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Information on EC 3.1.1.8 - cholinesterase 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
                3.1.1.8 cholinesterase
IUBMB Comments
Acts on a variety of choline esters and a few other compounds.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
cholinesterase, butyrylcholinesterase, buche, plasma cholinesterase, serum cholinesterase, pseudocholinesterase, choline esterase, hubche, hbche, plasma esterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl choline acylhydrolase
-
-
acylcholine acyl-hydrolase
-
-
Acylcholine acylhydrolase
-
-
-
-
benzoylcholinesterase
-
-
-
-
BtChoEase
-
-
BuChE
butyrocholinesterase
-
-
butyrylcholine esterase
-
-
-
-
butyrylcholinesterase
butyrylcholinesterase K
-
-
calcium-activated butyrylcholinesterase
-
-
ChE-II
-
-
choline esterase
-
-
choline esterase II (unspecific)
-
-
-
-
cholinesterase
-
-
EQ-BCHE
-
-
-
-
esterase, butyrylcholine
-
-
-
-
esterase, choline
-
-
-
-
hBChE
non specific cholinesterase
-
-
non-specific cholinesterase
propionylcholinesterase
-
-
-
-
pseudo choline esterase
-
-
pseudo cholinesterase
-
-
pseudocholinesterase
-
-
serum cholinesterase
-
-
additional information
-
cf. EC 3.5.1.13
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acylcholine + H2O = choline + a carboxylate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acylcholine acylhydrolase
Acts on a variety of choline esters and a few other compounds.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-08-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-cocaine + H2O
?
show the reaction diagram
(+/-)-cocaine + H2O
?
show the reaction diagram
-
-
-
?
(-)-cocaine + H2O
?
show the reaction diagram
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
show the reaction diagram
-
-
-
?
(S)-butyrylthiocholine + H2O
thiocholine + butyrate
show the reaction diagram
-
-
-
?
2,2,2-trifluoro-N-(2-nitrophenyl)acetamide + H2O
2-nitroaniline + trifluoroacetate
show the reaction diagram
-
a neutral amide
-
-
?
2-nitroacetanilide + H2O
2-nitroaniline + acetate
show the reaction diagram
-
a neutral amide
-
-
?
2-nitrophenyl butyrate
2-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
3-(acetamido) N,N,N-trimethylanilinium + H2O
3-amino-N,N,N-trimethylanilinium + acetate
show the reaction diagram
-
a positively charged amide, hydrolysis by the wild-type enzyme and the mutant D70G shows a long transient phase preceeding the steady state, hysteretic burst induction phase, overview
-
-
?
3-(acetamido)N,N,N-trimethylanilinium + H2O
?
show the reaction diagram
-
-
-
-
?
3-nitroacetanilide + H2O
3-nitroaniline + acetate
show the reaction diagram
-
a neutral amide
-
-
?
6-monoacetylmorphine + H2O
morphine + acetate
show the reaction diagram
-
-
-
?
acetylcholine + H2O
acetate + choline
show the reaction diagram
-
-
-
-
?
acetylcholine + H2O
choline + acetate
show the reaction diagram
acetylsalicylic acid + H2O
acetate + salicylate
show the reaction diagram
-
-
-
?
acetylthiocholine + H2O
?
show the reaction diagram
-
detection with 5,5-dithiobis(2-nitrobenzoic acid)
-
-
?
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
acetylthiocholine iodide + H2O
acetate + thiocholine iodide
show the reaction diagram
-
-
-
?
adipyldicholine + H2O
adipic acid + choline
show the reaction diagram
lower activity, monitoring the dicholine substrates, the monocholine intermediates, the dicarboxylic acid and choline products by mass spectrometry,
-
-
?
BChE-FP + H2O
?
show the reaction diagram
-
structure-based design and application of a fluorogenic molecular probe, BChE-FP, specific to butyrylcholinesterase (BChE). This compound is rationally designed by mimicking the native substrate and optimized stepwise by manipulating the steric feature and the reactivity of the designed probe targeting the structural difference of the active pockets of BChE and acetylcholinesterase (AChE). The refined probe, BChE-FP, exhibits high specificity toward BChE compared to AChE, producing about 275fold greater fluorescence enhancement upon the catalysis by BChE, molecular docking simulation, overview. The proximity of Ser198 to the carbonyl group of BChE-FP is about 4.3 A in the BChE active site, whereas the proximity of Ser203 to the carbonyl group of BChE-FP is about 7.4 A in the AChE active site. The binding affinity of BChE-FP with BChE is B100fold greater than that of acetylthiocholine, while the catalytic constant for BChE-FP is 190fold lower than that of acetylthiocholine
-
-
?
benzoylcholine + H2O
benzoate + choline
show the reaction diagram
benzoylcholine + H2O
benzoic acid + choline
show the reaction diagram
-
-
-
?
benzoylcholine + H2O
choline + benzoate
show the reaction diagram
benzoylthiocholine + H2O
?
show the reaction diagram
-
-
-
-
?
benzoylthiocholine + H2O
thiocholine + benzoate
show the reaction diagram
butyrylcholine + H2O
butanoate + choline
show the reaction diagram
-
-
-
-
?
butyrylcholine + H2O
butyrate + choline
show the reaction diagram
-
-
-
-
?
butyrylcholine + H2O
choline + butyrate
show the reaction diagram
butyrylthiocholine + H2O
?
show the reaction diagram
-
-
-
-
?
butyrylthiocholine + H2O
butanoate + thiocholine
show the reaction diagram
-
-
-
-
?
butyrylthiocholine + H2O
butyrate + thiocholine
show the reaction diagram
butyrylthiocholine + H2O
thiocholine + butyrate
show the reaction diagram
butyrylthiocholine iodide + H2O
butyrate + thiocholine iodide
show the reaction diagram
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
butyrylthiocholine iodide + H2O
thiocholine iodide + butyrate
show the reaction diagram
choline esters + H2O
?
show the reaction diagram
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
show the reaction diagram
D-butyryl-alpha-methylcholine + H2O
butanoate + alpha-methylcholine
show the reaction diagram
-
-
-
-
?
D-butyryl-beta-methylcholine + H2O
butanoate + beta-methylcholine
show the reaction diagram
-
-
-
-
?
echothiophate + H2O
?
show the reaction diagram
substrate for mutant enzyme G117H
-
-
?
ethyl ([2-[bis(propan-2-yl)amino]ethyl]-sulfanyl)(methyl)phosphinate + H2O
?
show the reaction diagram
substrate for mutant enzyme G117H
-
-
?
heroin + H2O
6-monoacetylmorphine + acetate
show the reaction diagram
-
-
-
?
heroin + H2O
?
show the reaction diagram
-
-
-
?
L-butyryl-alpha-methylcholine + H2O
butanoate + alpha-methylcholine
show the reaction diagram
-
-
-
-
?
L-butyryl-beta-methylcholine + H2O
butanoate + beta-methylcholine
show the reaction diagram
-
-
-
-
?
N-methyl-(7-dimethylcarbamoxy)quinolinium iodide + H2O
?
show the reaction diagram
-
atypical and usual enzyme
-
-
?
N-methylindoxyl acetate + H2O
N-methylindole + acetate
show the reaction diagram
-
-
-
?
O-ethyl-O-(4-nitrophenyl)-phenylphosphonothioate + H2O
?
show the reaction diagram
-
-
-
-
?
o-nitrophenylbutyrate + H2O
o-nitrophenol + butanoate
show the reaction diagram
-
atypical and usual enzyme
-
-
?
propionylthiocholine + H2O
?
show the reaction diagram
propionylthiocholine + H2O
propanoate + thiocholine
show the reaction diagram
-
propylthiocholine
-
-
?
propionylthiocholine + H2O
thiocholine + propionate
show the reaction diagram
-
-
-
?
S-butyrylthiocholine + H2O
butyrate + thiocholine
show the reaction diagram
-
-
-
-
?
sarin + H2O
?
show the reaction diagram
substrate for mutant enzyme G117H
-
-
?
sebacyldicholine + H2O
sebacic acid + choline
show the reaction diagram
high activity, monitoring the dicholine substrates, the monocholine intermediates, the dicarboxylic acid and choline products by mass spectrometry, sebacyldicholine is hydrolyzed at both choline ester sites, though hydrolysis of dicholine is faster than hydrolysis of monocholine, overview
-
-
?
succinylcholine + H2O
succinate + choline
show the reaction diagram
-
-
-
-
?
succinyldithiocholine + H2O
?
show the reaction diagram
-
-
-
-
?
succinylmonocholine + H2O
succinate + choline
show the reaction diagram
-
-
-
-
?
succinylthiocholine + H2O
thiocholine + succinate
show the reaction diagram
-
-
-
?
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
acetylsalicylic acid + H2O
acetate + salicylate
show the reaction diagram
-
-
-
?
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
-
-
-
?
benzoylcholine + H2O
benzoic acid + choline
show the reaction diagram
-
-
-
?
butyrylcholine + H2O
butyrate + choline
show the reaction diagram
-
-
-
-
?
butyrylcholine + H2O
choline + butyrate
show the reaction diagram
butyrylthiocholine + H2O
butyrate + thiocholine
show the reaction diagram
butyrylthiocholine + H2O
thiocholine + butyrate
show the reaction diagram
choline esters + H2O
?
show the reaction diagram
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
show the reaction diagram
-
-
-
-
?
heroin + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates 9fold at 0.5 mM with substrate O-ethyl-O-(4-nitrophenyl)-phenylphosphonothioate via a specific EF-hand calcium binding site, molecular modelling of Ca2+ binding to EF-hands, disruption by H2O2-mediated oxidation
Zn2+
-
1-2 mM, 10% activation, inhibitory above
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-cocaine
-
-
(+)-debromoflustramine B
-
-
(+/-)-6-bromo-N-((1-(2,3-dihydro-1H-inden-2-yl)-piperidin-3-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
-
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-1-naphthamide
-
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide
the inhibitor is highly selective for BChE versus acetylcholinesterase, AChE, and shows selective reversible huBChE inhibition in the picomolar concentration range. Enzyme-binding crystal structure determination and analysis, overview. The compound has a picomolar inhibition constant versus BChE due to strong cation-Pi interactions, as revealed by the solved crystal structure of its complex with human BChE. Additionally, the inhibitor inhibits BChE ex vivo and is noncytotoxic. In vitro pharmacokinetic experiments show that (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide is highly protein-bound, highly permeable, and metabolically stable. (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide crosses the blood-brain barrier and improves memory, cognitive functions, and learning abilities of mice in a scopolamine model of dementia. (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide is thus a promising advanced lead compound for the development of drugs for alleviating symptoms of cholinergic hypofunction in patients with advanced Alzheimer's disease
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(3-methoxypropyl)-2-naphthamide
-
(+/-)-N-((1-(benzo[d]thiazol-2-ylmethyl)piperidin-3-yl)methyl)-2-naphthamide
-
(+/-)-N-((1-benzylpiperidin-3-yl)methyl)-2-naphthamide
-
(+/-)-N-((1-benzylpiperidin-3-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
-
(-)-cocaine
-
-
(-)-debromoflustramine B
-
-
(-)-huperzine A
-
(2x)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-([[(2E)-3-phenylprop-2-enoyl]oxy]carbonyl)-D-arabino-hexitol
96% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(2-methylbutanoyl)-D-arabino-hexitol
99% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(biphenyl-4-ylcarbonyl)-D-arabino-hexitol
99% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(carboxycarbamoyl)-D-arabino-hexitol
92% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(cyclopentylcarbonyl)-D-arabino-hexitol
99% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(cyclopropylcarbonyl)-D-arabino-hexitol
97% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(phenoxycarbonyl)-D-arabino-hexitol
99% inhibition at 0.1 mM, highly selective for BuChE, with about 50000fold selectivity over human erythrocyte acetylcholinesterase. Competitive, and slowly reversible inhibition by active site carbamylation
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-([[(4-methylphenyl)sulfonyl]oxy]carbonyl)-D-arabino-hexitol
25% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-([[(trifluoromethyl)sulfonyl]oxy]carbonyl)-D-arabino-hexitol
85% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(2H-chromen-2-yloxy)carbonyl]-D-arabino-hexitol
100% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(3,4-dihydroxyphenyl)carbonyl]-D-arabino-hexitol
38% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(pentanoyloxy)carbonyl]-D-arabino-hexitol
95% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(propanoyloxy)carbonyl]-D-arabino-hexitol
97% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[([[4-(heptyloxy)phenyl]carbonyl]oxy)carbonyl]-D-arabino-hexitol
80% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(methylsulfonyl)oxy]carbonyl]-D-arabino-hexitol
9.8% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(naphthalen-2-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
100% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(pyridin-3-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
99% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(pyridin-4-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
97% inhibition at 0.1 mM
(2xi)-1,4:3,6-dianhydro-2-O-([2-[(carbamoyloxy)methyl]-5-hydroxybenzyl]carbamoyl)-D-arabino-hexitol
95% inhibition at 0.1 mM
(2xi)-5-O-[(acetyloxy)carbonyl]-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-D-arabino-hexitol
97% inhibition at 0.1 mM
(2Z)-4-[(2-aminophenyl)amino]-4-oxobut-2-enoic acid
-
one of the best inhibitors
(2Z)-4-[(4-nitrophenyl)amino]-4-oxobut-2-enoic acid
-
weak inhibition
(3,4-dimethoxyphenyl)-(4-([(2-dimethylaminoethyl)-methylamino]methyl)phenyl)-methanone
-
-
(3,4-dimethoxyphenyl)-(4-([(2-methoxybenzyl)methylamino]methyl)phenyl)-methanone
-
-
(3,4-dimethoxyphenyl)-(4-([methyl-(3-methylbenzyl)amino]methyl)phenyl)methanone
-
-
(3,4-dimethoxyphenyl)-(4-([methyl-(3-nitrobenzyl)amino]methyl)phenyl)methanone
-
-
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl (2-methylphenyl)carbamate
-
50% inhibition at 1950 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 50 nM
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl ethylcarbamate
-
50% inhibition at 4 nM
(3aR)-1,3a,8-trimethyl-1,2,3,3a,8,8a-hexahydropyrrolo(2,3-b)indol-5-yl methylcarbamate
-
50% inhibition at 16 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl (2-methylphenyl)carbamate
-
50% inhibition at 1560 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 17 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl ethylcarbamate
-
50% inhibition at 2 nM
(3aR)-3a,8-dimethyl-3,3a,8,8a-tetrahydro-2H-furo(2,3-b)indol-5-yl methylcarbamate
-
50% inhibition at 4 nM
(4-([benzyl-(2-dimethylaminoethyl)amino]methyl)-phenyl)-(3,4-dimethoxyphenyl)methanone
-
-
(4-([benzyl-(2-hydroxyethyl)amino]methyl)phenyl)-(3,4-dimethoxyphenyl)methanone
-
-
(4-[(benzylethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
-
-
(4-[(benzylmethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
-
-
(4-[(benzylmethylamino)methyl]phenyl)-(3-fluoro-4-methoxyphenyl)methanone
-
-
(4-[(benzylmethylamino)methyl]phenyl)-(4-methoxyphenyl)methanone
-
-
(4-[3-(benzylmethylamino)propenyl]phenyl)-(3,4-dimethoxyphenyl)methanone
-
-
(7R,11R)-huprine 19
binding structure from analysis of the crystal structure
(7S,11S)-huprine W
binding structure from analysis of the crystal structure
(E)-1-(4-carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)but-2-ene
-
(R)-bambuterol monocarbamate
inhibition kinetics of human and dog plasma butyrylcholinesterase 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 and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
E2020, acetylcholinesterase inhibitor used in treatment of Alzheimer's diaease, inhibition kinetics
(RS)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate
i.e. rac-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(S)-bambuterol monocarbamate
inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
(S)-[3-[2-(tert-butylamino)-1-hydroxyethyl]-5-(dimethylcarbamoyloxy)phenyl] N,N-dimethylcarbamate
i.e. (S)-bambuterol, inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
1,1'-(2E)-but-2-ene-1,4-diyldipyridinium dibromide
-
-
1,1'-(2Z)-but-2-ene-1,4-diyldipyridinium dichloride
-
-
1,1'-(benzene-1,2-diyldimethanediyl)dipyridinium dibromide
-
-
1,1'-(benzene-1,3-diyldimethanediyl)dipyridinium dibromide
-
-
1,1'-(benzene-1,4-diyldimethanediyl)dipyridinium dibromide
-
-
1,1'-(naphthalene-2,7-diyldimethanediyl)dipyridinium dibromide
-
-
1,1'-(oxydiethane-2,1-diyl)dipyridinium dibromide
-
-
1,1'-(oxydimethanediyl)dipyridinium dichloride
-
-
1,1'-butane-1,4-diyldipyridinium dibromide
-
-
1,1'-decane-1,10-diyldipyridinium dibromide
-
-
1,1'-heptane-1,7-diyldipyridinium dibromide
-
-
1,1'-hexane-1,6-diyldipyridinium dibromide
-
-
1,1'-nonane-1,9-diyldipyridinium dibromide
-
-
1,1'-octane-1,8-diyldipyridinium dibromide
-
-
1,1'-pentane-1,5-diyldipyridinium dibromide
-
-
1,1'-undecane-1,11-diyldipyridinium dibromide
-
-
1,3-bis[5(diethyl-o-nitrobenzylammonium)pentyl]-6-methyluracil dibromide
compound C547, a fast-binding reversible inhibitor of mixed-type on human BChE. The inhibitor shows a high level of pharmacological selectivity in inhibiting acetylcholinesterase (AChE, EC 3.1.1.7) as compared to butyrylcholinesterase
1,3a,8-tris(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-nitro-D-threo-hexitol
96% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-(butylcarbamoyl)-5-O-nitro-D-threo-hexitol
92% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-(cyclohexylcarbamoyl)-5-O-nitro-D-threo-hexitol
99% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-(ethylcarbamoyl)-5-O-nitro-D-threo-hexitol
73% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-(methylcarbamoyl)-5-O-nitro-D-threo-hexitol
82% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-nitro-5-O-(phenylcarbamoyl)-D-threo-hexitol
37% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-nitro-5-O-(propylcarbamoyl)-D-threo-hexitol
93% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-nitro-5-O-[[4-(trifluoromethyl)phenyl]carbamoyl]-D-threo-hexitol
10% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-[(2-chlorophenyl)carbamoyl]-5-O-nitro-D-threo-hexitol
11% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-[(3,4-dichlorophenyl)carbamoyl]-5-O-nitro-D-threo-hexitol
28% inhibition at 0.1 mM
1,4:3,6-dianhydro-2-O-[(3-chlorophenyl)carbamoyl]-5-O-nitro-D-threo-hexitol
11% inhibition at 0.1 mM
1,5-bis(4-allyldimethylammoniumphenyl)pentan-3-one dibromide
i.e. BW284c51
1-(2-nitrophenyl)-1H-pyrrole-2,5-dione
-
weak inhibition
1-(2-nitrophenyl)pyrrolidine-2,5-dione
-
weak inhibition
1-(3-aminophenyl)pyrrolidine-2,5-dione
-
one of the best inhibitors
1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium)butane
-
1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium)propane
-
1-benzyl-5-methoxy-3a,8-bis(3-methylbut-2-enyl)-1,2,3,3a,8,8ahexahydropyrrolo[2,3-b]indole
-
-
1-butanoyl-3-(2,6-dimethylphenyl) thiourea
-
1-butanoyl-3-(3-methoxyphenyl)thiourea
-
1-butanoyl-3-(4-chlorophenyl)thiourea
-
1-butanoyl-3-benzylthiourea
-
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl (2-methylphenyl)carbamate
-
50% inhibition above 0.030 mM
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 22 nM
1-methyl-8,10-dioxatricyclo(7.2.1.0 2,7)dodeca-2,4,6-trien-5-yl ethylcarbamate
-
50% inhibition at 24 nM
1-naphthyl phenothiazine carbamate
-
-
1-[2-(4-carboxyphenyl)-5-(ethoxycarbonyl)-1H-benzimidazol-1-yl]-4-ethylmorpholin-1-ium
-
-
10-(2,2-dimethylpropanoyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 4.7
10-(2-ethylbutanoyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(3,3-dimethylbutanoyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(3-methylbutanoyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(chloroacetyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 7.3
10-(cyclobutylcarbonyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 11.6
10-(cycloheptylcarbonyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(cyclohexylacetyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(cyclohexylcarbonyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(cyclopentylacetyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(cyclopentylcarbonyl)-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-(cyclopropylcarbonyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 1.9
10-(methoxyacetyl)-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 0.8
10-acetyl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 1.1
10-butyryl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 1.9
10-heptanoyl-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-hexanoyl-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-isobutyryl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 2.7
10-pentanoyl-10H-phenothiazine
-
not inhibitory to EC 3.1.1.7
10-propionyl-10H-phenothiazine
-
relative potency EC 3.1.1.8 to EC 3.1.1.7 is 1.8
2'-ethylphenylgeneserine N-oxide
-
50% inhibition at 1700 nM
2,3-dimethoxy-6-methyl-9H-xanthen-9-one
-
-
2-(1-piperidinyl)ethyl phenothiazine carbamate
-
-
2-(1-pyrrolidinyl)ethyl phenothiazine carbamate
-
-
2-(3-methylphenyl)-4H-chromen-4-one
-
-
2-(4-(((7-(diethylamino)-2,4-dioxo-2H-chromen-3(4H)-ylidene)methyl)amino)phenyl)-N'-1,2,3,4-tetrahydroacridin-9-ylacetohydrazide
-
-
2-(4-methylphenyl)-4H-chromen-4-one
-
-
2-(4-morpholino)ethyl phenothiazine carbamate
-
-
2-(benzylaminocarbonyloxy)-5-(phenylcarbonyloxyimino-)-1,4 3,6-dianhydro-D-glucitol
-
9% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-deoxy, 5-dehydro-((ethyloxycarbonyl)ene-)-1,4 3,6-dianhydro-D-glucitol
-
4.9% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-deoxy-5-phenylcarbonylamino-1,4 3,6-dianhydro-D-glucitol
-
46% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-deoxy-L-xylohex-6-enitol
-
9.8% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-keto-1,4 3,6-dianhydro-D-glucitol
-
10% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-ketoxime-1,4 3,6-dianhydro-D-glucitol
-
83% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-O-(phenylpropyloxy)-1,4 3,6-dianhydro-D-glucitol
-
55% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy)-5-O-benzyl-1,4 3,6-dianhydro-D-glucitol
-
55% inhibition at 0.1 mM
2-(benzylaminocarbonyloxy-)-5-O-(1-naphthoyl)-1,4:3,6-dianhydro-D-glucitol
99% inhibition at 0.1 mM
2-(diethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
-
2-(dimethylamino)ethyl (2Z)-2-[[(2-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-2-[[(2-chlorophenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-2-[[(3-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-2-[[(4-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-2-[[(4-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoate
-
2-(dimethylamino)ethyl (2Z)-3-phenyl-2-[(phenylcarbonyl)amino]prop-2-enoate
-
2-(dimethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
-
2-chlorophenyl phenothiazine carbamate
-
-
2-dimethylaminoethyl esters of N-substituted alpha,beta-dehydrophenylalanine
inhibition potencies, overview
-
2-methoxyphenyl phenothiazine carbamate
-
-
2-methylphenyl phenothiazine carbamate
-
-
2-naphthyl phenothiazine carbamate
-
-
2-t-butylphenyl phenothiazine carbamate
-
-
2-[[(2Z)-2-[[(2-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
2-[[(2Z)-2-[[(2-chlorophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
2-[[(2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium
i.e. compound IIIf, a choline ester of dehydrophenylalanine, the amine group of the amino acid is derivatized with a benzoyl group containing a methoxy in the 2-position, binding structure and modelling, overview
2-[[(2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
2-[[(2Z)-2-[[(3-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
2-[[(2Z)-2-[[(4-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
2-[[(2Z)-2-[[(4-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
-
3-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)benzoic acid
-
one of the best inhibitors
3-(3-methylphenyl)-2H-chromen-2-one
-
-
3-(4-methylphenyl)-2H-chromen-2-one
-
-
3-(diethylamino)propyl 10H-phenothiazine-10-carboxylate
-
-
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-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-[(methyl[7-[(9-oxo-9H-xanthen-3-yl)oxy]heptyl]amino)methyl]phenyl methylcarbamate
-
-
3-[10-(benzylmethylamino)decyloxy]xanthen-9-one
-
-
3-[11-(benzylmethylamino)undecyloxy]xanthen-9-one
-
-
3-[12-(benzylmethylamino)dodecyloxy]xanthen-9-one
-
-
3-[2-(4-carboxyphenyl)-5-(ethoxycarbonyl)-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
-
-
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-(benzylmethylamino)pentyloxy]xanthen-9-one
-
-
3-[5-(ethoxycarbonyl)-2-(4-hydroxyphenyl)-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
-
-
3-[5-(ethoxycarbonyl)-2-[4-(trifluoromethyl)phenyl]-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
-
-
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, inhibition with high selectivity toward BuChE
3a,8-dibenzyl-1-methyl-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
3a,8-dibenzyl-5-methoxy-1-methyl-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl (2-methylphenyl)carbamate
-
50% inhibition above 0.030 mM
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl (4-isopropylphenyl)carbamate
-
50% inhibition at 27 nM
3a-methyl-2,3,3a,8a-tetrahydrofuro(2,3-b)(1)benzofuran-5-yl ethylcarbamate
-
50% inhibition at 6 nM
4,4'-Bipyridine
-
competitive, reversible
4-biphenyl phenothiazine carbamate
-
-
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-chlorophenyl phenothiazine carbamate
-
-
4-methoxyphenyl phenothiazine carbamate
-
-
4-methylphenyl phenothiazine carbamate
-
-
4-t-butylphenyl phenothiazine carbamate
-
-
4-[(2-aminophenyl)amino]-4-oxobutanoic acid
-
one of the best inhibitors
4-[(3-aminophenyl)amino]-4-oxobutanoic acid
-
weak inhibition
5-deoxy-5-azido-1,4 3,6-dianhydro-D-glucitol
-
5% inhibition at 0.1 mM
5-methoxy-1-methyl-3a,8-bis(3-methylbut-2-en-1-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
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-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-[7-(benzylmethylamino)heptyloxy]-2,3-dimethoxyxanthen-9-one
-
-
7-exo-(benzylaminocarbonyloxy)-3-oxo-2,5,9-trioxabicyclo [4.3.0] nonane
-
10% inhibition at 0.1 mM
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-methoxy-N-nonyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride (1:1)
-
-
7-methoxy-N-octyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
7-methoxy-N-pentyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
7-methoxy-N-propyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
7-O-galloyl-D-sedoheptulose
a mixed-type inhibitor, enzyme interacting residues, overview
7-[(diethoxyphosphoryl)oxy]-1-methylquinolinium iodide
-
an irreversible inhibitor
8-benzyl-1-methyl-3a-(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
8-benzyl-5-methoxy-1-methyl-3a-(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
-
-
9-amino-7-methoxy-1,2,3,4-tetrahydroacridine
-
-
amberboin
a sesquiterpene lactone from extract of Volutaria abyssinica, inhibition mechanism
AP2238
-
-
bambuterol
Benzoylcholine
-
competitive
Berberine
-
bisnorcymserine
-
inhibition in the nanomolar range
butyl carbamate
-
-
Butyrylcholine
-
competitive to butyrylthiocholine
butyrylthiocholine
BW284c51
chlorogenic acid
-
30.8% inhibition at 1 mM
chlorpromazine
-
not inhibitory to EC 3.1.1.7
chlorpyrifos
-
-
chlorpyrifos oxon
-
Michaelis-Menten kinetics, ki: 3048 nM/h, KD: 2.02 nM
chlorpyrifos-oxon
-
-
choline
-
competitive
clomipramine
-
competitive inhibition
cryptotanshinone
uncompetitive inhibitor
CuSO4
-
-
cyclopentyl phenothiazine carbamate
-
-
cyclosarin
cymserine
decamethonium
demethyldebromoflustramine B
-
-
diazoxon
-
second order rate constant for inhibition is 77000000 per M and min
Dibucaine
-
-
dihydrobenzodioxepine cymserine
-
i.e. DHBDC
dihydrotanshinone
uncompetitive inhibitor
diisopropyl fluorophosphate
inhibition, aging, and reactivation kinetics
diisopropyl phosphorofluoridate
-
rank order of decreasing inhibition: soman, sarin, diisopropyl phosphorofluoridate, echothiohate, paraoxon
diisopropylfluorophosphate
-
-
donepezil
Echothiophate
-
an organophosphorous compound, inhibition kinetics, overview
edrophonium
EDTA
-
inhibitory above 1 mM
eptastigmine
eserine
-
native enzyme, 50% inhibition at 5 nM, recombinant enzyme, 50% inhibition at 5 nM
ethopropazine
ethyl 1-(3-(1H-imidazol-1-yl)propyl)-2-(4-nitrophenyl)-1H-benzo[d]imidazole-5-carboxylate
-
best inhibitor
ethyl carbamate
-
-
ethyl carbamoyl
-
native enzyme, 50% inhibition at 10 nM, recombinant enzyme, 50% inhibition at 5 nM
ethylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
fluoride
-
reversible inhibitor, forms a complex with the enzyme
FP-biotin
-
i.e. 10-(fluoroethoxyphosphinyl)-N-(biotinamidopentyl)decanamide, second order rate constant for inhibition is 160000000 per M and min, binding affinity is about 5.8 nM
galantamine
galanthamine
gallic acid
-
48.8% inhibition at 1 mM
genistein
-
65.7% inhibition at 1 mM
HgCl2
-
-
HI 6
-
competitive, reversible
huperzine
-
50% inhibition at 0.03 mM
huperzine A
huprine 19
-
imipramine
-
competitive inhibition
iodine methylated 2-dimethylaminoethyl esters of N-substituted alpha,beta-dehydrophenylalanine
inhibition potencies, overview
-
iso-butylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
iso-ompa
iso-propyl carbamate
-
-
isosorbide-di-(4-nitrophenyl carbamate)
-
-
isosorbide-di-(benzylcarbamate)
-
77% inhibition at 0.1 mM
isosorbide-di-(butylcarbamate)
-
13% inhibition at 0.1 mM
isosorbide-di-(ethylcarbamate)
-
-
isosorbide-di-(propylcarbamate)
-
28% inhibition at 0.1 mM
isosorbide-di-phenylcarbamate
-
77% inhibition at 0.1 mM
K074
-
a bispyridinium para-aldoxime with butane linker, reversible inhibition
K075
-
a bispyridinium para-aldoxime with but-2-ene linker, reversible inhibition
K114
-
a bispyridinium para-aldoxime with xylene-like linker, reversible, noncompetitive inhibition
kaempferol
-
loganin
a mixed-type inhibitor, enzyme interacting residues, overview
luteolin 7-O-rutinoside
-
54.9% inhibition at 1 mM
malachite green
-
linear mixed inhibition
malaoxon
-
-
malathion
-
-
methyl carbamate
-
-
methyl green
-
competitive
methylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
metoclopramide
-
0.001-0.0019 mM, 50% competitive inhibition
metrifonate
-
50% inhibition at 0.018 mM
morphine
-
0.0013 mM, 6% inhibition
morroniside
a mixed-type inhibitor, enzyme interacting residues, overview
myricetin
-
N,N,N-trimethyl-2-([(2Z)-3-phenyl-2-[(phenylcarbonyl)amino]prop-2-enoyl]oxy)ethanaminium iodide
-
N-((1-benzylpiperidin-4-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
-
N-(1,3-thiazol-5-ylcarbamothioyl)butanamide
-
N-(3-ferrocenylphenyl)-2-chlorobenzamide
-
N-(3-ferrocenylphenyl)-2-fluorobenzamide
-
N-(3-ferrocenylphenyl)-2-methoxybenzamide
-
N-(3-ferrocenylphenyl)-2-methylbenzamide
-
N-(3-ferrocenylphenyl)-3-chlorobenzamide
-
N-(3-ferrocenylphenyl)-3-fluorobenzamide
-
N-(3-ferrocenylphenyl)-3-methoxybenzamide
-
N-(3-ferrocenylphenyl)-3-methylbenzamide
-
N-(3-ferrocenylphenyl)-4-chlorobenzamide
-
N-(3-ferrocenylphenyl)-4-fluorobenzamide
-
N-(3-ferrocenylphenyl)-4-methoxybenzamide
-
N-(3-ferrocenylphenyl)-4-methylbenzamide
-
N-(3-ferrocenylphenyl)benzamide
-
N-(4-ferrocenylphenyl)-2-chlorobenzamide
-
N-(4-ferrocenylphenyl)-2-fluorobenzamide
-
N-(4-ferrocenylphenyl)-2-methoxybenzamide
-
N-(4-ferrocenylphenyl)-2-methylbenzamide
-
N-(4-ferrocenylphenyl)-3-chlorobenzamide
-
N-(4-ferrocenylphenyl)-3-fluorobenzamide
-
N-(4-ferrocenylphenyl)-3-methoxybenzamide
-
N-(4-ferrocenylphenyl)-3-methylbenzamide
-
N-(4-ferrocenylphenyl)-4-chlorobenzamide
-
N-(4-ferrocenylphenyl)-4-fluorobenzamide
-
N-(4-ferrocenylphenyl)-4-methoxybenzamide
-
N-(4-ferrocenylphenyl)-4-methylbenzamide
-
N-(4-ferrocenylphenyl)benzamide
-
N-butyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
n-butylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
N-ethyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
N-hexyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine
-
-
N-hexyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
-
-
N-methyl, N-alkyl carbamates
-
inhibition of human BChE by divers derivatives of phenylethylamines and aminoindans is less influenced by the size of the alkyl group and more dependent on the structure of the leaving group, overview
-
N-methyl-7-exo-(benzylaminocarbonyloxy-)-3-oxo-5,9-dioxa-2-azabicyclo[4.3.0] nonane
-
6.5% inhibition at 0.1 mM
N-methyl-N-(3-carbamoyloxyphenyl)methyl-amino inhibitor
-
-
N-methylphenothiazine
-
not inhibitory to EC 3.1.1.7
n-propylsarin
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
N-[(1-benzylpiperidin-3-yl)methyl]-N-(2-methoxyethyl)naphthalene-2-sulfonamide
the inhibitor is highly selective for BChE versus acetylcholinesterase, AChE
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-[[1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl]methyl]-N-(2-methoxyethyl)naphthalene-2-carboxamide
the inhibitor is highly selective for BChE versus acetylcholinesterase, AChE. It is a potent, selective, and reversible slow tight-binding inhibitor of human BChE
NaCl
-
-
naringin
-
13.7% inhibition at 1 mM
neostigmine
neostigmine bromide
-
-
O,O-diethyl-4-nitrophenylphosphate
-
syn: paraoxon, rank order of decreasing inhibition: soman, sarin, diisopropyl phosphorofluoridate, echothiohate, paraoxon
O,O-diethyl-S-(2-N,N,N-trimethylammonioethyl) phosphorothiolate iodide
-
syn: echothiophate, rank order of decreasing inhibition: soman, sarin, diisopropyl phosphorofluoridate, echothiohate, paraoxon
O-ethyl S-2-diisopropylaminoethyl methyl phosphonothiolate
VX, a highly toxic chemical warfare agent, inhibition of butyrylcholinesterase (BChE) activity by VX is due to formation of a phosphorylated BChE adduct
O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate
nerve agent VX
O-isopropyl methylphosphonofluoridate
-
syn: sarin, rank order of decreasing inhibition: soman, sarin, diisopropyl phosphorofluoridate, echothiohate, paraoxon
O-pinacolyl methylphosphonofluoridate
-
syn: soman, rank order of decreasing inhibition: soman, sarin, diisopropyl phosphorofluoridate, echothiohate, paraoxon
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
-
PAM-2
-
competitive, reversible
paraoxon
pararosaniline
-
linear mixed inhibition
parathion
paroxetine
-
mixed-type inhibition
phenethyl cymserine
-
native enzyme, 50% inhibition at 7 nM, recombinant enzyme, 50% inhibition at 50 nM
phenothiazine
phenserine
phenyl phenothiazine carbamate
-
-
phenyl trimethyl ammonium
-
specific inhibitor
phenylcoumarin
-
-
phenylethylcymserine
-
inhibition in the nanomolar range
phosphostigmine
-
competitive, reversible
physostigmine
pralidoxime
-
procainamide
-
specific inhibitor
propidium
propionylthiocholine
-
substrate inhibition above 10 mM
propyl phenothiazine carbamate
-
-
prostigmin
-
-
pyridostigmine
pyridostigmine bromide
-
native enzyme, 50% inhibition at 300 nM, recombinant enzyme, 50% inhibition at 500 nM
quercetin
quinidine
-
0.007 mM, 5.7% inhibition
rac-bambuterol monocarbamate
inhibition kinetics of human and dog plasma butyrylcholinesterase by bambuterol and bambuterol monocarbamate enantiomers
rivastigmine
Ro 02-0683
-
progressive inhibitor
sarin
sertraline
-
mixed-type inhibition
silibinin
-
51.4% inhibition at 1 mM
silymarin
-
43.2% inhibition at 1 mM
Sodium fluoride
-
-
soman
-
a methylfluorophosphonate, enzyme reactivation by oximes, overview
Succinylcholine
-
-
Tabun
tacrine
tert-butyl 10H-phenothiazine-10-carboxylate
-
-
tetra monoisopropyl pyrophosphomide
-
50% inhibition at 0.055 mM
tetra(monoisopropyl) diphosphortetramide
-
i.e. iso-OMPA
tetra(monoisopropyl)diphosphortetramide
irreversible
tetraethylammonium
-
-
tetraisopropyl diphosphoramide
Tetramethylammonium
-
-
thioflavin T
binding structure from analysis of the crystal structure, PDB ID 6ESY, inhibition kinetics and thermodynamics, overview
thioridazine
-
0.0054 mM, 10% inhibition
tolserine
-
native enzyme, 50% inhibition at 50 nM, recombinant enzyme, 50% inhibition at 80 nM
tolserine N-dimethyl ammonium bromide
-
native enzyme, 50% inhibition at 44 nM, recombinant enzyme, 50% inhibition at 45 nM
trimedoxime
-
VX (nerve agent)
-
a nerve agent
xanthostigmine
Zn2+
-
1-2 mM, 10% activation, inhibitory above
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetylthiocholine
-
Butyrylcholine
-
substrate activation, overview
butyrylthiocholine
-
homocysteine thiolactone
-
non-substrate activation
propionylthiocholine
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
107
(+)-cocaine
-
pH 7.4, 25°C
0.0031 - 0.065
(-)-cocaine
0.12 - 1.9
2-Nitrophenyl butyrate
8.6
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
0.027 - 0.148
Acetylcholine
0.029 - 0.96
acetylthiocholine
0.057 - 1.476
acetylthiocholine iodide
0.00301
BChE-FP
-
pH 7.0, 30°C
0.003 - 0.024
Benzoylcholine
0.00295 - 0.0592
benzoylthiocholine
0.021
butyryl thiocholine
-
pH 7, 22°C, native and intermediate state of the enzyme
0.0256
butyryl thiocholine iodide
-
pH 7, mutant with only 5 N-glycosylation sites
0.0083 - 6
butyrylthiocholine
0.042 - 0.434
cocaine
0.12
heroin
recombinant enzyme, pH 7.4, 37°C
0.00008 - 0.002
N-methyl-(7-dimethylcarbamoxy)quinolinium iodide
0.066 - 0.162
N-methylindoxyl acetate
0.14
o-nitrophenylbutyrate
-
usual and atypical enzyme
0.017 - 0.76
propionylthiocholine
0.003 - 11
succinylthiocholine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0085
(+)-cocaine
-
pH 7.4, 25°C
0.009 - 6.08
(-)-cocaine
250 - 600
2-Nitrophenyl butyrate
0.0042
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
125 - 1433
Acetylcholine
38.3 - 336.7
acetylthiocholine
1.75
BChE-FP
-
pH 7.0, 30°C
14.7 - 303
Benzoylcholine
0.82 - 21.6
benzoylthiocholine
535
butyryl thiocholine iodide
-
pH 7, mutant with only 5 N-glycosylation sites
0.016 - 1050
butyrylthiocholine
386.8 - 418.3
cocaine
30.67
heroin
recombinant enzyme, pH 7.4, 37°C
0.0000417
N-methyl-(7-dimethylcarbamoxy)quinolinium iodide
-
usual and atypical enzyme
200 - 300
N-methylindoxyl acetate
800
o-nitrophenylbutyrate
-
usual and atypical enzyme
53.3
propionylthiocholine
recombinant enzyme, pH 8.0, 22°C
3 - 6
succinylthiocholine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.19
(-)-cocaine
recombinant enzyme, pH 7.4, 37°C
0.0005
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
3000 - 9667
Acetylcholine
1235.5 - 11500
acetylthiocholine
1087
BChE-FP
-
pH 7.0, 30°C
3333.3 - 56670
butyrylthiocholine
255.56
heroin
recombinant enzyme, pH 7.4, 37°C
3135.3
propionylthiocholine
recombinant enzyme, pH 8.0, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0085
(+)-cocaine
-
pH 7.4, 25°C
0.009
(-)-cocaine
-
pH 7.4, 37°C
0.0756
(-)-huperzine A
pH 8.0, 22°C
0.0008 - 0.12
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
0.00177
1,3-bis[5(diethyl-o-nitrobenzylammonium)pentyl]-6-methyluracil dibromide
pH and temperature not specified in the publication
0.0019
1,5-bis(4-allyldimethylammoniumphenyl)pentan-3-one dibromide
pH 8.0, 22°C
0.00633
10-(2,2-dimethylpropanoyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00643
10-(2-ethylbutanoyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00359
10-(3,3-dimethylbutanoyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00646
10-(3-methylbutanoyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0109
10-(chloroacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0048
10-(cyclobutylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00086
10-(cycloheptylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00168
10-(cyclohexylacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00126
10-(cyclohexylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00222
10-(cyclopentylacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.00421
10-(cyclopentylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0231
10-(cyclopropylcarbonyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0296
10-(methoxyacetyl)-10H-phenothiazine
-
pH 8.0, 23°C
0.0358
10-acetyl-10H-phenothiazine
-
pH 8.0, 23°C
0.0162
10-butyryl-10H-phenothiazine
-
pH 8.0, 23°C
0.00831
10-heptanoyl-10H-phenothiazine
-
pH 8.0, 23°C
0.00637
10-hexanoyl-10H-phenothiazine
-
pH 8.0, 23°C
0.0132
10-isobutyryl-10H-phenothiazine
-
pH 8.0, 23°C
0.0102
10-pentanoyl-10H-phenothiazine
-
pH 8.0, 23°C
0.0256
10-propionyl-10H-phenothiazine
-
pH 8.0, 23°C
0.0032
2-(1-piperidinyl)ethyl phenothiazine carbamate
-
23°C
0.00065
2-(1-pyrrolidinyl)ethyl phenothiazine carbamate
-
23°C
0.0024
2-(4-morpholino)ethyl phenothiazine carbamate
-
23°C
0.0006
2-(diethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
23°C
0.0025
2-(dimethylamino)ethyl 10H-phenothiazine-10-carboxylate
-
23°C
0.00074
3-(diethylamino)propyl 10H-phenothiazine-10-carboxylate
-
23°C
0.273
4-carbamoyl-1-(3-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
pH 7.4, 25°C
0.14
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
pH 7.4, 25°C
0.195
4-carbamoyl-1-(4-(3,5-dichloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)propyl)pyridinium
pH 7.4, 25°C
0.265
4-carbamoyl-1-(4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)butyl)pyridinium
pH 7.4, 25°C
0.187
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
0.294
4-carbamoyl-1-[(2E)-4-(3-chloro-4-[(hydroxyimino)methyl]-pyridinium-1-yl)but-2-en-1-yl]pyridinium
pH 7.4, 25°C
0.13502
7-O-galloyl-D-sedoheptulose
pH and temperature not specified in the publication
0.0374
apigenin
-
0.215
asoxime
pH 7.4, 25°C
0.0032 - 0.007
Benzoylcholine
0.0322
chlorpromazine
-
pH 8.0, 23°C
11 - 15.89
choline
0.0032
cyclopentyl phenothiazine carbamate
-
23°C
38
cymserine
-
pH 7.0, 25°C
0.0008 - 0.0045
decamethonium
0.049 - 0.0504
edrophonium
0.00000088 - 0.00000174
eserine
0.000051 - 0.000166
ethopropazine
0.0234
ethyl carbamate
-
23°C
0.0000071 - 0.000023
ethyl carbamoyl
0.09
fisetin
-
0.0069
galangin
-
0.0181
iso-propyl carbamate
-
23°C
0.127
K074
-
-
0.338
K075
-
-
0.059
K114
-
-
0.043
kaempferol
-
0.06935
loganin
pH and temperature not specified in the publication
0.166
luteolin
-
0.00028
malachite green
-
25°C, pH 8.0
0.0102
methyl carbamate
-
23°C
0.00012
methyl green
-
25°C, pH 8.0
0.001 - 0.0019
metoclopramide
-
competitive inhibition
0.09506
morroniside
pH and temperature not specified in the publication
0.071
myricetin
-
0.0134
n-butyl carbamate
-
23°C
0.0369
N-methylphenothiazine
-
pH 8.0, 23°C
0.0019
pararosaniline
-
25°C, pH 8.0
0.0000152 - 0.0000356
phenethyl cymserine
0.0318
phenothiazine
-
pH 8.0, 23°C
0.000655 - 0.0013
phenserine
0.39
pralidoxime
pH 7.4, 25°C
0.0004 - 0.00043
propidium
0.26
propyl phenothiazine carbamate
-
23°C
0.00046 - 0.000616
pyridostigmine bromide
0.068
quercetin
-
0.5
rutin
-
0.0012 - 0.005
Succinylcholine
0.000008 - 0.00001069
tacrine
0.0043
tert-butyl 10H-phenothiazine-10-carboxylate
-
23°C
0.00005
tetra(monoisopropyl)diphosphortetramide
pH 8.0, 22°C
2 - 400
tetraethylammonium
4 - 600
Tetramethylammonium
0.0008
thioflavin T
pH and temperature not specified in the publication
0.000073 - 0.000139
tolserine
0.00009
tolserine N-dimethyl ammonium bromide
-
22°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
(+)-debromoflustramine B
Homo sapiens
-
-
0.00041
(+/-)-6-bromo-N-((1-(2,3-dihydro-1H-inden-2-yl)-piperidin-3-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.000067
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-1-naphthamide
Homo sapiens
pH 8.0, 25°C
0.00000103
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.00003824
(+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(3-methoxypropyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.000632
(+/-)-N-((1-(benzo[d]thiazol-2-ylmethyl)piperidin-3-yl)methyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.001437
(+/-)-N-((1-benzylpiperidin-3-yl)methyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.00023
(+/-)-N-((1-benzylpiperidin-3-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.00137
(-)-debromoflustramine B
Homo sapiens
-
-
0.000137
(2x)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-([[(2E)-3-phenylprop-2-enoyl]oxy]carbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000072
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(2-methylbutanoyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000012
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(biphenyl-4-ylcarbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000006
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(cyclopentylcarbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000334
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(cyclopropylcarbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0000043
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-(phenoxycarbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.00036
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-([[(trifluoromethyl)sulfonyl]oxy]carbonyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000073
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(2H-chromen-2-yloxy)carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000669
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(3,4-dihydroxyphenyl)carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0007
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(pentanoyloxy)carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.00098
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[(propanoyloxy)carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0028
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[([[4-(heptyloxy)phenyl]carbonyl]oxy)carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000032
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(naphthalen-2-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.00057
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(pyridin-3-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.000088
(2xi)-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-[[(pyridin-4-ylcarbonyl)oxy]carbonyl]-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0037
(2xi)-1,4:3,6-dianhydro-2-O-([2-[(carbamoyloxy)methyl]-5-hydroxybenzyl]carbamoyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0041
(2xi)-5-O-[(acetyloxy)carbonyl]-1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-D-arabino-hexitol
Homo sapiens
pH 7.4, 37°C
0.0888
(3,4-dimethoxyphenyl)-(4-([(2-dimethylaminoethyl)-methylamino]methyl)phenyl)-methanone
Homo sapiens
-
pH 8.0, 37°C
0.0162
(3,4-dimethoxyphenyl)-(4-([(2-methoxybenzyl)methylamino]methyl)phenyl)-methanone
Homo sapiens
-
pH 8.0, 37°C
0.125
(3,4-dimethoxyphenyl)-(4-([methyl-(3-methylbenzyl)amino]methyl)phenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.1
(3,4-dimethoxyphenyl)-(4-([methyl-(3-nitrobenzyl)amino]methyl)phenyl)methanone
Homo sapiens
-
above, pH 8.0, 37°C
0.0332
(4-([benzyl-(2-dimethylaminoethyl)amino]methyl)-phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.172
(4-([benzyl-(2-hydroxyethyl)amino]methyl)phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0715
(4-[(benzylethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.0607
(4-[(benzylmethylamino)methyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.1
(4-[(benzylmethylamino)methyl]phenyl)-(3-fluoro-4-methoxyphenyl)methanone
Homo sapiens
-
pH 8.0, 37°C
0.1
(4-[(benzylmethylamino)methyl]phenyl)-(4-methoxyphenyl)methanone
Homo sapiens
-
above, pH 8.0, 37°C
0.044
(4-[3-(benzylmethylamino)propenyl]phenyl)-(3,4-dimethoxyphenyl)methanone
Homo sapiens
-
above, pH 8.0, 37°C
0.541
1,1'-(2E)-but-2-ene-1,4-diyldipyridinium dibromide
Homo sapiens
-
-
1.27
1,1'-(2Z)-but-2-ene-1,4-diyldipyridinium dichloride
Homo sapiens
-
-
0.345
1,1'-(benzene-1,2-diyldimethanediyl)dipyridinium dibromide
Homo sapiens
-
-
1.38
1,1'-(benzene-1,3-diyldimethanediyl)dipyridinium dibromide
Homo sapiens
-
-
0.529
1,1'-(benzene-1,4-diyldimethanediyl)dipyridinium dibromide
Homo sapiens
-
-
0.0008
1,1'-(naphthalene-2,7-diyldimethanediyl)dipyridinium dibromide
Homo sapiens
-
-
2.36
1,1'-(oxydiethane-2,1-diyl)dipyridinium dibromide
Homo sapiens
-
-
0.583
1,1'-(oxydimethanediyl)dipyridinium dichloride
Homo sapiens
-
-
9.8
1,1'-butane-1,4-diyldipyridinium dibromide
Homo sapiens
-
-
0.005
1,1'-decane-1,10-diyldipyridinium dibromide
Homo sapiens
-
-
0.078
1,1'-heptane-1,7-diyldipyridinium dibromide
Homo sapiens
-
-
0.13
1,1'-hexane-1,6-diyldipyridinium dibromide
Homo sapiens
-
-
0.006
1,1'-nonane-1,9-diyldipyridinium dibromide
Homo sapiens
-
-
0.029
1,1'-octane-1,8-diyldipyridinium dibromide
Homo sapiens
-
-
0.12
1,1'-pentane-1,5-diyldipyridinium dibromide
Homo sapiens
-
-
0.007
1,1'-undecane-1,11-diyldipyridinium dibromide
Homo sapiens
-
-
0.00172
1,3a,8-tris(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.000051
1,4:3,6-dianhydro-2-O-(benzylcarbamoyl)-5-O-nitro-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.000894
1,4:3,6-dianhydro-2-O-(butylcarbamoyl)-5-O-nitro-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.0025
1,4:3,6-dianhydro-2-O-(cyclohexylcarbamoyl)-5-O-nitro-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.0039
1,4:3,6-dianhydro-2-O-(ethylcarbamoyl)-5-O-nitro-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.0051
1,4:3,6-dianhydro-2-O-(methylcarbamoyl)-5-O-nitro-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.000639
1,4:3,6-dianhydro-2-O-nitro-5-O-(propylcarbamoyl)-D-threo-hexitol
Homo sapiens
pH 7.4, 37°C
0.04998
1-benzyl-5-methoxy-3a,8-bis(3-methylbut-2-enyl)-1,2,3,3a,8,8ahexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.121
1-butanoyl-3-(2,6-dimethylphenyl) thiourea
Homo sapiens
pH 7.7, 37°C
0.00696
1-butanoyl-3-(3-methoxyphenyl)thiourea
Homo sapiens
pH 7.7, 37°C
0.0162
1-butanoyl-3-(4-chlorophenyl)thiourea
Homo sapiens
pH 7.7, 37°C
0.113
1-butanoyl-3-benzylthiourea
Homo sapiens
pH 7.7, 37°C
0.01808
1-[2-(4-carboxyphenyl)-5-(ethoxycarbonyl)-1H-benzimidazol-1-yl]-4-ethylmorpholin-1-ium
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.000113
2,3-dimethoxy-6-methyl-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0000637
2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000016
2-(4-(((7-(diethylamino)-2,4-dioxo-2H-chromen-3(4H)-ylidene)methyl)amino)phenyl)-N'-1,2,3,4-tetrahydroacridin-9-ylacetohydrazide
Homo sapiens
-
-
0.0000702
2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000028
2-(benzylaminocarbonyloxy-)-5-O-(1-naphthoyl)-1,4:3,6-dianhydro-D-glucitol
Homo sapiens
pH 7.4, 37°C
0.0011
2-(dimethylamino)ethyl (2Z)-2-[[(2-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.00414
2-(dimethylamino)ethyl (2Z)-2-[[(2-chlorophenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0006
2-(dimethylamino)ethyl (2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0025
2-(dimethylamino)ethyl (2Z)-2-[[(3-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0138
2-(dimethylamino)ethyl (2Z)-2-[[(4-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0402
2-(dimethylamino)ethyl (2Z)-2-[[(4-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0028
2-(dimethylamino)ethyl (2Z)-3-phenyl-2-[(phenylcarbonyl)amino]prop-2-enoate
Homo sapiens
pH 7.6, 25°C
0.0009
2-[[(2Z)-2-[[(2-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.0013
2-[[(2Z)-2-[[(2-chlorophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.00008
2-[[(2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium
Homo sapiens
pH 7.6, 25°C
0.00015
2-[[(2Z)-2-[[(2-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.0017
2-[[(2Z)-2-[[(3-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.0146
2-[[(2Z)-2-[[(4-bromophenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.0327
2-[[(2Z)-2-[[(4-methoxyphenyl)carbonyl]amino]-3-phenylprop-2-enoyl]oxy]-N,N,N-trimethylethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.0000807
3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000594
3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000165
3-([7-[methyl(3-[[(methylamino)oxy]carbonyl]benzyl)amino]heptyl]oxy)-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0000762
3-methoxy-6-methyl-9H-xanthen-9-one
Homo sapiens
-
pH 8.0, 37°C
0.0000793
3-methyl-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.0165
3-[(methyl[7-[(9-oxo-9H-xanthen-3-yl)oxy]heptyl]amino)methyl]phenyl methylcarbamate
Homo sapiens
-
-
0.0001
3-[10-(benzylmethylamino)decyloxy]xanthen-9-one
Homo sapiens
-
-
0.00012
3-[11-(benzylmethylamino)undecyloxy]xanthen-9-one
Homo sapiens
-
-
0.00015
3-[12-(benzylmethylamino)dodecyloxy]xanthen-9-one
Homo sapiens
-
-
0.01144
3-[2-(4-carboxyphenyl)-5-(ethoxycarbonyl)-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.00833
3-[3-(benzylmethylamino)propoxy]xanthen-9-one
Homo sapiens
-
-
0.00191
3-[3-[(2-methoxybenzyl)methylamino]propoxy]-xanthen-9-one
Homo sapiens
-
-
0.00265
3-[4-(benzylmethylamino)butoxy]xanthen-9-one
Homo sapiens
-
-
0.00249
3-[5-(benzylmethylamino)pentyloxy]xanthen-9-one
Homo sapiens
-
-
0.00681
3-[5-(ethoxycarbonyl)-2-(4-hydroxyphenyl)-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.00659
3-[5-(ethoxycarbonyl)-2-[4-(trifluoromethyl)phenyl]-1H-benzimidazol-1-yl]-1-propyl-1H-imidazol-3-ium
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.00143
3-[6-(benzylmethylamino)hexyloxy]xanthen-9-one
Homo sapiens
-
-
0.0008
3-[7-(benzylmethylamino)-heptyloxy]xanthen-9-one
Homo sapiens
-
-
0.0461
3-[7-(benzylmethylamino)heptyloxy]-6-methoxyxanthen-9-one
Homo sapiens
-
-
0.00201
3-[7-[(2,3-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
Homo sapiens
-
-
0.00127
3-[7-[(2,5-dimethoxybenzyl)methylamino]heptyloxy]xanthen-9-one
Homo sapiens
-
-
0.269
3-[7-[(2-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.00093
3-[7-[(2-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.0638
3-[7-[(3-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.00185
3-[7-[(3-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.127
3-[7-[(4-chlorobenzyl)methylamino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.00211
3-[7-[(4-methoxybenzyl)methylamino]heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.00032
3-[7-[ethyl-(2-methoxybenzyl)amino]heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.001
3-[7-[methyl-(2,3,4-trimethoxybenzyl)amino]-heptyloxy]xanthen-9-one
Homo sapiens
-
-
0.0295
3-[7-[methyl-(2-methylbenzyl)amino]-heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.014
3-[7-[methyl-(2-nitrobenzyl)amino]heptyloxy]-xanthen-9-one
Homo sapiens
-
-
0.00008
3-[8-(benzylmethylamino)octyloxy]xanthen-9-one
Homo sapiens
-
-
0.0001
3-[9-(benzylmethylamino)nonyloxy]xanthen-9-one
Homo sapiens
-
-
0.0221
3a,8-dibenzyl-1-methyl-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.00589
3a,8-dibenzyl-5-methoxy-1-methyl-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.00459
5-methoxy-1-methyl-3a,8-bis(3-methylbut-2-en-1-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.000072
6,7-dimethoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.0000448
6,7-dimethoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.000295
6,7-dimethoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000652
6-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000091
6-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.0000815
6-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000383
6-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.00308
6-[7-(benzylmethylamino)heptyloxy]-2,3-dimethoxyxanthen-9-one
Homo sapiens
-
-
0.0000574
7-methoxy-2-(3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.000107
7-methoxy-2-(4-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH 8.0, 37°C
0.0000415
7-methoxy-3-(3-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.0000723
7-methoxy-3-(4-methylphenyl)-2H-chromen-2-one
Homo sapiens
-
pH 8.0, 37°C
0.00036
7-methoxy-N-nonyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride (1:1)
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
7-methoxy-N-octyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.016
7-methoxy-N-pentyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.07
7-methoxy-N-propyl-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.08794
7-O-galloyl-D-sedoheptulose
Homo sapiens
pH and temperature not specified in the publication
0.01
8-benzyl-1-methyl-3a-(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.00754
8-benzyl-5-methoxy-1-methyl-3a-(3-methylbut-2-enyl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole
Homo sapiens
-
-
0.021
9-amino-7-methoxy-1,2,3,4-tetrahydroacridine
Homo sapiens
-
pH and temperature not specified in the publication
0.00058
amberboin
Homo sapiens
pH and temperature not specified in the publication
0.00685
Berberine
Homo sapiens
pH and temperature not specified in the publication
0.00666
cryptotanshinone
Homo sapiens
pH and temperature not specified in the publication
0.00026
demethyldebromoflustramine B
Homo sapiens
-
-
0.00551
dihydrotanshinone
Homo sapiens
pH and temperature not specified in the publication
0.00714 - 0.00795
donepezil
0.00512
ethyl 1-(3-(1H-imidazol-1-yl)propyl)-2-(4-nitrophenyl)-1H-benzo[d]imidazole-5-carboxylate
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.008 - 6.6
galantamine
0.00099
huprine 19
Homo sapiens
pH 7.0, 25°C, recombinant enzyme
0.0054
isosorbide-di-(4-nitrophenyl carbamate)
Homo sapiens
-
-
0.0065
isosorbide-di-(ethylcarbamate)
Homo sapiens
-
-
0.03302
loganin
Homo sapiens
pH and temperature not specified in the publication
0.03778
morroniside
Homo sapiens
pH and temperature not specified in the publication
0.0031
N,N,N-trimethyl-2-([(2Z)-3-phenyl-2-[(phenylcarbonyl)amino]prop-2-enoyl]oxy)ethanaminium iodide
Homo sapiens
pH 7.6, 25°C
0.000702
N-((1-benzylpiperidin-4-yl)methyl)-N-(2-methoxyethyl)-2-naphthamide
Homo sapiens
pH 8.0, 25°C
0.0365
N-(1,3-thiazol-5-ylcarbamothioyl)butanamide
Homo sapiens
pH 7.7, 37°C
0.015
N-(3-ferrocenylphenyl)-2-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.009
N-(3-ferrocenylphenyl)-2-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.014
N-(3-ferrocenylphenyl)-2-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.013
N-(3-ferrocenylphenyl)-2-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.015
N-(3-ferrocenylphenyl)-3-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.014
N-(3-ferrocenylphenyl)-3-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.009
N-(3-ferrocenylphenyl)-3-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.012
N-(3-ferrocenylphenyl)-3-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.014
N-(3-ferrocenylphenyl)-4-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.014
N-(3-ferrocenylphenyl)-4-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.013
N-(3-ferrocenylphenyl)-4-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.01
N-(3-ferrocenylphenyl)-4-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.013
N-(3-ferrocenylphenyl)benzamide
Homo sapiens
pH 7.6, 37°C
0.016
N-(4-ferrocenylphenyl)-2-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.015
N-(4-ferrocenylphenyl)-2-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.021
N-(4-ferrocenylphenyl)-2-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.016
N-(4-ferrocenylphenyl)-2-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.025
N-(4-ferrocenylphenyl)-3-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.024
N-(4-ferrocenylphenyl)-3-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.024
N-(4-ferrocenylphenyl)-3-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.021
N-(4-ferrocenylphenyl)-3-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.021
N-(4-ferrocenylphenyl)-4-chlorobenzamide
Homo sapiens
pH 7.6, 37°C
0.021
N-(4-ferrocenylphenyl)-4-fluorobenzamide
Homo sapiens
pH 7.6, 37°C
0.016
N-(4-ferrocenylphenyl)-4-methoxybenzamide
Homo sapiens
pH 7.6, 37°C
0.024
N-(4-ferrocenylphenyl)-4-methylbenzamide
Homo sapiens
pH 7.6, 37°C
0.017
N-(4-ferrocenylphenyl)benzamide
Homo sapiens
pH 7.6, 37°C
0.064
N-butyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.097
N-ethyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N-hexyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
N-hexyl-7-methoxy-1,2,3,4-tetrahydroacridin-9-amine hydrochloride
Homo sapiens
-
pH and temperature not specified in the publication
0.00000491
N-[(1-benzylpiperidin-3-yl)methyl]-N-(2-methoxyethyl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.0, 25°C
0.15
N-[(2,3-dichlorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0439
N-[(2,4,6-trimethylphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0155
N-[(2,4-dichlorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0231
N-[(2,6-dichloro-4-fluorophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0758
N-[(2-methoxyphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0645
N-[(3-nitrophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0741
N-[(4-methoxyphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0366
N-[(4-methylphenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0681
N-[(4-nitrophenyl)carbamothioyl]butanamide
Homo sapiens
pH 7.7, 37°C
0.0000213
N-[[1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl]methyl]-N-(2-methoxyethyl)naphthalene-2-carboxamide
Homo sapiens
pH 8.0, 25°C
0.0008 - 0.0496
neostigmine
16
pyridostigmine
Homo sapiens
-
-
0.00259
rac debromoflustramine B
Homo sapiens
-
-
0.00037 - 0.022
rivastigmine
0.000012 - 0.000023
tacrine
0.000048 - 0.048
xanthostigmine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0011
-
BChE activity in colon cancer
0.0026
-
BChE activity in kidney
0.003
-
BChE activity in colon
0.0291
-
BChE activity in blood serum
260
purified recombinant enzyme, pH 7.4, 25°C
630
purified recombinant truncated enzyme, pH 7.0, 25°C
685
-
purified enzyme from plasma
760
-
purified enzyme from Cohn Fraction IV-4
97
-
benzoylcholine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7 - 8
7.3
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
enzyme retains activity at pH 5 and below under conditions of excess substrate activation
5.5 - 8.5
6 - 8.5
-
increasing activity with increasing pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
24
-
assay at
30
-
assay at
37 - 42
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
non-small lung carcinoma
Manually annotated by BRENDA team
-
endogenous BChE is located in the cytoplasm of PANC-1 cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
compound C547 and pyridostigmine show efficiency to reduce muscle weakness symptoms and ability to activate contractions of urinary bladder in a rat model of autoimmune myasthenia gravis (MG). At a dose effectively reducing MG symptoms, C547 does not affect activity of rat urinary bladder, while at equipotent dose, pyridostigmine causes a significant increase in tonus and force of spontaneous contractions of bladder wall
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHLE_HUMAN
602
2
68418
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A024CHX5_HUMAN
113
2
12889
TrEMBL
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
280000
-
gel filtration
340000
366000
-
ultracentrifugation, density gradient
70000 - 75000
-
SDS-PAGE, recombinant enzyme
85000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
-
monomer
oligomer
-
BChE forms monomers, dimers and tetramers
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with echothiophate before and after suicide aging reaction and with diisopropyl-fluorophosphate after aging
in complex with tacrine, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 2.1 M ammonium sulfate
monomeric enzyme, lacking four out of nine N-glycosylation sites and the C-terminal oligomerization domain, hanging drop vapor diffusion method
-
mutant enzyme G117H without additives and bound to MgF3-, sulfate, echothiophate, or VX, hanging drop vapor diffusion method
purified enzyme human BChE in complex with the reversible ligands, decamethonium, thioflavin T, propidium, huprine, and ethopropazine, crystals of the BChES2-propidium complex were grown by cocrystallization in the presence of 1 mM ligand. The structure of the complex is solved at 3.0 A resolution, the structure of enzyme-decamethonium is solved at 2.3 A resolution, crystals of the BChECHO-ethopropazine complex are grown by cocrystallization in the presence of 1 mM ligand, the structure is solved at 2.35 A resolution
purified enzyme in complex with inhibitor (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide, hanging drop vapour diffusion method, preincubation of 0.5 mM (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide dichloride in 1% dimethylsulfoxide aqueous solution with the enzyme solution (0.090 mM) for 3 h, X-ray diffraction structure determination and analysis at 2.1 A resolution, modeling
purified recombinant enzyme, 8 mg/ml protein in 50 mM Tris-HCl and 10 mM MES, pH 8.0, sitting drop vapour diffusion method, 20°C, 0.005 ml protein solution are mixed with 0.001 ml of reservoir solution containing at least 1.6 M ammonium sulfate and other additives, e.g. 0.2 M diammonium phosphate, 0.2 M ammonium iodide, and 0.5 M lithium chloride, two different crystal forms are obtained, X-ray diffraction structure determination and analysis at 2.8-4.6 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A184V
-
naturally occuring mutation in exon 2
A199S/F227A/S287G/A328W/E441D
-
the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A199S/F227A/S287G/A328W/Y332G/E441D
-
the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A199S/S287G/A328W/Y332G
-
the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A277W
-
mutation does not affect binding of E2020
A328C
-
the mutation leads to hysteresis with butyrylthiocholine
A328F
A328G
-
mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328I
-
mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328W
A328W/Y332A
A328Y
A539T
D70G/Y332A
-
catalytic activity similar to wild-type enzyme
D79G
-
increased Km
E197D
-
moderately reduced substrate activation
E197G
-
strongly reduced substrate activation
E197Q
E255D
-
naturally occuring mutation in exon 2
E497V/A539T
-
J-variant
E797V
-
catalytic activity similar to wild-type enzyme
F329A
-
the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
G115D
-
naturally occuring mutation in exon 2
G117H
G117H/A199E
-
the mutation leads to hysteresis with benzoylthiocholine
G117H/E197Q
-
the double mutant does not age after phosphonylation with soman
G135D
-
unstable variant BChE115D
G328G
-
retained substrate activation
G333C
-
naturally occuring mutation, the mutant shows about 80% decreases enzyme activity compared to the wild-type enzyme
G390V
-
naturally occuring mutation in exon 2
K12R
-
naturally occuring mutation in exon 2
K339M
-
retained substrate activation
L286W
-
mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
N83A
-
loss of substrate activation
N83Q
-
loss of substrate activation
Q119Y
-
altered Ki for E2020
Q119Y/V288F/A328Y
-
altered Ki for E2020
R470W
-
naturally occuring mutation in exon 2
S198C
-
site-directed mutagenesis, inactive catalytic site mutant
S198D
-
site-directed mutagenesis, inactive catalytic site mutant
T234M
-
naturally occuring mutation in exon 2
V288F
-
Ki for E2020 similar to wild-type enzyme
V288W
-
mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
V294M
-
naturally occuring mutation in exon 2
W430A
-
retained substrate activation, strongly reduced affinity for tetramethylammonium, bimolecular rate constant for reaction with diisopropyl fluorophosphate is reduced 10000fold
Y332A
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30% loss of activity after 24 h in Tris buffer pH 8
40
-
incubation for 24 h inactivates the enzyme, 25% loss of activity after 24 h, enzyme can not be reactivated at 4°C
55
-
25% remaining activity after 25 min, heat inactivation is retarded in the presence of 2 mM fluoride
60 - 120
-
thermal inactivation rate of BChE at different temperatures, bi-exponential decay equation, inactivation kinetics, overview
67
-
1 min, complete loss of activity in water and deuterium oxide
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
half-life of wild-type enzyme in culture: 1.41h, half-life of A539T mutant enzyme in culture: 1.55h, half-life of E497V/A539T mutant enzyme in culture: 1.49h
-
pressure and heat lead to inactivation of the enzyme by irreversible formation of an active intermediate state and a denatured state
-
stabilized by glycerol, polythylene glycol, or ammonium sulfate, all best at 20% w/v
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, lyophilized enzyme, stable for at least 2 years
-
25°C, lyophilized enzyme, stable for at least 2 years
-
30°C, 20% w/v ammonium sulfate, 12 weeks, 62% loss of activity
-
30°C, 20% w/v glycerol, 12 weeks, 38% loss of activity
-
30°C, 20% w/v polyethylene glycol 6000, 12 weeks, 20% loss of activity
-
37°C, lyophilized enzyme, stable for at least 2 years
-
45°C, lyophilized enzyme, stable for at least 2 years
-
4°C, 20% w/v ammonium sulfate, 12 weeks, no loss of activity
-
4°C, 20% w/v glycerol, 12 weeks, no loss of activity
-
4°C, 20% w/v polyethylene glycol 6000, 12 weeks, no loss of activity
-
4°C, lyophilized enzyme, stable for at least 2 years
-
4°C, purified enzyme, 2 months, loss of about 15% of activity
-
the purified recombinant enzyme is stable during storage at 4°C in 20 mM potassium phosphate, 1 mM EDTA, pH 7.0, containing 0.02% NaN3
unstable variant BChE115D loses activity upon freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
6600fold
-
atypical and typical enzyme
-
native enzyme by a single step procainamide affinity chromatography purification
-
native enzyme from outdated plasma or Cohn Fraction IV-4, large scale, method development, optimization, and evaluation, involving procainamide adsorption chromatography, dialysis, and anion exchange chromatography to 95% purity to homogeneity
-
native enzyme is purified from Cohn fraction IV-4 paste
QFF resin anion-exchange chromatography and Hypatite C column chromatography
-
recombinant C-terminally truncated enzyme BChE from CHO-S cells by affinity chromatography
recombinant enzyme from C57BL/6 mice serum by dialysis, anion exchange chromatography, desalting gel filtration, and procainamide affinity chromatography, followed by ultrafiltration
recombinant extracellular truncated human enzyme from CHO-K1 cell culture medium by Hupresin affinity chromatography, elution is best with 0.1M tetramethylammonium bromide in 20mM TrisCl, pH 7.5, followed by dialysis and ultrafiltration, to homogeneity. Loss of 24% during the dialysis and concentration steps
recombinant full-length enzyme from CHO cells
recombinant human BChE from the milk of transgenic goats to homogeneity
-
recombinant human enzyme from Nicotiana benthamiana by tangential flow ultrafiltration, anion exchange chromatography, and tacrine-huperzine A hybrid (Hupresin) affinity chromatography, method optimization and evaluation, comparison to procainamide affinity chromatography purification method. Citrate buffer at pH 4.0 is selected to minimize extraction of host plant proteins and shows a 4.5fold enhancement in rBChE specific activity compared to Tris buffer, pH 8.0. Anion exchange chromatography increases the purity of rBChE by 70% by removing major host plant protein impurities. The rBChE is then adsorbed to Hupresin® and purified to homogeneity and over 95% purity for an overall process yield of 34%. The purification process represents a 3fold higher product yield over the established process
recombinant wild-type and mutant enzymes from CHO-K1 cells by anion exchange and affinity chromatography
-
separation from acetylcholine esterase
-
VX-inhibited BChE adducts from human plasma by the procainamide affinity gel method or the immunomagnetic separation (IMS) method. The purification efficiency of IMS is 5fold greater than that of the procainamide affinity gel method because the antibody conjugate with protein G magnetic beads ensures highly selective capture and high recovery of VX-inhibited BChE from plasma, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally truncated human enzyme (BChE) 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
expressed in Baculovirus-infected cabbage looper larvae and COS-7 cells
-
expressed in CHO cells
-
expressed in CHO-K1 cells
expression of a A328W/Y332A mutant BChE with improved cocaine hydrolase activity in transgenic Nicotiana benthamiana plants
-
expression of full-length enzyme in CHO or HEK-293 cells, overview
expression of the recombinant human BChE in the milk of transgenic goats
-
expression of wild-type and mutant enzymes in CHO-K1 cells
-
gene BCHE located at chromosome 3q26.1-q26.2, DNA and amino acid sequence determination and analysis, genotyping in Brasilian population and polymorpshisms, expression of mutants in HEK-293T cells and CHO cells, overview
-
gene BCHE, recombinant expression of human butyrylcholinesterase in Nicotiana benthamiana using the Agrobacterium tumefaciens-mediated transfection method, sequence comparison to human native wild-type enzyme
gene organization and evolution of cholinesterases
-
K variant of gene BCHE, relationship between BCHE genotype and butyrylcholinesterase activity in autopsy brain tissue, BuChE activity in temporal cortex is 37% higher in K homozygotes than in wild-type homozygotes, overview
-
monomeric enzyme, lacking four out of nine N-glycosylation sites and the C-terminal oligomerization domain, expressed in CHO cells
-
mutant GG117H is expressed in CHO cells
recombinant expression of the enzyme in C57BL/6 mice
recombinant expression of truncated human enzyme in stably transfected CHO-K1 cells, the recombinant enzyme is secreted
wild type and mutant enzymes are expressed in HEK-293T/17 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
type 2 diabetics with or without metabolic syndrome have significantly higher activity of butyrylcholinesterase than control group
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
enzyme BChE is a promising drug target in advanced Alzheimer's disease. (+/-)-N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-N-(2-(dimethylamino)ethyl)-2-naphthamide is thus a promising advanced lead compound for the development of drugs for alleviating symptoms of cholinergic hypofunction in patients with advanced Alzheimer's disease
medicine
pharmacology
effective use of exogenous human BChE as a bioscavenger for organophosphorus toxicants, e.g. paraoxon. Paraoxon elicites near complete inhibition of liver carboxylesterase at 40 nM
additional information
-
human serum butyrylcholinesterase is the most viable candidate for the prophylactic treatment of organophosphate poisoning
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reiner, E.; Simeon-Rudolf, V.; Skrinjaric-Spoljar, M.
Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera
Toxicol. Lett.
82/83
447-452
1995
Homo sapiens
Manually annotated by BRENDA team
Lockridge, O.; La Du, B.N.
Comparison of atypical and usual human serum cholinesterase
J. Biol. Chem.
253
361-366
1978
Homo sapiens
Manually annotated by BRENDA team
Brown, S.S.; Kalow, W.; Pilz, W.; Whittaker, M.; Woronick, C.L.
The plasma cholinesterase: a new perspective
Adv. Clin. Chem.
22
1-123
1981
Canis lupus familiaris, Equus caballus, Homo sapiens, Mus musculus, Pleuronectes platessa, Pseudomonas aeruginosa, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Ralston, J.S.; Main, A.R.; Kilpatrick, B.F.; Chasson, A.L.
Use of procainamide gels in the purification of human and horse serum cholinesterases
Biochem. J.
211
243-250
1983
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Prody, C.A.; Zevin-Sonkin, D.; Gnatt, A.; Goldberg, O.; Soreq, H.
Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues
Proc. Natl. Acad. Sci. USA
84
3555-3559
1987
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Laurentie, M.
Stability of butyrylcholinesterase: thermal inactivation in water and deuterium oxide
Biochim. Biophys. Acta
957
111-121
1988
Homo sapiens
Manually annotated by BRENDA team
Mutero, A.; Pralavorio, M.; Simeon, V.; Fournier, D.
Catalytic properties of cholinesterase: importance of tyrosine 109 in Drosophila protein
NeuroReport
3
39-42
1992
Homo sapiens
Manually annotated by BRENDA team
Rao, R.V.; Balasubramanian, A.S.
The peptidase activity of human serum butyrylcholinesterase: Studies using monoclonal antibodies and characterization of the peptidase
J. Protein Chem.
12
103-110
1993
Homo sapiens
Manually annotated by BRENDA team
Graham, S.G.; Crossley, A.W.A.
The characteristics of the inhibition of serum cholinesterase by metoclopramide
Eur. J. Clin. Pharmacol.
48
225-228
1995
Homo sapiens
Manually annotated by BRENDA team
Primo-Parmo, S.L.; Lightstone, H.; La Du, B.N.
Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase
Pharmacogenetics
7
27-34
1997
Homo sapiens
Manually annotated by BRENDA team
Weingand-Ziade, A.; Ribes, F.; Renault, F.; Masson, P.
Pressure- and heat-induced inactivation of butyrylcholinesterase: evidence for multiple intermediates and the remnant inactivation process
Biochem. J.
356
487-493
2001
Homo sapiens
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
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Xie, W.; Froment, M.T.; Lockridge, O.
Effects of mutations of active site residues and amino acids interacting with the W loop on substrate activation of butyrylcholinesterase
Biochim. Biophys. Acta
1544
166-176
2001
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Froment, M.T.; Fort, S.; Ribes, F.; Bec, N.; Balny, C.; Schopfer, L.M.
Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior
Biochim. Biophys. Acta
1597
229-243
2002
Homo sapiens
Manually annotated by BRENDA team
Platteborze, P.L.; Broomfield, C.A.
Expression of biologically active human butyrylcholinesterase in the cabbage looper (Trichoplusia ni)
Biotechnol. Appl. Biochem.
31
225-229
2000
Homo sapiens
-
Manually annotated by BRENDA team
Darvesh, S.; Kumar, R.; Roberts, S.; Walsh, R.; Martin, E.
Butyrylcholinesterase-mediated enhancement of the enzymatic activity of trypsin
Cell. Mol. Neurobiol.
21
285-296
2001
Homo sapiens
Manually annotated by BRENDA team
Nachon, F.; Nicolet, Y.; Viguie, N.; Masson, P.; Fontecilla-Camps, J.C.; Lockridge, O.
Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: expression, purification, characterization and crystallization
Eur. J. Biochem.
269
630-637
2002
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Nachon, F.; Bartels, C.F.; Froment, M.T.; Ribes, F.; Matthews, C.; Lockridge, O.
High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine
Eur. J. Biochem.
270
315-324
2003
Homo sapiens
Manually annotated by BRENDA team
Saxena, A.; Fedorko, J.M.; Vinayaka, C.R.; Medhekar, R.; Radic, Z.; Taylor, P.; Lockridge, O.; Doctor, B.P.
Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases
Eur. J. Biochem.
270
4447-4458
2003
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Goldstein, B.N.; Debouzy, J.C.; Froment, M.T.; Lockridge, O.; Schopfer, L.M.
Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate
Eur. J. Biochem.
271
220-234
2004
Homo sapiens
Manually annotated by BRENDA team
Zhan, C.G.; Zheng, F.; Landry, D.W.
Fundamental reaction mechanism for cocaine hydrolysis in human butyrylcholinesterase
J. Am. Chem. Soc.
125
2462-2474
2003
Homo sapiens
Manually annotated by BRENDA team
Sun, H.; El Yazal, J.; Lockridge, O.; Schopfer, L.M.; Brimijoin, S.; Pang, Y.P.
Predicted Michaelis-Menten complexes of cocaine-butyrylcholinesterase. Engineering effective butyrylcholinesterase mutants for cocaine detoxication
J. Biol. Chem.
276
9330-9336
2001
Homo sapiens
Manually annotated by BRENDA team
Nicolet, Y.; Lockridge, O.; Masson, P.; Fontecilla-Camps, J.C.; Nachon, F.
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
J. Biol. Chem.
278
41141-41147
2003
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Altamirano, C.V.; Bartels, C.F.; Lockridge, O.
The butyrylcholinesterase K-variant shows similar cellular protein turnover and quaternary interaction to the wild-type enzyme
J. Neurochem.
74
869-877
2000
Homo sapiens
Manually annotated by BRENDA team
Cengiz, D.; Cokugras, A.N.; Tezcan, E.F.
A new perspective on thermal inactivation kinetics of human serum butyrylcholinesterase
J. Protein Chem.
21
145-149
2002
Homo sapiens
Manually annotated by BRENDA team
Sun, H.; Pang, Y.P.; Lockridge, O.; Brimijoin, S.
Re-engineering butyrylcholinesterase as a cocaine hydrolase
Mol. Pharmacol.
62
220-224
2002
Homo sapiens (P06276)
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
Ashani, Y.; Segev, O.; Balan, A.
The effect of fluoride on the scavenging of organophosphates by human butyrylcholinesterase in buffer solutions and human plasma
Toxicol. Appl. Pharmacol.
194
90-99
2004
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
Bailey, D.N.; Briggs, J.R.
Studies of the inhibition of serum pseudocholinesterase activity in vitro by commonly used drugs
Am. J. Clin. Pathol.
124
226-228
2005
Homo sapiens
Manually annotated by BRENDA team
Kucukkilinc, T.; Ozer, I.
Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: mechanistic implications
Arch. Biochem. Biophys.
440
118-122
2005
Homo sapiens
Manually annotated by BRENDA team
Nachon, F.; Asojo, O.A.; Borgstahl, G.E.; Masson, P.; Lockridge, O.
Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging
Biochemistry
44
1154-1162
2005
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Kamal, M.A.; Al-Jafari, A.A.; Yu, Q.S.; Greig, N.H.
Kinetic analysis of the inhibition of human butyrylcholinesterase with cymserine
Biochim. Biophys. Acta
1760
200-206
2006
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
Saxena, A.; Sun, W.; Luo, C.; Doctor, B.P.
Human serum butyrylcholinesterase: In vitro and in vivo stability, pharmacokinetics, and safety in mice
Chem. Biol. Interact.
157-158
199-203
2005
Homo sapiens
Manually annotated by BRENDA team
Cerasoli, D.M.; Griffiths, E.M.; Doctor, B.P.; Saxena, A.; Fedorko, J.M.; Greig, N.H.; Yu, Q.S.; Huang, Y.; Wilgus, H.; Karatzas, C.N.; Koplovitz, I.; Lenz, D.E.
In vitro and in vivo characterization of recombinant human butyrylcholinesterase (Protexia) as a potential nerve agent bioscavenger
Chem. Biol. Interact.
157-158
363-365
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
Masson, P.; Bec, N.; Froment, M.T.; Nachon, F.; Balny, C.; Lockridge, O.; Schopfer, L.M.
Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine. Volumetric study of wild-type and D70G mutant behavior
Eur. J. Biochem.
271
1980-1990
2004
Homo sapiens
Manually annotated by BRENDA team
Tormos, J.R.; Wiley, K.L.; Seravalli, J.; Nachon, F.; Masson, P.; Nicolet, Y.; Quinn, D.M.
The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate
J. Am. Chem. Soc.
127
14538-14539
2005
Homo sapiens
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
Gao, D.; Zhan, C.G.
Modeling effects of oxyanion hole on the ester hydrolysis catalyzed by human cholinesterases
J. Phys. Chem. B
109
23070-23076
2005
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Mehrani, H.
Simplified procedures for purification and stabilization of human plasma butyrylcholinesterase
Proc. Biochem.
39
877-882
2004
Homo sapiens
-
Manually annotated by BRENDA team
Suarez, D.; Field, M.J.
Molecular dynamics simulations of human butyrylcholinesterase
Proteins
59
104-117
2005
Homo sapiens
Manually annotated by BRENDA team
Gao, D.; Zhan, C.G.
Modeling evolution of hydrogen bonding and stabilization of transition states in the process of cocaine hydrolysis catalyzed by human butyrylcholinesterase
Proteins
62
99-110
2006
Homo sapiens
Manually annotated by BRENDA team
Darvesh, S.; McDonald, R.S.; Darvesh, K.V.; Mataija, D.; Mothana, S.; Cook, H.; Carneiro, K.M.; Richard, N.; Walsh, R.; Martin, E.
On the active site for hydrolysis of aryl amides and choline esters by human cholinesterases
Bioorg. Med. Chem.
14
4586-4599
2006
Homo sapiens
Manually annotated by BRENDA team
Ngamelue, M.N.; Homma, K.; Lockridge, O.; Asojo, O.A.
Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase
Acta Crystallogr. Sect. F
63
723-727
2007
Homo sapiens (P06276), 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
Walsh, R.; Martin, E.; Darvesh, S.
A versatile equation to describe reversible enzyme inhibition and activation kinetics: modeling beta-galactosidase and butyrylcholinesterase
Biochim. Biophys. Acta
1770
733-746
2007
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Froment, M.; Gillon, E.; Nachon, F.; Darvesh, S.; Schopfer, L.M.
Kinetic analysis of butyrylcholinesterase-catalyzed hydrolysis of acetanilides
Biochim. Biophys. Acta
1774
1139-1147
2007
Homo sapiens
Manually annotated by BRENDA team
Montenegro, M.F.; Moral-Naranjo, M.T.; de la Cadena, M.P.; Campoy, F.J.; Munoz-Delgado, E.; Vidal, C.J.
Human butyrylcholinesterase components differ in aryl acylamidase activity
Biol. Chem.
389
425-432
2008
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
Boopathy, R.; Rajesh, R.V.; Darvesh, S.; Layer, P.G.
Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity
Clin. Chim. Acta
380
151-156
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
Kamal, M.A.; Klein, P.; Luo, W.; Li, Y.; Holloway, H.W.; Tweedie, D.; Greig, N.H.
Kinetics of human serum butyrylcholinesterase inhibition by a novel experimental alzheimer therapeutic, dihydrobenzodioxepine cymserine
Neurochem. Res.
33
745-753
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
Grigoryan, H.; Halebyan, G.; Lefebvre, B.; Brasme, B.; Masson, P.
Mechanism of hydrolysis of dicholine esters with long polymethylene chain by human butyrylcholinesterase
Biochim. Biophys. Acta
1784
1818-1824
2008
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Bromberg, A.; Marx, S.; Frishman, G.
Kinetic study of the thermal inactivation of cholinesterase enzymes immobilized in solid matrices
Biochim. Biophys. Acta
1784
961-966
2008
Homo sapiens
Manually annotated by BRENDA team
Masson, P.; Nachon, F.; Broomfield, C.A.; Lenz, D.E.; Verdier, L.; Schopfer, L.M.; Lockridge, O.
A collaborative endeavor to design cholinesterase-based catalytic scavengers against toxic organophosphorus esters
Chem. Biol. Interact.
175
273-280
2008
Homo sapiens
Manually annotated by BRENDA team
Massoulie, J.; Perrier, N.; Noureddine, H.; Liang, D.; Bon, S.
Old and new questions about cholinesterases
Chem. Biol. Interact.
175
30-44
2008
Homo sapiens
Manually annotated by BRENDA team
Calic, M.; Bosak, A.; Kuca, K.; Kovarik, Z.
Interactions of butane, but-2-ene or xylene-like linked bispyridinium para-aldoximes with native and tabun-inhibited human cholinesterases
Chem. Biol. Interact.
175
305-308
2008
Homo sapiens
Manually annotated by BRENDA team
Geyer, B.C.; Woods, R.R.; Mor, T.S.
Increased organophosphate scavenging in a butyrylcholinesterase mutant
Chem. Biol. Interact.
175
376-379
2008
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
Li, H.; Tong, L.; Schopfer, L.M.; Masson, P.; Lockridge, O.
Fast affinity purification coupled with mass spectrometry for identifying organophosphate labeled plasma butyrylcholinesterase
Chem. Biol. Interact.
175
68-72
2008
Homo sapiens
Manually annotated by BRENDA team
Gao, Y.; LaFleur, D.; Shah, R.; Zhao, Q.; Singh, M.; Brimijoin, S.
An albumin-butyrylcholinesterase for cocaine toxicity and addiction: catalytic and pharmacokinetic properties
Chem. Biol. Interact.
175
83-87
2008
Homo sapiens
Manually annotated by BRENDA team
Grigoryan, H.A.; Hambardzumyan, A.A.; Mkrtchyan, M.V.; Topuzyan, V.O.; Halebyan, G.P.; Asatryan, R.S.
alpha,beta -Dehydrophenylalanine choline esters, a new class of reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase
Chem. -Biol. Interact.
171
108-116
2008
Homo sapiens (P06276), 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
Stojanov, M.D.; Jovicic, D.M.; Djuric, S.P.; Konjevic, M.M.; Todorovic, Z.M.; Prostran, M.S.
Butyrylcholinesterase activity and mortality risk in hemodialysis patients: comparison to hsCRP and albumin
Clin. Biochem.
42
22-26
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
Equus caballus, 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
Liang, D.; Blouet, J.P.; Borrega, F.; Bon, S.; Massoulie, J.
Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase
FEBS J.
276
94-108
2009
Homo sapiens
Manually annotated by BRENDA team
Ahmed, M.; Batista, J.; Rocha, T.; Mazzanti, C.M.; Hassan, W.; Morsch, V.M.; Loro, V.L.; Thome, G.; Schetinger, M.R.
Comparative study of the inhibitory effect of antidepressants on cholinesterase activity in Bungarus sindanus (krait) venom, human serum and rat striatum
J. Enzyme Inhib. Med. Chem.
23
912-917
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
Rivera-Becerril, E.; Joseph-Nathan, P.; Perez-Alvarez, V.M.; Morales-Rios, M.S.
Synthesis and biological evaluation of (-)- and (+)-debromoflustramine B and its analogues as selective butyrylcholinesterase inhibitors
J. Med. Chem.
51
5271-5284
2008
Homo sapiens
Manually annotated by BRENDA team
Carolan, C.G.; Dillon, G.P.; Gaynor, J.M.; Reidy, S.; Ryder, S.A.; Khan, D.; Marquez, J.F.; Gilmer, J.F.
Isosorbide-2-carbamate esters: potent and selective butyrylcholinesterase inhibitors
J. Med. Chem.
51
6400-6409
2008
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Podoly, E.; Bruck, T.; Diamant, S.; Melamed-Book, N.; Weiss, A.; Huang, Y.; Livnah, O.; Langermann, S.; Wilgus, H.; Soreq, H.
Human recombinant butyrylcholinesterase purified from the milk of transgenic goats interacts with beta-amyloid fibrils and suppresses their formation in vitro
Neurodegener. Dis.
5
232-236
2008
Homo sapiens
Manually annotated by BRENDA team
Tasker, A.; Ballard, C.G.; Joachim, C.; Warden, D.R.; Okello, E.J.; Perry, R.H.; Khan, N.; Smith, A.D.; Lehmann, D.J.; Perry, E.K.
Butyrylcholinesterase K variant associated with higher enzyme activity in the temporal cortex of elderly patients
Neurosci. Lett.
442
297-299
2008
Homo sapiens
Manually annotated by BRENDA team
Mikami, L.R.; Wieseler, S.; Souza, R.L.; Schopfer, L.M.; Nachon, F.; Lockridge, O.; Chautard-Freire-Maia, E.A.
Five new naturally occurring mutations of the BCHE gene and frequencies of 12 butyrylcholinesterase alleles in a Brazilian population
Pharmacogenet. Genomics
18
213-218
2008
Homo sapiens
Manually annotated by BRENDA team
Saxena, A.; Luo, C.; Doctor, B.P.
Developing procedures for the large-scale purification of human serum butyrylcholinesterase
Protein Expr. Purif.
61
191-196
2008
Homo sapiens
Manually annotated by BRENDA team
Kolarich, D.; Weber, A.; Pabst, M.; Stadlmann, J.; Teschner, W.; Ehrlich, H.; Schwarz, H.P.; Altmann, F.
Glycoproteomic characterization of butyrylcholinesterase from human plasma
Proteomics
8
254-263
2008
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Orhan, I.; Kartal, M.; Tosun, F.; Sener, B.
Screening of various phenolic acids and flavonoid derivatives for their anticholinesterase potential
Z. Naturforsch. C
62
829-832
2008
Homo sapiens
Manually annotated by BRENDA team
Gholivand, K.; Alizadehgan, A.M.; Mojahed, F.; Dehghan, G.; Mohammadirad, A.; Abdollahi, M.
Some new carbacylamidophosphates as inhibitors of acetylcholinesterase and butyrylcholinesterase
Z. Naturforsch. C
63
241-250
2008
Homo sapiens
Manually annotated by BRENDA team
Musilek, K.; Komloova, M.; Zavadova, V.; Holas, O.; Hrabinova, M.; Pohanka, M.; Dohnal, V.; Nachon, F.; Dolezal, M.; Kuca, K.; Jung, Y.S.
Preparation and in vitro screening of symmetrical bispyridinium cholinesterase inhibitors bearing different connecting linkage-initial study for Myasthenia gravis implications
Bioorg. Med. Chem. Lett.
20
1763-1766
2010
Homo sapiens
Manually annotated by BRENDA team
Dillon, G.P.; Gaynor, J.M.; Khan, D.; Carolan, C.G.; Ryder, S.A.; Marquez, J.F.; Reidy, S.; Gilmer, J.F.
Isosorbide-based cholinesterase inhibitors; replacement of 5-ester groups leading to increased stability
Bioorg. Med. Chem.
18
1045-1053
2010
Homo sapiens
Manually annotated by BRENDA team
Hofmann, J.; Keifer, M.; Furlong, C.; De Roos, A.; Farin, F.; Fenske, R.; van Belle, G.; Checkoway, H.
Serum cholinesterase inhibition in relation to paraoxonase-1 (PON1) status among organophosphate-Exposed agricultural pesticide handlers
Environ. Health Perspect.
117
1402-1408
2009
Homo sapiens
Manually annotated by BRENDA team
Katalinic, M.; Rusak, G.; Domacinovic Barovic, J.; Sinko, G.; Jelic, D.; Antolovic, R.; Kovarik, Z.
Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase
Eur. J. Med. Chem.
45
186-192
2010
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Elsinghorst, P.W.; Haertig, W.; Goldhammer, S.; Grosche, J.; Guetschow, M.
A gorge-spanning, high-affinity cholinesterase inhibitor to explore beta-amyloid plaques
Org. Biomol. Chem.
7
3940-3946
2009
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
Umar, R.; Hassan, S.; Ndukwe, O.
Butyrylcholinesterase activity in Nigerian type 2 diabetics with and without metabolic syndrome
Afr. J. Biotechnol.
9
4110-4113
2010
Homo sapiens
-
Manually annotated by BRENDA team
Nachon, F.; Carletti, E.; Wandhammer, M.; Nicolet, Y.; Schopfer, L.; Masson, P.; Lockridge, O.
X-ray crystallographic snapshots of reaction intermediates in the G117H mutant of human butyrylcholinesterase, a nerve agent target engineered into a catalytic bioscavenger
Biochem. J.
434
73-82
2011
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Korabecny, J.; Musilek, K.; Holas, O.; Binder, J.; Zemek, F.; Marek, J.; Pohanka, M.; Opletalova, V.; Dohnal, V.; Kuca, K.
Synthesis and in vitro evaluation of N-alkyl-7-methoxytacrine hydrochlorides as potential cholinesterase inhibitors in Alzheimer disease
Bioorg. Med. Chem. Lett.
20
6093-6095
2010
Homo sapiens
Manually annotated by BRENDA team
Yang, W.; Xue, L.; Fang, L.; Chen, X.; Zhan, C.
Characterization of a high-activity mutant of human butyrylcholinesterase against (-)-cocaine
Chem. Biol. Interact.
187
148-152
2010
Homo sapiens
Manually annotated by BRENDA team
Kovarik, Z.; Katalinic, M.; Sinko, G.; Binder, J.; Holas, O.; Jung, Y.; Musilova, L.; Jun, D.; Kuca, K.
Pseudo-catalytic scavenging: Searching for a suitable reactivator of phosphorylated butyrylcholinesterase
Chem. Biol. Interact.
187
167-171
2010
Homo sapiens (P06276), 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 (P06276), Homo sapiens
Manually annotated by BRENDA team
Darvesh, S.; Reid, G.; Martin, E.
Biochemical and histochemical comparison of cholinesterases in normal and Alzheimer brain tissues
Curr. Alzheimer Res.
7
386-400
2010
Homo sapiens
Manually annotated by BRENDA team
Xue, L.; Ko, M.; Tong, M.; Yang, W.; Hou, S.; Fang, L.; Liu, J.; Zheng, F.; Woods, J.; Tai, H.; Zhan, C.
Design, preparation, and characterization of high-activity mutants of human butyrylcholinesterase specific for detoxification of cocaine
Mol. Pharmacol.
79
290-297
2011
Homo sapiens
Manually annotated by BRENDA team
Dingova, D.; Leroy, J.; Check, A.; Garaj, V.; Krejci, E.; Hrabovska, A.
Optimal detection of cholinesterase activity in biological samples: Modifications to the standard Ellmans assay
Anal. Biochem.
462
67-75
2014
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Nachon, F.; Carletti, E.; Ronco, C.; Trovaslet, M.; Nicolet, Y.; Jean, L.; Renard, P.Y.
Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimers drugs targeting acetyl- and butyryl-cholinesterase
Biochem. J.
453
393-399
2013
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Masson, P.
Time-dependent kinetic complexities in cholinesterase-catalyzed reactions
Biochemistry
77
1147-1161
2012
Homo sapiens
Manually annotated by BRENDA team
Yoon, Y.K.; Ali, M.A.; Wei, A.C.; Choon, T.S.; Khaw, K.Y.; Murugaiyah, V.; Osman, H.; Masand, V.H.
Synthesis, characterization, and molecular docking analysis of novel benzimidazole derivatives as cholinesterase inhibitors
Bioorg. Chem.
49
33-39
2013
Homo sapiens
Manually annotated by BRENDA team
Trovaslet, M.; Trapp, M.; Weik, M.; Nachon, F.; Masson, P.; Tehei, M.; Peters, J.
Relation between dynamics, activity and thermal stability within the cholinesterase family
Chem. Biol. Interact.
203
14-18
2013
Homo sapiens
Manually annotated by BRENDA team
Correa-Basurto, J.; Bello, M.; Rosales-Hernandez, M.C.; Hernandez-Rodriguez, M.; Nicolas-Vazquez, I.; Rojo-Dominguez, A.; Trujillo-Ferrara, J.G.; Miranda, R.; Flores-Sandoval, C.A.
QSAR, docking, dynamic simulation and quantum mechanics studies to explore the recognition properties of cholinesterase binding sites
Chem. Biol. Interact.
209
1-13
2014
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
Homo sapiens (P06276)
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 (P06276), Homo sapiens, Sus scrofa (P32752), Sus scrofa
Manually annotated by BRENDA team
Bhakta, H.K.; Park, C.H.; Yokozawa, T.; Min, B.S.; Jung, H.A.; Choi, J.S.
Kinetics and molecular docking studies of loganin, morroniside and 7-O-galloyl-D-sedoheptulose derived from Corni fructus as cholinesterase and beta-secretase 1 inhibitors
Arch. Pharm. Res.
39
794-805
2016
Homo sapiens (P06276)
Manually annotated by BRENDA team
Alkanaimsh, S.; Corbin, J.; Kailemia, M.; Karuppanan, K.; Rodriguez, R.; Lebrilla, C.; McDonald, K.; Nandi, S.
Purification and site-specific N-glycosylation analysis of human recombinant butyrylcholinesterase from Nicotiana benthamiana
Biochem. Eng. J.
142
58-67
2019
Homo sapiens (P06276)
-
Manually annotated by BRENDA team
Pope, C.; Uchea, C.; Flynn, N.; Poindexter, K.; Geng, L.; Brimijoin, W.S.; Hartson, S.; Ranjan, A.; Ramsey, J.D.; Liu, J.
In vitro characterization of cationic copolymer-complexed recombinant human butyrylcholinesterase
Biochem. Pharmacol.
98
531-539
2015
Homo sapiens (P06276), Homo sapiens
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 (P06276)
Manually annotated by BRENDA team
Yang, S.H.; Sun, Q.; Xiong, H.; Liu, S.Y.; Moosavi, B.; Yang, W.C.; Yang, G.F.
Discovery of a butyrylcholinesterase-specific probe via a structure-based design strategy
Chem. Commun. (Camb.)
53
3952-3955
2017
Homo sapiens
Manually annotated by BRENDA team
Altaf, A.A.; Hamayun, M.; Lal, B.; Tahir, M.N.; Holder, A.A.; Badshah, A.; Crans, D.C.
Ferrocene-based anilides synthesis, structural characterization and inhibition of butyrylcholinesterase
Dalton Trans.
47
11769-11781
2018
Homo sapiens (P06276)
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 (P06276)
Manually annotated by BRENDA team
Macdonald, I.R.; Maxwell, S.P.; Reid, G.A.; Cash, M.K.; DeBay, D.R.; Darvesh, S.
Quantification of butyrylcholinesterase activity as a sensitive and specific biomarker of Alzheimers disease
J. Alzheimers Dis.
58
491-505
2017
Homo sapiens
Manually annotated by BRENDA team
Lockridge, O.; David, E.; Schopfer, L.M.; Masson, P.; Brazzolotto, X.; Nachon, F.
Purification of recombinant human butyrylcholinesterase on Hupresin?
J. Chromatogr. B
1102-1103
109-115
2018
Homo sapiens (P06276), Homo sapiens
Manually annotated by BRENDA team
Lee, J.Y.
Comparison of efficiency of purification (from human plasma) of a nerve agent adduct of butyrylcholinesterase between the affinity gel method and immunomagnetic separation
J. Chromatogr. Sci.
56
248-253
2018
Homo sapiens (P06276), 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 (P06276)
Manually annotated by BRENDA team
Kosak, U.; Brus, B.; Knez, D.; Zakelj, S.; Trontelj, J.; Pislar, A.; Sink, R.; Jukic, M.; Zivin, M.; Podkowa, A.; Nachon, F.; Brazzolotto, X.; Stojan, J.; Kos, J.; Coquelle, N.; Salat, K.; Colletier, J.P.; Gobec, S.
The magic of crystal structure-based inhibitor optimization development of a butyrylcholinesterase inhibitor with picomolar affinity and in vivo activity
J. Med. Chem.
61
119-139
2018
Homo sapiens (P06276), Homo sapiens, Rattus norvegicus (Q9JKC1)
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 (P06276), Homo sapiens, Canis lupus familiaris (P32750), Canis lupus familiaris
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 (P06276)
-
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 (P06276), Homo sapiens
Manually annotated by BRENDA team