]ethyl]-1,3-thiazol-3-ium
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00003451
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,3,5,6-tetramethylbenzyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.0000428
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2,4,6-trimethylbenzyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.00003885
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(2-methylbenzyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.00004901
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(3-methylbenzyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.00005047
2-chloro-1-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-3-(4-methylbenzyl)imidazolidine
Homo sapiens
pH and temperature not specified in the publication
0.00000067
2-[(1-[2-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]ethyl]piperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
Homo sapiens
-
-
0.00000027
2-[(1-[3-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]propyl]piperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
Homo sapiens
-
-
0.0025
2-[(2-acetyl-6,6-dimethyl-4-phenyl-5,6-dihydro-2H-1,2-oxazin-3-yl)methyl]-1H-isoindole-1,3(2H)-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0174
2-[(E)-(hydroxyimino)methyl]-1-[[(3-nonanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0275
2-[(E)-(hydroxyimino)methyl]-1-[[(3-octanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.1486
2-[(E)-(hydroxyimino)methyl]-1-[[(3-pentanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.2406
2-[(E)-(hydroxyimino)methyl]-1-[[(3-propanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.0124
2-[(E)-(hydroxyimino)methyl]-1-[[(3-undecanoylpyridinium-1-yl)methoxy]methyl]pyridinium diiodide
Homo sapiens
-
at pH 7.4 and 37°C
0.00004031
2-[3-(3-benzyl-2-bromo-imidazolidin-1-yl)-propyl]isoindole-1,3-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-diethylethanamine
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 20°C
0.01068
2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-dimethylethanamine
Homo sapiens
-
at pH 8.0 and 20°C
0.00875
2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-diethylethanamine
Homo sapiens
-
at pH 8.0 and 20°C
0.00802
2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]-N,N-dimethylethanamine
Homo sapiens
-
at pH 8.0 and 20°C
0.00103
2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]-imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.00213
2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]-imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.01
2-[5-methyl-3-(trifluoromethyl)-1H-pyrazol-1-yl]-N-[3-nitro-5-(pyridin-3-yloxy)phenyl]acetamide
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.06532
2-[[(4S)-6,6-dimethyl-4-phenyl-5,6-dihydro-4H-1,2-oxazin-3-yl]methyl]-1H-isoindole-1,3(2H)-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0000133
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.0000204
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.000275
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.000716
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.0000036
3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000012
3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
1
3-(dimethylcarbamoyl)-1-methyl-1,4-dihydroquinolin-5-yl dimethylcarbamate
Homo sapiens
-
above
0.000015
3-(dimethylcarbamoyl)-5-[(dimethylcarbamoyl)oxy]-1-methylquinolinium
Homo sapiens
-
-
0.00000032
3-([7-[methyl(3-[[(methylamino)oxy]carbonyl]benzyl)amino]heptyl]oxy)-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.01
3-ethyl-2-[(1E)-2-(phenylamino)but-1-en-1-yl]naphtho[2,3-d][1,3]oxazol-3-ium
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001076
3-ethyl-2-[(E)-(1-ethyl-6-methoxyquinolin-2(1H)-ylidene)methyl]-5-methoxy-1,3-benzothiazol-3-ium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001252
3-ethyl-2-[(E)-(1-ethyl-6-methylquinolin-2(1H)-ylidene)methyl]-5-hydroxy-1,3-benzothiazol-3-ium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001391
3-ethyl-2-[(E)-(1-ethylquinolin-2(1H)-ylidene)methyl]-5-iodo-1,3-benzothiazol-3-ium
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00000085
3-methoxy-6-methyl-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00000176
3-methyl-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000051
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.00004
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.000094
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Homo sapiens
pH 8.0, 25°C
0.388
3-[10-(benzylmethylamino)decyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.626
3-[11-(benzylmethylamino)undecyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.908
3-[12-(benzylmethylamino)dodecyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00268
3-[3-(benzylmethylamino)propoxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0034
3-[3-[(2-methoxybenzyl)methylamino]propoxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00625
3-[4-(benzylmethylamino)butoxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0000166
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[4-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]butyl]propanamide
Homo sapiens
-
-
0.0000096
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[5-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]pentyl]propanamide
Homo sapiens
-
-
0.0000111
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[6-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]hexyl]propanamide
Homo sapiens
-
-
0.0000144
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[7-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]heptyl]propanamide
Homo sapiens
-
-
0.000014
3-[5-(4-chlorophenyl)-3,4-dihydro-2H-pyrano[3,2-c]quinolin-9-yl]-N-[8-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]octyl]propanamide
Homo sapiens
-
-
0.00778
3-[5-(benzylmethylamino)pentyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00289
3-[6-(benzylmethylamino)hexyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00282
3-[7-(benzylmethylamino)-heptyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00784
3-[7-(benzylmethylamino)heptyloxy]-6-methoxyxanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.138
3-[7-[(2,3-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.127
3-[7-[(2,5-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.433
3-[7-[(2-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00218
3-[7-[(2-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.594
3-[7-[(3-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.04
3-[7-[(3-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
1.05
3-[7-[(4-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.36
3-[7-[(4-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.00315
3-[7-[ethyl-(2-methoxybenzyl)amino]heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.155
3-[7-[methyl-(2,3,4-trimethoxybenzyl)amino]-heptyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.565
3-[7-[methyl-(2-methylbenzyl)amino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.413
3-[7-[methyl-(2-nitrobenzyl)amino]heptyloxy]-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0103
3-[8-(benzylmethylamino)octyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.152
3-[9-(benzylmethylamino)nonyloxy]xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.1
4-(1H-benzimidazol-2-yl)phenol
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 20°C
0.1
4-(5-chloro-1H-benzimidazol-2-yl)phenol
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 20°C
0.1
4-(5-methyl-1H-benzimidazol-2-yl)phenol
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 20°C
0.26
4-bromo-N-[di(morpholin-4-yl)phosphoryl]benzamide
Homo sapiens
-
pH 7.4, 37°C
0.057
4-chloro-N-[di(morpholin-4-yl)phosphoryl]benzamide
Homo sapiens
-
pH 7.4, 37°C
0.1
4-[2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 20°C
0.00973
4-[2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
Homo sapiens
-
at pH 8.0 and 20°C
0.01292
4-[2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]morpholine
Homo sapiens
-
at pH 8.0 and 20°C
0.00013
5(6)-chloro-2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.0014
5(6)-chloro-2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.00039
5(6)-methyl-2-[4-[2-(piperidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.0004
5(6)-methyl-2-[4-[2-(pyrrolidin-1-yl)ethoxy]phenyl]-1H-benzo[d]imidazole
Homo sapiens
-
at pH 8.0 and 20°C
0.000004
5,6-dimethoxy-2-([1-[2-(1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]piperidin-4-yl]methyl)-2,3-dihydro-1H-inden-1-one
Homo sapiens
-
-
0.00000088
5,6-dimethoxy-2-([1-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]piperidin-4-yl]methyl)-2,3-dihydro-1H-inden-1-one
Homo sapiens
-
-
0.00005
5-(4-chlorophenyl)-N-[10-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]decyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Homo sapiens
-
-
0.00000192
5-(4-chlorophenyl)-N-[6-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]hexyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Homo sapiens
-
-
0.0000183
5-(4-chlorophenyl)-N-[7-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]heptyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Homo sapiens
-
-
0.0000073
5-(4-chlorophenyl)-N-[8-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]octyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Homo sapiens
-
-
0.0000249
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Homo sapiens
-
-
0.000029
5-[(dimethylcarbamoyl)oxy]-1-methyl-3-(methylcarbamoyl)quinolinium
Homo sapiens
-
-
0.00086
5-[(dimethylcarbamoyl)oxy]-1-methyl-3-(morpholin-4-ylcarbonyl)quinolinium
Homo sapiens
-
-
0.000007
5-[(dimethylcarbamoyl)oxy]-3-(ethoxycarbonyl)-1-methylquinolinium
Homo sapiens
-
-
0.00011
5-[(dimethylcarbamoyl)oxy]-3-(methoxycarbonyl)-1-methylquinolinium
Homo sapiens
-
-
0.01
5-[(E)-(dimethylhydrazinylidene)methyl]-1-(4-methoxy-3-nitrobenzyl)-1H-imidazole
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.006
5-[(ethylcarbamoyl)oxy]-3-(methoxycarbonyl)-1-methylquinolinium
Homo sapiens
-
-
0.00000131
6,7-dimethoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.00000316
6,7-dimethoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000109
6,7-dimethoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000026
6-chloro-N-(2-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]ethyl)-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens
-
-
0.00000106
6-chloro-N-(3-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]propyl)-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens
-
-
0.0000083
6-chlorotacrine
Homo sapiens
-
-
0.00000076
6-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.00000063
6-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000006
6-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.000004
6-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.00232
6-[7-(benzylmethylamino)heptyloxy]-2,3-dimethoxyxanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0018
7-deoxy-trans-dihydronarciclasine
Homo sapiens
-
-
0.00000051
7-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.00000072
7-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.0000027
7-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000056
7-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0005
7-[(dimethylcarbamoyl)oxy]-3-(ethoxycarbonyl)-1-methylquinolinium
Homo sapiens
-
-
0.0023
8-demethoxy-10-O-methylhostasine
Homo sapiens
-
-
0.01
9-(3-bromo-5-ethoxy-4-hydroxyphenyl)-3,3,6,6-tetramethyl-3,4,5,6,7,9-hexahydro-1H-xanthene-1,8(2H)-dione
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001895
9-amino-1,2,3,4-tetrahydroacridin-1-ol
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000342
9-aminoacridine
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000023
AH233683
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001685
Aldicarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
aldicarb-sulfone
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
aldicarb-sulfoxide
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00079
amberboin
Homo sapiens
pH and temperature not specified in the publication
0.01183
aminocarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00387
assoanine
Homo sapiens
-
-
0.004559
azamethiphos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000736
bendiocarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.932
benzoylphosphoramidic dichloride
Homo sapiens
-
pH 7.4, 37°C
0.001928
bromchlophos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
butocarboxim
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
butoxycarboxim
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000075
BW284c51
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000977
carbanolate
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.008185
Carbaryl
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000247
carbofuran
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.01574
chlorfenvinphos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00143
coumaphos-oxon
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.006978
Crotoxyphos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00467
cryptotanshinone
Homo sapiens
pH and temperature not specified in the publication
0.03
demeton-S-methyl
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
dichlorvos
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
dicrotophos
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00089
dihydrotanshinone
Homo sapiens
pH and temperature not specified in the publication
0.012 - 0.01435
dimethyl (2-acetyl-6,6-dimethyl-4-phenyl-5,6-dihydro-2H-1,2-oxazin-3-yl)propanedioate
0.07535
dimethyl [(9R)-9-phenyl-6-oxa-7-azaspiro[3.5]non-7-en-8-yl]propanedioate
Homo sapiens
-
pH and temperature not specified in the publication
0.04676
dimethyl [2-acetyl-4-(4-chlorophenyl)-6,6-dimethyl-5,6-dihydro-2H-1,2-oxazin-3-yl]propanedioate
Homo sapiens
-
pH and temperature not specified in the publication
0.02601
dioxacarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.19
disodium calenduladiol disulfate
Homo sapiens
-
-
0.000016
donecopride
Homo sapiens
pH 8.0, 25°C
0.0000064 - 0.00006
donepezil
0.0000116
donepizil
Homo sapiens
-
-
0.009
epinorgalantamine
Homo sapiens
-
-
0.03
ethiofencarb
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
1
ethyl 5-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
Homo sapiens
-
above
1
ethyl 7-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
Homo sapiens
-
above
0.03
famphur-O
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.007341
fenobucarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.0097
fenoxon
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
0.0807
fenthion
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
0.001521
fospirate
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00107
galantamine
Homo sapiens
-
-
0.002908 - 0.0087
galanthamine
0.03
heptenophos
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000006
heptylene-bis-tacrine
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00004
huperzine A
Homo sapiens
-
pH 7.4, 37°C
0.0097
infractopicrin
Homo sapiens
-
-
0.008646
isoprocarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00052
lipidiol
Homo sapiens
pH and temperature not specified in the publication
0.004212
methiocarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00288
methomyl
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
1
methyl 5-[(dimethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
Homo sapiens
-
above
1
methyl 5-[(ethylcarbamoyl)oxy]-1-methyl-1,4-dihydroquinoline-3-carboxylate
Homo sapiens
-
above
0.03512
methyl [(10R)-10-phenyl-7-oxa-8-azaspiro[4.5]dec-8-en-9-yl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
methyl [(1S,4S,4'R)-4'-phenyl-4'H-spiro[bicyclo[2.1.1]hexane-5,5'-[1,2]oxazin]-3'-yl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.002946
metrifonate
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.004501
mevinphos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.006511
mexacarbate
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
Monocrotophos
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.01
N'-[(1E)-1-(4-hydroxyphenyl)ethylidene]-2-(2-nitrophenoxy)acetohydrazide
Homo sapiens
-
IC50 above 0.01 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.05098
N,N-diethyl-2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethanamine
Homo sapiens
-
at pH 8.0 and 20°C
40.9
N,N-dimethyl phosphoramidic acid bis-(4-chlorophenyl) ester
Homo sapiens
-
-
35.4
N,N-dimethyl phosphoramidic acid bis-(4-methylphenyl) ester
Homo sapiens
-
-
31.3
N,N-dimethyl phosphoramidic acid bis-phenyl ester
Homo sapiens
-
-
0.01234
N,N-dimethyl-2-[4-(5(6)-methyl-1H-benzo[d]imidazol-2-yl)phenoxy]ethanamine
Homo sapiens
-
at pH 8.0 and 20°C
0.0104
N-(1,3-thiazol-5-ylcarbamothioyl)butanamide
Homo sapiens
pH 7.7, 37°C
0.00000513
N-(2-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]ethyl)-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens
-
-
0.00000216
N-(3-[4-[(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl)methyl]piperidin-1-yl]propyl)-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens
-
-
0.00111
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethyl-carbamoyl-3-hydroxy-1-phenylbut-2-yl)-5-[methyl-(methylsulfonyl)amino]-N'-[(R)-1-phenylethyl]isophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00168
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethylcarbamoyl-3-hydroxy-1-phenylbut-2-yl)-N',N'-dipropyl-5-nitroisophthalamide
Homo sapiens
-
pH 8.0, 37°C
0.00139
N-([2S,3(R,S)]-2-[4-(1-benzylpiperidin-4-yl)]ethylcarbamoyl-3-hydroxy-1-phenylbut-2-yl)-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]iso phthalamide
Homo sapiens
-
pH 8.0, 37°C
1.567 - 2.34
N-benzoyl N',N'-(tert-butybenzyl) phosphoramidic chloride
2.986 - 4.64
N-benzoyl N',N'-(tert-butybenzyl) thiophosphoramidic chloride
0.158
N-[(2,3-dichlorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0589
N-[(2,4,6-trimethylphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0427
N-[(2,4-dichlorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0403
N-[(2,6-dichloro-4-fluorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0966
N-[(2-methoxyphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0264
N-[(3-nitrophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0491
N-[(4-methoxyphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0425
N-[(4-methylphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0297
N-[(4-nitrophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.02342
N-[2-[4-(1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]-N-isopropylpropan-2-amine
Homo sapiens
-
at pH 8.0 and 20°C
0.00368
N-[2-[4-(5(6)-chloro-1H-benzo[d]imidazol-2-yl)phenoxy]ethyl]-N-isopropylpropan-2-amine
Homo sapiens
-
at pH 8.0 and 20°C
2.89
N-[di(morpholin-4-yl)phosphoryl]-4-methylbenzamide
Homo sapiens
-
pH 7.4, 37°C
0.62
N-[di(morpholin-4-yl)phosphoryl]benzamide
Homo sapiens
-
pH 7.4, 37°C
0.0000503 - 0.0222
neostigmine
0.00143
norsanguinine
Homo sapiens
-
-
0.03
omethoate
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.031
oxydemeton methyl
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000217
paraoxon
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.03
Phosphamidon
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000061 - 0.0026
physostigmine
0.03
pirimicarb
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.01509
profenofos
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000733
promecarb
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.001132
propidium iodide
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.003562
propoxur
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.000904 - 0.003122
pyridostigmine
0.0001
sanguinine
Homo sapiens
-
-
0.0000118 - 0.00071
tacrine
0.03
tetrachlorvinphos
Homo sapiens
-
IC50 above 0.03 mM, at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.004811
tetraethylpyrophosphate
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00831
thioflavin T
Homo sapiens
-
at 22°C in 10 mM Na2HPO4/NaH2PO4, pH 7.4
0.00035
ungeremine
Homo sapiens
-
-
0.0000003 - 0.0003
xanthostigmine
0.054
[4-(3,4-dihydro-1H-isoquinolin-2-ylmethyl)phenyl]-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
additional information
additional information
Homo sapiens
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0146
-
hemolysate, at pH 7.4 and 37°C
20.4
-
term placenta low salt-solubilizable fraction
200
-
purified recombinant enzyme, activity detection by a simple and specific development reaction with indoxyl acetate as the chromogenic substrate
22.4
-
term placenta detergent-solubilizable fraction
29.6
-
-
3.94
-
term placenta 2000 x g supernatant fraction
38 - 41
-
-
40
-
recombinant enzyme in Pichia pastoris culture supernatant
4572
-
-
9.22
-
after 658fold purification, at pH 7.4 and 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 8.5
-
-
7
-
assay at
7.3
-
assay at
7.4 - 7.6
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
assay at
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
well-differentiated colonic adenocarcinoma cell line
Manually annotated by BRENDA team
-
non-small lung carcinoma
Manually annotated by BRENDA team
-
from patients with cerebral tumor, cerebral haemorrhage, bacterial meningitis and encephalitis, hydrocephalus
Manually annotated by BRENDA team
-
from astrocytoma
Manually annotated by BRENDA team
-
of endothelial vein
Manually annotated by BRENDA team
-
fetal cerebral tissue
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
leukemic cells
Manually annotated by BRENDA team
-
from acute lymphoblastic leukemia patient blood
Manually annotated by BRENDA team
-
non-small lung carcinoma
Manually annotated by BRENDA team
-
multiple molecular forms of the enzyme in different tissue fractions, i.e. the 2000 x g supernatant, the low salt-solubilizable fraction, and the detergent-solubilizable fraction, overview
Manually annotated by BRENDA team
neuroblastoma-derived cell line
Manually annotated by BRENDA team
-
endothelial cell of
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACES_HUMAN
614
0
67796
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
260000
-
gel filtration
60000
-
C-terminally truncated form, SDS-PAGE
70000
-
x * 70000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer or tetramer
AChE can exist in the forms of dimer and tetramer
polymer
-
-
tetramer
-
3 types of tetrameres: 1. ChE-I which contains only butyrylcholinesterase, ChE-II which contains acetyl cholinesterase and butyrylcholinesterase and ChE-III which contains only acetylcholinesterase
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
sialoprotein
-
-
side-chain modification
-
glycoprotein
additional information
glycosylation is required for membrane trafficking. When considered in this regard, the use of Escherichia coli seems to be compatible for recombinant hAChE production
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structure PDB ID 4ey4
purified recombinant His8-tagged enzyme in apoform or ligand-bound structures, sitting drop vapor diffusion, mixing of 16 mg/ml protein in 10 mM HEPES, pH 7.0, and 10 mM NaCl with crystallization solution containing 15-21% PEG 3350 and 0.17-0.21 M potassium nitrate, 22°C, 5-8 days, crystals of ligand (e.g. inhibitors or HI-6) in complex with hAChE are obtained by soaking apo crystals at 22°C in crystallization buffer accompanied by 20-25% ethylene glycol and specific concentrations of each ligand for individually designated periods of time, X-ray diffraction structure determination and analysis at 2.26-2.44 A resolution
wild-type enzyme and E202Q mutant, complexed with fasciculin-II
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C580S
-
-
D74G
-
shows no substrate activation
E202A
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
E202D
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
E202Q
F295A
-
KM-value similar to wild-type
F295A/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295D
-
strong increase in Km-value, strong decrease in kcat-value
F295D/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295I/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295L
-
30% increase in Km-value
F295L/F338A
-
2fold increase in Km-value, strong decrease in kcat-value
F295M
-
KM-value similar to wild-type
F295M/F338A
-
70% increase in Km-value, 75% decrease in kcat-value
F295N/F338A
-
6fold increase in Km-value, strong decrease in kcat-value
F295Q/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295R
-
strong increase in Km-value, strong decrease in kcat-value
F295R/F338A
-
8fold increase in Km-value, strong decrease in kcat-value
F295S/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295T/F338A
-
strong increase in Km-value, strong decrease in kcat-value
F295V/F338A
-
12fold increase in Km-value, strong decrease in kcat-value
F295W/F338A
-
2fold increase in Km-value, strong decrease in kcat-value
F295Y
-
60% decrease in Km-value
F295Y/F338A
-
6fold increase in Km-value, strong decrease in kcat-value
F338A
-
80% increase in Km-value, 50% decrease in kcat-value
G117H
-
site-directed mutagenesis, the mutant enzyme hydrolyzes organophosphorous compounds in contrast to the wild-type enzyme
W68A
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
W68F
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
W86F
-
shows substrate activation at low concentration and substrate inhibition at high concentrations
Y337A
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
Y337F
-
results in significant reduction in binding of extended acetylcholine in the catalytically productive orientation
additional information
acetylcholinesterase is physically adsorbed on to a mesoporous silicon surface, immobilization method, overview. The porous silicon-immobilized enzyme retains 50% of its activity, shows thermal stability up to 90°C, reusability for up to three cycles, pH stability over a broad range of pH 4.0-9.0, and a shelf-life of 44 days, with an optimal hydrolytic response towards acetylthiocholine iodide at variable drug concentrations
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
activity loss below pH 4.0 and above pH 9.0
114133
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% loss of activity, 3 hours, dialysis against deionized water
-
circulatory retention of heterologous AChE in non-human primates is dependent on sialic acid content of the enzyme, AChE without sialic acid residues is rapidly eliminated from the circulation.
-
circulatory retention time of heterologous AChE in non-human primates is dependent on attachment of polyethylene glycol side chains to lysine residues, retention time is increased by attachment of PEG side chains
-
compared to phosphate buffer, the inhibition and reactivation kinetics of human erythrocyte AChE are markedly changed by Tris and in part by MOPS, whereas Tyrode buffer shows similar results to phosphate buffer (0.1 M each)
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally truncated form
-
large scale
-
native enzyme from greenbug aphids
-
partial
-
R-isoform, expressed in Nicotiana benthamiana
-
recombinant C-terminally truncated enzyme AChE from CHO-S cells by affinity chromatography
recombinant enzyme from stably expressing CHO cells by affinity chromatography on a procainamide resin, to homogeneity
-
recombinant enzyme HuAChE from CHO cells by procainamide affinity chromatography
recombinant His8-tagged enzyme from HEK-293-H cells by affinity chromatography and dialysis
recombinant secreted enzyme from Pichia pastoris strain GS115 culture supernatant by anion-exchange and affinity chromatography to about 96% purity
-
recombinant SUMO-His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Sepharose 4B-L-tyrosine-tacrine affinity column chromatography
-
solublization of protein using Triton X-100
-
the protein is purified in mg quantities by adsorption and desorption from an antiFLAG peptide resin
-
W86F and D74G mutant
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally truncated enzyme
-
C-terminally truncated human enzyme (AChE) is genetically fused to the N-terminal of the Fc portion of wild-type human IgG (Fc(WT)) by overlapping extension PCR, cloned and ligated to the pCMV-MCS expression vector and expressed in CHO-S cells
cloned from 18-weeks-old fetal cerebral tissue, expression in Pichia pastoris strain GS115, secretion of the active recombinant AChE at high level
-
expressed in Drosophila S2 cells
-
expressed in HEK-293 cells
-
expression of recombinant enzyme in Escherichia coli
-
gene ACHE, recombinant expression in HEK-293 cells
gene ACHE, recombinant expression of His8-tagged enzyme comprising amino acid sequence 1-574 (preprocessed protein numbering which includes the native secretion signal) in HEK-293-H cells
gene ache, recombinant expression of SUMO-His6-tagged human brain acetylcholinesterase in Escherichia coli strain BL21(DE3), method evaluation, overview
recombinant expression of HuAChE in CHO cells
semiquantitative PCR expression analysis, overview
-
stable expression in CHO cells
-
stable expression of mutant enzyme in CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in erythrocytes from occupational workers exposed to mixture of the pesticides pirimiphosmethyl, chlorpyrifos, temephos and malathion, AChE activity is significantly decreased
-
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 K033 and HI-6 for the intact enzymes than obidoxime and pralidoxime. Markedly low affinity of obidoxime to human enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
drug development
environmental protection
-
pesticide and organophosphate analysis in different soil samples using the enzyme in a photometric assay, overview
medicine
pharmacology
poisoning by organophosphorus compounds (OP) is characterized by inhibition of the key enzyme acetylcholinesterase (AChE) and potentially fatal outcomes in humans. Insufficient efficacy of the standard therapy with atropine and AChE reactivators (oximes) against certain OP initiates synthesis of non-oxime reactivators basing on the common structure 4-amino-2-((diethylamino)methyl)phenol (ADOC). 10 to 34Fold reactivation potency of compound 4-amino-2-[[ethyl(methyl)amino]methyl]phenol compared to 4-amino-2-((diethylamino)methyl)phenol mainly due to improved affinity
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ciliv, G.; Oezand, P.T.
Human erythrocyte acetylcholinesterase; purification, properties and kinetic behavior
Biochim. Biophys. Acta
284
136-156
1972
Homo sapiens
Manually annotated by BRENDA team
Sihotang, K.
Properties of human erythrocyte acetylcholinesterase
J. Biochem.
75
939-941
1974
Homo sapiens
Manually annotated by BRENDA team
Das, P.K.; Hong-Ming Lo, E.; Goedde, H.W.
Heterogeneity and partial purification of human erythrocyte membrane acetylcholinesterase
Hoppe-Seyler's Z. Physiol. Chem.
358
149-157
1977
Homo sapiens
Manually annotated by BRENDA team
Rosenberry, T.L.; Scoggin, D.M.
Structure of human erythrocyte acetylcholinesterase. Characterization of intersubunit disulfide bonding and detergent interaction
J. Biol. Chem.
259
5643-5652
1984
Homo sapiens
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
Ravazzolo, R.; Garr, C.; Bianchi-Scarr , G.; Barresi, R.; Damiani, G.; Capra, V.; Ajmar, F.
Characterization, localization, and biosynthesis of acetylcholinesterase in K562 cells
Arch. Biochem. Biophys.
267
245-251
1988
Homo sapiens
Manually annotated by BRENDA team
Spinedi, A.; Rufini, P.; Luly, P.; Farias, R.
The temperature-dependence of human erythrocyte acetylcholinesterase activity is not affected by membrane cholesterol enrichment
Biochem. J.
255
547-551
1988
Homo sapiens
Manually annotated by BRENDA team
Rogers, A.; Harrison, R.; Jehanli, A.M.T.; Lunt, G.G.
Culture of human spinal cord neurons and neuron-muscle cells in chemically defined media
Biochem. Soc. Trans.
14
1234-1235
1986
Homo sapiens
-
Manually annotated by BRENDA team
Brimijoin, St.; Mintz, K.P.
Human acetylcholinesterase. Immunochemical studies with monoclonal antibodies
Biochim. Biophys. Acta
828
290-297
1985
Homo sapiens
Manually annotated by BRENDA team
Fischer, M.; Ittah, A.; Gorecki, M.; Werber, M.M.
Recombinant human acetylcholinesterase expressed in Escherichia coli: refolding, purification and characterization
Biotechnol. Appl. Biochem.
21
295-311
1995
Homo sapiens
Manually annotated by BRENDA team
Kryger, G.; Harel, M.; Giles, K.; Toker, L.; Velan, B.; Lazar, A.; Kronman, C.; Barak, D.; Ariel, N.; Shafferman, A.; Silman, I.; Sussman, J.L.
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
Acta Crystallogr. Sect. D
D56
1385-1394
2000
Homo sapiens
-
Manually annotated by BRENDA team
Schallreuter, K.U.; Elwary, S.M.A.; Gibbons, N.C.J.; Rokos, H.; Wood, J.M.
Activation/deactivation of acetylcholinesterase by H2O2: more evidence for oxidative stress in vitiligo
Biochem. Biophys. Res. Commun.
315
502-508
2004
Homo sapiens
Manually annotated by BRENDA team
Cohen, O.; Kronman, C.; Chitlaru, T.; Ordentlich, A.; Velan, B.; Shafferman, A.
Effect of chemical modification of recombinant human acetylcholinesterase by polyethylene glycol on its circulatory longevity
Biochem. J.
357
795-802
2001
Homo sapiens
Manually annotated by BRENDA team
Cohen, O.; Kronman, C.; Velan, B.; Shafferman, A.
Amino acid domains control the circulatory residence time of primate acetylcholinesterases in rhesus macaques (Macaca mulatta)
Biochem. J.
378
117-128
2004
Bos taurus, Homo sapiens, Macaca mulatta (Q67BC1), Macaca mulatta (Q67BC2), Macaca mulatta
Manually annotated by BRENDA team
Bar-On, P.; Millard, C.B.; Harel, M.; Dvir, H.; Enz, A.; Sussman, J.L.; Silman, I.
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug Rivastigmine
Biochemistry
41
3555-3564
2002
Drosophila melanogaster, Homo sapiens, Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Johnson, J.L.; Cusack, B.; Davies, M.P.; Fauq, A.; Rosenberry, T.L.
Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
Biochemistry
42
5438-5452
2003
Homo sapiens
Manually annotated by BRENDA team
Kluge, W.H.; Kluge, H.H.; Hochstetter, A.; Vollandt, R.; Seidel, F.; Venbrocks, R.
Acetylcholinesterase in lumbar and ventricular cerebrospinal fluid
Clin. Chim. Acta
305
55-63
2001
Homo sapiens
Manually annotated by BRENDA team
Plageman, L.R.; Pauletti, G.M.; Skau, K.A.
Characterization of acetylcholinesterase in Caco-2 cells
Exp. Biol. Med.
227
480-486
2002
Homo sapiens
Manually annotated by BRENDA team
Rozengart, E.V.; Basova, N.E.; Suvorov, A.A.; Khovanskikh, A.E.
Indophenol chromogenic substrates of cholinesterases of different origin
J. Evol. Biochem. Physiol.
38
16-23
2002
Homo sapiens, Neptunea eulimata
-
Manually annotated by BRENDA team
Zhukovskii, Y.G.
On establishment of individuality of the cholinesterase enzyme in the studied preparation
J. Evol. Biochem. Physiol.
39
281-290
2003
Homo sapiens
-
Manually annotated by BRENDA team
Giacobini, E.
Cholinesterases: New roles in brain function and in Alzheimer's disease
Neurochem. Res.
28
515-522
2003
Homo sapiens
Manually annotated by BRENDA team
Garcia-Ayllon, M.S.; Saez-Valero, J.; Munoz-Delgado, E.; Vidal, C.J.
Identification of hybrid cholinesterase forms consisting of acetyl- and butyrylcholinesterase subunits in human glioma
Neuroscience
107
199-208
2001
Homo sapiens
Manually annotated by BRENDA team
Kua, J.; Zhang, Y.; Eslami, A.C.; Butler, J.R.; McCammon, J.A.
Studying the roles of W86, E202, and Y337 in binding of acetylcholine to acetylcholinesterase using a combined molecular dynamics and multiple docking approach
Protein Sci.
12
2675-2684
2003
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Worek, F.; Thiermann, H.; Szinicz, L.; Eyer, P.
Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes
Biochem. Pharmacol.
68
2237-2248
2004
Homo sapiens
Manually annotated by BRENDA team
Kaplan, D.; Barak, D.; Ordentlich, A.; Kronman, C.; Velan, B.; Shafferman, A.
Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
Biochemistry
43
3129-3136
2004
Homo sapiens
Manually annotated by BRENDA team
Darvesh, S.; McDonald, R.S.; Penwell, A.; Conrad, S.; Darvesh, K.V.; Mataija, D.; Gomez, G.; Caines, A.; Walsh, R.; Martin, E.
Structure-activity relationships for inhibition of human cholinesterases by alkyl amide phenothiazine derivatives
Bioorg. Med. Chem.
13
211-222
2004
Homo sapiens
Manually annotated by BRENDA team
Martinez-Moreno, P.; Nieto-Ceron, S.; Torres-Lanzas, J.; Ruiz-Espejo, F.; Tovar-Zapata, I.; Martinez-Hernandez, P.; Rodriguez-Lopez, J.N.; Vidal, C.J.; Cabezas-Herrera, J.
Cholinesterase activity of human lung tumours varies according to their histological classification
Carcinogenesis
27
429-436
2006
Homo sapiens
Manually annotated by BRENDA team
Geyer, B.C.; Muralidharan, M.; Cherni, I.; Doran, J.; Fletcher, S.P.; Evron, T.; Soreq, H.; Mor, T.S.
Purification of transgenic plant-derived recombinant human acetylcholinesterase-R
Chem. Biol. Interact.
157-158
331-334
2005
Homo sapiens
Manually annotated by BRENDA team
Molochkina, E.M.; Zorina, O.M.; Fatkullina, L.D.; Goloschapov, A.N.; Burlakova, E.B.
H2O2 modifies membrane structure and activity of acetylcholinesterase
Chem. Biol. Interact.
157-158
401-404
2005
Homo sapiens
Manually annotated by BRENDA team
Schopfer, L.M.; Voelker, T.; Bartels, C.F.; Thompson, C.M.; Lockridge, O.
Reaction kinetics of biotinylated organophosphorus toxicant, FP-biotin, with human acetylcholinesterase and human butyrylcholinesterase
Chem. Res. Toxicol.
18
747-754
2005
Homo sapiens
Manually annotated by BRENDA team
Rozengart, E.V.; Basova, N.E.
Elementorganic bisonium reversible inhibitors of different cholinesterases
Dokl. Biochem. Biophys.
395
99-103
2004
Homo sapiens
Manually annotated by BRENDA team
Katewa, S.D.; Katyare, S.S.
Antimalarials inhibit human erythrocyte membrane acetylcholinesterase
Drug Chem. Toxicol.
28
467-482
2005
Homo sapiens
Manually annotated by BRENDA team
Carvalho, F.A.; Graca, L.M.; Martins-Silva, J.; Saldanha, C.
Biochemical characterization of human umbilical vein endothelial cell membrane bound acetylcholinesterase
FEBS J.
272
5584-5594
2005
Homo sapiens
Manually annotated by BRENDA team
Gholivand, K.; Shariatinia, Z.; Ghadimi, S.; Mojahed, F.; Alizadegan, A.M.; Khajeh, K.; Naderi-Manesh, H.
Acetylcholinesterase inhibition by diaza- and dioxophosphole compounds: synthesis and determination of IC50 values
J. Enzyme Inhib. Med. Chem.
19
403-407
2004
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Luo, W.; Yu, Q.s.; Zhan, M.; Parrish, D.; Deschamps, J.R.; Kulkarni, S.S.; Holloway, H.W.; Alley, G.M.; Lahiri, D.K.; Brossi, A.; Greig, N.H.
Novel anticholinesterases based on the molecular skeletons of furobenzofuran and methanobenzodioxepine
J. Med. Chem.
48
986-994
2005
Homo sapiens
Manually annotated by BRENDA team
Tsakiris, S.; Giannoulia-Karantana, A.; Simintzi, I.; Schulpis, K.H.
The effect of aspartame metabolites on human erythrocyte membrane acetylcholinesterase activity
Pharm. Res.
53
1-5
2006
Homo sapiens
Manually annotated by BRENDA team
Rosenfeld, C.A.; Sultatos, L.G.
Concentration-dependent kinetics of acetylcholinesterase inhibition by the organophosphate paraoxon
Toxicol. Sci.
90
460-469
2006
Homo sapiens
Manually annotated by BRENDA team
Ma, X.; Tan, J.; Wei, D.; Zhu, P.; Sun, M.
High-level secretion and purification of recombinant acetylcholinesterase from human cerebral tissue in P. pastoris and identification by chromogenic reaction
Appl. Microbiol. Biotechnol.
72
316-322
2006
Homo sapiens
Manually annotated by BRENDA team
Schallreuter, K.U.; Gibbons, N.C.; Elwary, S.M.; Parkin, S.M.; Wood, J.M.
Calcium-activated butyrylcholinesterase in human skin protects acetylcholinesterase against suicide inhibition by neurotoxic organophosphates
Biochem. Biophys. Res. Commun.
355
1069-1074
2007
Homo sapiens
Manually annotated by BRENDA team
Eckert, S.; Eyer, P.; Mueckter, H.; Worek, F.
Kinetic analysis of the protection afforded by reversible inhibitors against irreversible inhibition of acetylcholinesterase by highly toxic organophosphorus compounds
Biochem. Pharmacol.
72
344-357
2006
Homo sapiens
Manually annotated by BRENDA team
Worek, F.; Aurbek, N.; Koller, M.; Becker, C.; Eyer, P.; Thiermann, H.
Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates
Biochem. Pharmacol.
73
1807-1817
2007
Homo sapiens
Manually annotated by BRENDA team
Eckert, S.; Eyer, P.; Herkert, N.; Bumm, R.; Weber, G.; Thiermann, H.; Worek, F.
Comparison of the oxime-induced reactivation of erythrocyte and muscle acetylcholinesterase following inhibition by sarin or paraoxon, using a perfusion model for the real-time determination of membrane-bound acetylcholinesterase activity
Biochem. Pharmacol.
75
698-703
2008
Homo sapiens
Manually annotated by BRENDA team
Luo, C.; Tong, M.; Chilukuri, N.; Brecht, K.; Maxwell, D.M.; Saxena, A.
An in vitro comparative study on the reactivation of nerve agent-inhibited guinea pig and human acetylcholinesterases by oximes
Biochemistry
46
11771-11779
2007
Cavia porcellus, Homo sapiens
Manually annotated by BRENDA team
Poyot, T.; Nachon, F.; Froment, M.; Loiodice, M.; Wieseler, S.; Schopfer, L.M.; Lockridge, O.; Masson, P.
Mutant of Bungarus fasciatus acetylcholinesterase with low affinity and low hydrolase activity toward organophosphorus esters
Biochim. Biophys. Acta
1764
1470-1478
2006
Bungarus fasciatus, Homo sapiens
Manually annotated by BRENDA team
Piazzi, L.; Belluti, F.; Bisi, A.; Gobbi, S.; Rizzo, S.; Bartolini, M.; Andrisano, V.; Recanatini, M.; Rampa, A.
Cholinesterase inhibitors: SAR and enzyme inhibitory activity of 3-[omega-(benzylmethylamino)alkoxy]xanthen-9-ones
Bioorg. Med. Chem.
15
575-585
2007
Homo sapiens
Manually annotated by BRENDA team
Gadepalli, R.S.; Rimoldi, J.M.; Fronczek, F.R.; Nillos, M.; Gan, J.; Deng, X.; Rodriguez-Fuentes, G.; Schlenk, D.
Synthesis of fenthion sulfoxide and fenoxon sulfoxide enantiomers: effect of sulfur chirality on acetylcholinesterase activity
Chem. Res. Toxicol.
20
257-262
2007
Electrophorus electricus, Homo sapiens
Manually annotated by BRENDA team
Pathak, R.; Kanwar, S.S.; Sanyal, S.N.
Kinetic behaviour of the multiple molecular forms of acetylcholinesterase in the human term placenta
Int. J. Mendel
23
57-58
2006
Homo sapiens
-
Manually annotated by BRENDA team
Gholivand, K.; Mojahed, F.; Salehi, M.; Naderi-Manesh, H.; Khajeh, K.
Synthesis, characterization and inhibitory potency of two oxono and thiono analogues of phosphoramidate compounds on acetylcholinesterase
J. Enzyme Inhib. Med. Chem.
21
521-525
2006
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.H.; Zhang, Z.K.; Yang, F.M.; Sun, Q.Y.; He, H.P.; Di, Y.T.; Mu, S.Z.; Lu, Y.; Chang, Y.; Zheng, Q.T.; Ding, M.; Dong, J.H.; Hao, X.J.
Benzylphenethylamine alkaloids from Hosta plantaginea with inhibitory activity against tobacco mosaic virus and acetylcholinesterase
J. Nat. Prod.
70
1458-1461
2007
Homo sapiens
Manually annotated by BRENDA team
Groner, E.; Ashani, Y.; Schorer-Apelbaum, D.; Sterling, J.; Herzig, Y.; Weinstock, M.
The kinetics of inhibition of human acetylcholinesterase and butyrylcholinesterase by two series of novel carbamates
Mol. Pharmacol.
71
1610-1617
2007
Homo sapiens
Manually annotated by BRENDA team
Bartling, A.; Worek, F.; Szinicz, L.; Thiermann, H.
Enzyme-kinetic investigation of different sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase
Toxicology
233
166-172
2007
Homo sapiens
Manually annotated by BRENDA team
Eckert, S.; Eyer, P.; Worek, F.
Reversible inhibition of acetylcholinesterase by carbamates or huperzine A increases residual activity of the enzyme upon soman challenge
Toxicology
233
180-186
2007
Homo sapiens
Manually annotated by BRENDA team
Zhu, Y.; Xiao, K.; Ma, L.; Xiong, B.; Fu, Y.; Yu, H.; Wang, W.; Wang, X.; Hu, D.; Peng, H.; Li, J.; Gong, Q.; Chai, Q.; Tang, X.; Zhang, H.; Li, J.; Shen, J.
Design, synthesis and biological evaluation of novel dual inhibitors of acetylcholinesterase and beta-secretase
Bioorg. Med. Chem.
17
1600-1613
2009
Homo sapiens
Manually annotated by BRENDA team
Dastmalchi, K.; Ollilainen, V.; Lackman, P.; Gennaes, G.B.; Dorman, H.J.; Jaervinen, P.P.; Yli-Kauhaluoma, J.; Hiltunen, R.
Acetylcholinesterase inhibitory guided fractionation of Melissa officinalis L.
Bioorg. Med. Chem.
17
867-871
2009
Homo sapiens
Manually annotated by BRENDA team
Jun, D.; Musilova, L.; Kuca, K.; Kassa, J.; Bajgar, J.
Potency of several oximes to reactivate human acetylcholinesterase and butyrylcholinesterase inhibited by paraoxon in vitro
Chem. Biol. Interact.
175
421-424
2008
Homo sapiens
Manually annotated by BRENDA team
Rizzo, S.; Cavalli, A.; Ceccarini, L.; Bartolini, M.; Belluti, F.; Bisi, A.; Andrisano, V.; Recanatini, M.; Rampa, A.
Structure-activity relationships and binding mode in the human acetylcholinesterase active site of pseudo-irreversible inhibitors related to xanthostigmine
ChemMedChem
4
670-679
2009
Homo sapiens
Manually annotated by BRENDA team
Battisti, V.; Schetinger, M.R.; Maders, L.D.; Santos, K.F.; Bagatini, M.D.; Correa, M.C.; Spanevello, R.M.; do Carmo Araujo, M.; Morsch, V.M.
Changes in acetylcholinesterase (AchE) activity in lymphocytes and whole blood in acute lymphoblastic leukemia patients
Clin. Chim. Acta
402
114-118
2009
Homo sapiens
Manually annotated by BRENDA team
Loizzo, M.R.; Tundis, R.; Menichini, F.; Menichini, F.
Natural products and their derivatives as cholinesterase inhibitors in the treatment of neurodegenerative disorders: an update
Curr. Med. Chem.
15
1209-1228
2008
Electrophorus electricus, Homo sapiens
Manually annotated by BRENDA team
Belluti, F.; Piazzi, L.; Bisi, A.; Gobbi, S.; Bartolini, M.; Cavalli, A.; Valenti, P.; Rampa, A.
Design, synthesis, and evaluation of benzophenone derivatives as novel acetylcholinesterase inhibitors
Eur. J. Med. Chem.
44
1341-1348
2008
Homo sapiens
Manually annotated by BRENDA team
Ghadimi, S.; Mousavi, S.L.; Javani, Z.
Synthesis, lipophilicity study and in vitro evaluation of some rodenticides as acetylcholinesterase reversible inhibitors
J. Enzyme Inhib. Med. Chem.
23
213-217
2008
Homo sapiens
Manually annotated by BRENDA team
Darvesh, S.; Darvesh, K.V.; McDonald, R.S.; Mataija, D.; Walsh, R.; Mothana, S.; Lockridge, O.; Martin, E.
Carbamates with differential mechanism of inhibition toward acetylcholinesterase and butyrylcholinesterase
J. Med. Chem.
51
4200-4212
2008
Homo sapiens
Manually annotated by BRENDA team
Silveyra, M.X.; Evin, G.; Montenegro, M.F.; Vidal, C.J.; Martinez, S.; Culvenor, J.G.; Saez-Valero, J.
Presenilin 1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation
Mol. Cell. Biol.
28
2908-2919
2008
Homo sapiens
Manually annotated by BRENDA team
Lima, M.M.; Lopez, J.A.; David, J.M.; Silva, E.P.; Giulietti, A.M.; de Queiroz, L.P.; David, J.P.
Acetylcholinesterase activity of alkaloids from the leaves of Waltheria brachypetala
Planta Med.
75
335-337
2008
Homo sapiens
Manually annotated by BRENDA team
Herkert, N.M.; Eckert, S.; Eyer, P.; Bumm, R.; Weber, G.; Thiermann, H.; Worek, F.
Identical kinetics of human erythrocyte and muscle acetylcholinesterase with respect to carbamate pre-treatment, residual activity upon soman challenge and spontaneous reactivation after withdrawal of the inhibitors
Toxicology
246
188-192
2008
Homo sapiens
Manually annotated by BRENDA team
Shenouda, J.; Green, P.; Sultatos, L.
An evaluation of the inhibition of human butyrylcholinesterase and acetylcholinesterase by the organophosphate chlorpyrifos oxon
Toxicol. Appl. Pharmacol.
241
135-142
2009
Homo sapiens
Manually annotated by BRENDA team
Young, S.; Fabio, K.; Guillon, C.; Mohanta, P.; Halton, T.A.; Heck, D.E.; Flowers, R.A.; Laskin, J.D.; Heindel, N.D.
Peripheral site acetylcholinesterase inhibitors targeting both inflammation and cholinergic dysfunction
Bioorg. Med. Chem. Lett.
20
2987-2990
2010
Homo sapiens
Manually annotated by BRENDA team
Geissler, T.; Brandt, W.; Porzel, A.; Schlenzig, D.; Kehlen, A.; Wessjohann, L.; Arnold, N.
Acetylcholinesterase inhibitors from the toadstool Cortinarius infractus
Bioorg. Med. Chem.
18
2173-2177
2010
Homo sapiens
Manually annotated by BRENDA team
Bharate, S.B.; Guo, L.; Reeves, T.E.; Cerasoli, D.M.; Thompson, C.M.
Bisquaternary pyridinium oximes: Comparison of in vitro reactivation potency of compounds bearing aliphatic linkers and heteroaromatic linkers for paraoxon-inhibited electric eel and recombinant human acetylcholinesterase
Bioorg. Med. Chem.
18
787-794
2010
Electrophorus electricus, Homo sapiens
Manually annotated by BRENDA team
Aurbek, N.; Herkert, N.M.; Koller, M.; Thiermann, H.; Worek, F.
Kinetic analysis of interactions of different sarin and tabun analogues with human acetylcholinesterase and oximes: Is there a structure-activity relationship?
Chem. Biol. Interact.
187
215-219
2010
Homo sapiens
Manually annotated by BRENDA team
Gaso-Sokac, D.; Katalinic, M.; Kovarik, Z.; Busic, V.; Kovac, S.
Synthesis and evaluation of novel analogues of vitamin B(6) as reactivators of tabun and paraoxon inhibited acetylcholinesterase
Chem. Biol. Interact.
187
234-237
2010
Homo sapiens
Manually annotated by BRENDA team
Camps, P.; Formosa, X.; Galdeano, C.; Gomez, T.; Munoz-Torrero, D.; Ramirez, L.; Viayna, E.; Gomez, E.; Isambert, N.; Lavilla, R.; Badia, A.; Clos, M.V.; Bartolini, M.; Mancini, F.; Andrisano, V.; Bidon-Chanal, A.; Huertas, O.; Dafni, T.; Luque, F.J.
Tacrine-based dual binding site acetylcholinesterase inhibitors as potential disease-modifying anti-Alzheimer drug candidates
Chem. Biol. Interact.
187
411-415
2010
Homo sapiens
Manually annotated by BRENDA team
Musilova, L.; Kuca, K.; Jung, Y.S.; Jun, D.
In vitro oxime-assisted reactivation of paraoxon-inhibited human acetylcholinesterase and butyrylcholinesterase
Clin. Toxicol. (Phila.)
47
545-550
2009
Homo sapiens
Manually annotated by BRENDA team
Fujiwara, M.; Yagi, N.; Miyazawa, M.
Acetylcholinesterase inhibitory activity of volatile oil from Peltophorum dasyrachis Kurz ex Bakar (yellow batai) and Bisabolane-type sesquiterpenoids
J. Agric. Food Chem.
58
2824-2829
2010
Homo sapiens
Manually annotated by BRENDA team
Pohanka, M.; Vlcek, V.; Kuca, K.; Bandouchova, H.; Pikula, J.
Pesticide sorption in typical Central European soils evaluated using a photometric microplate assay based on acetylcholinesterase inhibition
J. Appl. Biomed.
8
41-46
2010
Homo sapiens
-
Manually annotated by BRENDA team
Gholivand, K.; Abdollahi, M.; Mojahed, F.; Alizadehgan, A.M.; Dehghan, G.
Acetylcholinesterase/butyrylcholinesterase inhibition activity of some new carbacylamidophosphate derivatives
J. Enzyme Inhib. Med. Chem.
24
566-576
2009
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bohn, P.; Le Fur, N.; Hagues, G.; Costentin, J.; Torquet, N.; Papamicael, C.; Marsais, F.; Levacher, V.
Rational design of central selective acetylcholinesterase inhibitors by means of a bio-oxidisable prodrug strategy
Org. Biomol. Chem.
7
2612-2618
2009
Homo sapiens
Manually annotated by BRENDA team
Peng, L.; Zhang, G.; Zhang, D.; Xiang, J.; Zhao, R.; Wang, Y.; Zhu, D.
A fluorescence turn-on ensemble for acetylcholinesterase activity assay and inhibitor screening
Org. Lett.
11
4014-4017
2009
Homo sapiens
Manually annotated by BRENDA team
Gurovic, M.S.; Castro, M.J.; Richmond, V.; Faraoni, M.B.; Maier, M.S.; Murray, A.P.
Triterpenoids with acetylcholinesterase inhibition from Chuquiraga erinacea D. Don. subsp. erinacea (Asteraceae)
Planta Med.
76
607-610
2009
Homo sapiens
Manually annotated by BRENDA team
Pang, Y.P.; Ekstroem, F.; Polsinelli, G.A.; Gao, Y.; Rana, S.; Hua, D.H.; Andersson, B.; Andersson, P.O.; Peng, L.; Singh, S.K.; Mishra, R.K.; Zhu, K.Y.; Fallon, A.M.; Ragsdale, D.W.; Brimijoin, S.
Selective and irreversible inhibitors of mosquito acetylcholinesterases for controlling malaria and other mosquito-borne diseases
PLoS ONE
4
e6851
2009
Homo sapiens, Schizaphis graminum
Manually annotated by BRENDA team
Worek, F.; Herkert, N.M.; Koller, M.; Aurbek, N.; Thiermann, H.
Interaction of pentylsarin analogues with human acetylcholinesterase: a kinetic study
Toxicol. Lett.
187
119-123
2009
Homo sapiens
Manually annotated by BRENDA team
Tenberken, O.; Thiermann, H.; Worek, F.; Reiter, G.
Chromatographic preparation and kinetic analysis of interactions between tabun enantiomers and acetylcholinesterase
Toxicol. Lett.
195
142-146
2010
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Wille, T.; Thiermann, H.; Worek, F.
Effect of different buffers on kinetic properties of human acetylcholinesterase and the interaction with organophosphates and oximes
Arch. Toxicol.
85
193-198
2011
Homo sapiens
Manually annotated by BRENDA team
Wille, T.; Ekstroem, F.; Lee, J.C.; Pang, Y.P.; Thiermann, H.; Worek, F.
Kinetic analysis of interactions between alkylene-linked bis-pyridiniumaldoximes and human acetylcholinesterases inhibited by various organophosphorus compounds
Biochem. Pharmacol.
80
941-946
2010
Homo sapiens
Manually annotated by BRENDA team
Auletta, J.T.; Johnson, J.L.; Rosenberry, T.L.
Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase
Chem. Biol. Interact.
187
135-141
2010
Homo sapiens
Manually annotated by BRENDA team
Radi?, Z.; Kalisiak, J.; Fokin, V.V.; Sharpless, K.B.; Taylor, P.
Interaction kinetics of oximes with native, phosphylated and aged human acetylcholinesterase
Chem. Biol. Interact.
187
163-166
2010
Homo sapiens
Manually annotated by BRENDA team
Wong, K.K.; Ngo, J.C.; Liu, S.; Lin, H.Q.; Hu, C.; Shaw, P.C.; Wan, D.C.
Interaction study of two diterpenes, cryptotanshinone and dihydrotanshinone, to human acetylcholinesterase and butyrylcholinesterase by molecular docking and kinetic analysis
Chem. Biol. Interact.
187
335-339
2010
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Singh, S.; Kumar, V.; Thakur, S.; Banerjee, B.D.; Chandna, S.; Rautela, R.S.; Grover, S.S.; Rawat, D.S.; Pasha, S.T.; Jain, S.K.; Ichhpujani, R.L.; Rai, A.
DNA damage and cholinesterase activity in occupational workers exposed to pesticides
Environ. Toxicol. Pharmacol.
31
278-285
2011
Homo sapiens
Manually annotated by BRENDA team
Ilg, T.; Cramer, J.; Lutz, J.; Noack, S.; Schmitt, H.; Williams, H.; Newton, T.
The characterization of Lucilia cuprina acetylcholinesterase as a drug target, and the identification of novel inhibitors by high throughput screening
Insect Biochem. Mol. Biol.
41
470-483
2011
Homo sapiens, Lucilia cuprina (P91954), Lucilia cuprina
Manually annotated by BRENDA team
Fang, L.; Pan, Y.; Muzyka, J.L.; Zhan, C.G.
Active site gating and substrate specificity of butyrylcholinesterase and acetylcholinesterase: insights from molecular dynamics simulations
J. Phys. Chem. B
115
8797-8805
2011
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Saint-Andre, G.; Kliachyna, M.; Kodepelly, S.; Louise-Leriche, L.; Gillon, E.; Renard, P.; Nachon, F.; Baati, R.; Wagner, A.
Design, synthesis and evaluation of new α-nucleophiles for the hydrolysis of organophosphorus nerve agents: Application to the reactivation of phosphorylated acetylcholinesterase
Tetrahedron
67
6352-6361
2011
Homo sapiens
-
Manually annotated by BRENDA team
Herkert, N.M.; Thiermann, H.; Worek, F.
In vitro kinetic interactions of pyridostigmine, physostigmine and soman with erythrocyte and muscle acetylcholinesterase from different species
Toxicol. Lett.
206
41-46
2011
Cavia porcellus, Homo sapiens, Macaca mulatta, Sus scrofa
Manually annotated by BRENDA team
Kaya, H.B.; Oezcan, B.; Sisecioglu, M.; Ozdemir, H.
Purification of acetylcholinesterase by 9-amino-1,2,3,4-tetrahydroacridine from human erythrocytes
Appl. Biochem. Biotechnol.
170
198-209
2013
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sukhorukov, A.Y.; Nirvanappa, A.C.; Swamy, J.; Ioffe, S.L.; Nanjunda Swamy, S.; Basappa, S.; Rangappa, K.S.
Synthesis and characterization of novel 1,2-oxazine-based small molecules that targets acetylcholinesterase
Bioorg. Med. Chem. Lett.
24
3618-3621
2014
Homo sapiens
Manually annotated by BRENDA team
Alpan, A.S.; Parlar, S.; Carlino, L.; Tarikogullari, A.H.; Alptuezuen, V.; Guenes, H.S.
Synthesis, biological activity and molecular modeling studies on 1H-benzimidazole derivatives as acetylcholinesterase inhibitors
Bioorg. Med. Chem.
21
4928-4937
2013
Electrophorus electricus, Homo sapiens
Manually annotated by BRENDA team
Karade, H.N.; Valiveti, A.K.; Acharya, J.; Kaushik, M.P.
Synthesis and in vitro evaluation of bis-quaternary 2-(hydroxyimino)-N-(pyridin-3-yl)acetamide derivatives as reactivators against sarin and VX inhibited human acetylcholinesterase (hAChE)
Bioorg. Med. Chem.
22
2684-2691
2014
Homo sapiens
Manually annotated by BRENDA team
Acharya, J.; Dubey, D.K.; Srivastava, A.K.; Raza, S.K.
In vitro reactivation of sarin-inhibited human acetylcholinesterase (AChE) by bis-pyridinium oximes connected by xylene linkers
Toxicol. In Vitro
25
251-256
2011
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Herkert, N.M.; Freude, G.; Kunz, U.; Thiermann, H.; Worek, F.
Comparative kinetics of organophosphates and oximes with erythrocyte, muscle and brain acetylcholinesterase
Toxicol. Lett.
209
173-178
2012
Cavia porcellus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Worek, F.; Bierwisch, A.; Wille, T.; Koller, M.; Thiermann, H.
Kinetic interactions of a homologous series of bispyridinium monooximes (HGG oximes) with native and phosphonylated human acetylcholinesterase
Toxicol. Lett.
212
29-32
2012
Homo sapiens
Manually annotated by BRENDA team
Meirer, K.; Glatzel, D.; Kretschmer, S.; Wittmann, S.K.; Hartmann, M.; Bloecher, R.; Angioni, C.; Geisslinger, G.; Steinhilber, D.; Hofmann, B.; Fuerst, R.; Proschak, E.
Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase
Molecules
22
45
2016
Pardosa pseudoannulata (A0A1B1FIV8), Pardosa pseudoannulata (A0A1B1FIW0), Pardosa pseudoannulata (A0A1B1FIW2), Pardosa pseudoannulata (A0A1B1FIZ1), Pardosa pseudoannulata (V5QQC6), Tetronarce californica (P04058), Homo sapiens (P22303), Tetranychus urticae (Q86CZ4)
Manually annotated by BRENDA team
Saxena, A.; Belinskaya, T.; Schopfer, L.M.; Lockridge, O.
Characterization of butyrylcholinesterase from porcine milk
Arch. Biochem. Biophys.
652
38-49
2018
Homo sapiens (P22303)
Manually annotated by BRENDA team
Aktas, A.; Taslimi, P.; Guelcin, I.; Goek, Y.
Novel NHC precursors synthesis, characterization, and carbonic anhydrase and acetylcholinesterase inhibitory properties
Arch. Pharm.
350
e1700045
2017
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Chowdhary, S.; Bhattacharyya, R.; Banerjee, D.
1-Naphthyl acetate a chromogenic substrate for the detection of erythrocyte acetylcholinesterase activity
Biochimie
154
194-209
2018
Homo sapiens
Manually annotated by BRENDA team
Mohammed, A.; Sneathen, J.; Frojen, S.G.; Kuo, L.; Dupureur, C.M.
Stereospecific cholinesterase inhibition by O,S-diethylphenylphosphonothioate
Bioorg. Med. Chem.
25
3053-3058
2017
Electrophorus electricus (O42275), Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Saleem, M.; Rafiq, M.; Seo, S.Y.; Lee, K.H.
Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart
Biosci. Rep.
36
e00311
2016
Homo sapiens (P22303)
Manually annotated by BRENDA team
Kim, K.; Yao, J.; Jin, Z.; Zheng, F.; Zhan, C.G.
Kinetic characterization of cholinesterases and a therapeutically valuable cocaine hydrolase for their catalytic activities against heroin and its metabolite 6-monoacetylmorphine
Chem. Biol. Interact.
293
107-114
2018
Homo sapiens (P22303)
Manually annotated by BRENDA team
Bester, S.M.; Guelta, M.A.; Cheung, J.; Winemiller, M.D.; Bae, S.Y.; Myslinski, J.; Pegan, S.D.; Height, J.J.
Structural insights of stereospecific inhibition of human acetylcholinesterase by VX and subsequent reactivation by HI-6
Chem. Res. Toxicol.
31
1405-1417
2018
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Lalut, J.; Santoni, G.; Karila, D.; Lecoutey, C.; Davis, A.; Nachon, F.; Silman, I.; Sussman, J.; Weik, M.; Maurice, T.; Dallemagne, P.; Rochais, C.
Novel multitarget-directed ligands targeting acetylcholinesterase and sigma1 receptors as lead compounds for treatment of Alzheimers disease synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase
Eur. J. Med. Chem.
162
234-248
2018
Tetronarce californica (P04058), Tetronarce californica, Homo sapiens (P22303)
Manually annotated by BRENDA team
Larik, F.A.; Shah, M.S.; Saeed, A.; Shah, H.S.; Channar, P.A.; Bolte, M.; Iqbal, J.
New cholinesterase inhibitors for Alzheimers disease structure activity relationship, kinetics and molecular docking studies of 1-butanoyl-3-arylthiourea derivatives
Int. J. Biol. Macromol.
116
144-150
2018
Homo sapiens (P22303)
Manually annotated by BRENDA team
Carmany, D.O.; Mach, P.M.; Rizzo, G.M.; Dhummakupt, E.S.; McBride, E.M.; Sekowski, J.W.; Benton, B.; Demond, P.S.; Busch, M.W.; Glaros, T.
On-substrate enzymatic reaction to determine acetylcholinesterase activity in whole blood by paper spray mass spectrometry
J. Am. Soc. Mass Spectrom.
29
2436-2442
2018
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Sari, Y.; Aktas, A.; Taslimi, P.; Goek, Y.; Gulcin, I.
Novel N-propylphthalimide- and 4-vinylbenzyl-substituted benzimidazole salts synthesis, characterization, and determination of their metal chelating effects and inhibition profiles against acetylcholinesterase and carbonic anhydrase enzymes
J. Biochem. Mol. Toxicol.
32
e22009
2018
Homo sapiens (P22303)
Manually annotated by BRENDA team
Pohanka, M.; Holas, O.
Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay
J. Enzyme Inhib. Med. Chem.
30
796-799
2015
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Zorbaz, T.; Malinak, D.; Marakovic, N.; Macek Hrvat, N.; Zandona, A.; Novotny, M.; Skarka, A.; Andrys, R.; Benkova, M.; Soukup, O.; Katalinic, M.; Kuca, K.; Kovarik, Z.; Musilek, K.
Pyridinium oximes with ortho-positioned chlorine moiety exhibit improved physicochemical properties and efficient reactivation of human acetylcholinesterase inhibited by several nerve agents
J. Med. Chem.
61
10753-10766
2018
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Xiao, Q.; Zhou, H.; Wei, H.; Du, H.; Tan, W.; Zhan, Y.; Pistolozzi, M.
A new method to characterize the kinetics of cholinesterases inhibited by carbamates
J. Pharm. Biomed. Anal.
144
175-182
2017
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Elsebai, M.; Ghabbour, H.; Marzouk, A.; Salmas, R.; Orhan, I.; Senol, F.
Amberboin and lipidiol X-ray crystalographic data, absolute configuration and inhibition of cholinesterase
Phytochem. Lett.
27
44-48
2018
Homo sapiens (P22303)
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Horn, G.; de Koning, M.C.; van Grol, M.; Thiermann, H.; Worek, F.
Interactions between acetylcholinesterase, toxic organophosphorus compounds and a short series of structurally related non-oxime reactivators analysis of reactivation and inhibition kinetics in vitro
Toxicol. Lett.
299
218-225
2018
Homo sapiens (P22303), Homo sapiens
Manually annotated by BRENDA team
Ceylan, H.; Erdogan, O.
Cloning, expression, and characterization of human brain acetylcholinesterase in Escherichia coli using a SUMO fusion tag
Turk. J. Biol.
41
77-87
2017
Homo sapiens (P22303)
-
Manually annotated by BRENDA team