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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Tetronarce californica and UniProt Accession P04058

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.7 acetylcholinesterase
IUBMB Comments
Acts on a variety of acetic esters; also catalyses transacetylations.
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This record set is specific for:
Tetronarce californica
UNIPROT: P04058
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Word Map
The taxonomic range for the selected organisms is: Tetronarce californica
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ache, acetylcholinesterase, acetylcholine esterase, acetyl cholinesterase, hache, eeache, ache1, huache, tcache, membrane-bound acetylcholinesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
butyrylcholinesterase
-
AcCholE
-
-
-
-
acetyl beta-methylcholinesterase
-
-
-
-
acetylcholine esterase
-
-
-
-
acetylcholine hydrolase
-
-
-
-
acetylcholinesterase
-
-
acetylthiocholinesterase
-
-
-
-
choline esterase I
-
-
-
-
cholinesterase
-
-
-
-
esterase, acetyl choline
-
-
-
-
true cholinesterase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetylcholine + H2O = choline + acetate
show the reaction diagram
reaction mechanism, structure-function relationship analysis, binding structure and mechanism of substrate and product at both the peripheral and active sites, overview
acetylcholine + H2O = choline + acetate
show the reaction diagram
reaction mechanism, active site structure, the catalytic triad comprises the residues Ser203, His447, Glu334, residues Ser203 and His447 are directly involved in the reaction, serving as nucleophilic attacking group and general acid base catalytic elements, respectively, at the acylation stage of the enzymatic reaction. Modern molecular modeling using tools including molecular docking, molecular dynamics (MD), quantum chemistry and the combined quantum mechanical-molecular mechanical method, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
transacetylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylcholine acetylhydrolase
Acts on a variety of acetic esters; also catalyses transacetylations.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-81-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylcholine + H2O
choline + acetate
show the reaction diagram
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
-
-
-
?
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
acetylthiocholine iodide + H2O
thiocholine iodide + acetate
show the reaction diagram
-
-
-
?
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
-
-
-
?
additional information
?
-
the catalytic triad is formed by His440, Glu327, and Ser200, Trp84 and Trp279 are important for the enzyme activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetylcholine + H2O
choline + acetate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-huperzine A
synthetic enantiomer of the anti-Alzheimer drug (-)-huperzine A and of its natural homologue (-)-huperzine B, interacts with the anionic subsite of the active site
(-)-huperzine A
anti-Alzheimer drug
(-)-S-3-[1-(dimethylamino)ethyl]phenol
competitive reversible inhibitor
(2,3-trans)-3-(3-hydroxy-5-methoxyphenyl)-N-(4-hydroxyphenethyl)-7-((E)-3-[(4-hydroxyphenethyl)amino]-3-oxoprop-1-enyl)-2,3-dihydro-benzo[b][1,4]dioxine-2-carboxamide
-
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
a rigid DNP-like analogue compound, shows mixed-type inhibition
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one
a rigid DNP-like analogue compound, shows mixed-type inhibition
(7R,11R)-huprine 19
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(7S,11S)-huprine W
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(RS)-tacrine(10)-hupyridone
-
(S,S)-(-)-bis(10)-hupyridone
enzyme binding structure, analysis using structure PDB ID 1H22, detailed overview
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(4-amino-5-chloro-2-methoxyphenyl)-3-(1-butyl-4-piperidinyl)-1-propanone
i.e. RS67333
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-6-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-benzyl-3-[4-(4-benzylpiperazin-1-yl)butyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-[3-(4-benzylpiperazin-1-yl)propyl]-3-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-[5-(5-nitro-1H-indazol-3-yl)thiophen-3-yl]ethanone
-
2-(2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl)phenol
-
2-[2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
2-[2-(4-methylphenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
3,3'-demethyl-grossamide
87.37% inhibition at 0.1 mg/ml
3,3'-demethyl-heliotropamide
62.84% inhibition at 0.1 mg/ml
3,3'-[nonane-1,9-diylbis[(3S)-3-ethylazepane-1,3-diyl]]diphenol
binding by a bis-(-)-nor-meptazinol derivative disrupts the catalytic triad, structure analysis and molecular docking, overview
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
-
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-benzyl-1-[3-(4-benzylpiperazin-1-yl)propyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
-
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
4-oxo-N,N,N-trimethylpentanaminium iodide
i.e. OTMA, a hydrolysable substrate analogue, binding structure analysis
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[2,3-e]pyrazin-5(4H)-one
-
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[3,2-e]pyrazin-5(4H)-one
-
5,5'-dithiobis(2-nitrobenzoic acid)
inactivation, the peripheral site ligand propidium accelerates inactivation in the wild type ChE2, but retards inactivation in the F312I mutant
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
5-[(1-benzylpiperidin-4-yl)methoxy]-1-methylpyrrolo[1,2-a]thieno[2,3-e]pyrazine
-
5-[(1-benzylpiperidin-4-yl)methoxy]pyrrolo[1,2-a]thieno[3,2-e]pyrazine
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5-[4-(4-benzylpiperazin-1-yl)butyl]-7-phenyl-1,5-dihydro-4H-furo[2,3-b]pyrrolo[2,3-d]pyridin-4-one
-
7-O-galloyl-D-sedoheptulose
a mixed-type inhibitor, enzyme interacting residues, overview
Acetylcholine
substrate inhibition due to choline exit being hindered by a substrate molecule bound at the peripheral site
acetylthiocholine
interaction with Glu199 of ATCh, substrate inhibition due to choline exit being hindered by a substrate molecule bound at the peripheral site
cannabisin A
47.13% inhibition at 0.1 mg/ml
cannabisin C
42.89% inhibition at 0.1 mg/ml
cannabisin D
13.97% inhibition at 0.1 mg/ml
cannabisin E
11.17% inhibition at 0.1 mg/ml
cannabisin F
47.16% inhibition at 0.1 mg/ml
cannabisin N
51.99% inhibition at 0.1 mg/ml
decamethonium
decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site, where it is stabilized by the cation-Pi interactions illustrated in its complex with Torpedo californica AChE (TcAChE), binding structure, overview
donecopride
synthesized from donepezil and RS67333, shows a double mechanism of action and good bioavailability. Replacement of the benzene ring of the compound by an indole residue should increase the interaction of the ligand with the peripheral anionic site (PAS), thus resulting in increased inhibition of beta-amyloid aggregation
donepezil
ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
galantamine
grossamide
22.42% inhibition at 0.1 mg/ml
loganin
a mixed-type inhibitor, enzyme interacting residues, overview
morroniside
a noncompetitive inhibitor, enzyme interacting residues, overview
N-ethylmaleimide
inactivation
N-trans-caffeoyltyramine
83.28% inhibition at 0.1 mg/ml
N-trans-feruloyltyramine
13.25% inhibition at 0.1 mg/ml
propidium
structure of the complex is solved at 3.0 A resolution, absence involving Trp279 in TcAChE at the gorge
rivastigmine
sodium 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
thioflavin T
ThT, is not sufficiently long to span the P-site and the choline binding site pocket of enzyme TcAChE. The benzothiazole and dimethylaminophenyl rings, and the dimethylamino group of this ligand are coplanar and lay parallel to Trp279 and Tyr334 and Phe330, respectively. The dimethylamino group is at 3.3 A from the aromatic ring of Phe330 but remains far from the gorge bottom, at a distance of 8.5 A from the carboxylate oxygens of Glu199. This position at the P-site allows concomitant binding of A-site ligands like edrophonium or m-(N,N,N-trimethylammonio)trifluoroacetophenone (TMTFA) through an adjustment of the orientation of Phe330
[1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine iodide
caged compound, binding structure and mechanism with AChE, binding within the active-site gorge, overview
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
E2020, acetylcholinesterase inhibitor used in treatment of Alzheimer's diaease, interacts with the active site and the peripheral anionic site of the enzyme
buxamine-B
-
50% inhibition at 0.074 mM, noncompetitive
buxamine-C
-
50% inhibition at 0.0075 mM, noncompetitive
BW284c51
-
a reversible elongated gorge-spanning inhibitor, which bridges the two sites, the anionic subsite at the bottom of the active-site gorge and the peripheral anionic site at the entrance to the gorge
decamethonium
-
a reversible elongated gorge-spanning inhibitor, which bridges the two sites, the anionic subsite at the bottom of the active-site gorge and the peripheral anionic site at the entrance to the gorge
edrophonium
-
a reversible active-site directed inhibitor, which interacts with the catalytic anionic subsite, at the bottom of the active-site gorge
epinorgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
galanthamine
lycorine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
N-(14-methylallyl)norgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves, structure determination by NMR spectroscopy
N-allylnorgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves, structure determination by NMR spectroscopy
narwedine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
propidium
-
a reversible peripheral anionic site inhibitor, which interacts with a site at the entrance to the gorge
tacrine
-
a reversible active-site directed inhibitor, which interacts with the catalytic anionic subsite, at the bottom of the active-site gorge
tubocurarine
-
a reversible peripheral anionic site inhibitor, which interacts with a site at the entrance to the gorge
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
kinetics, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
(+)-huperzine A
pH 7, 25°C
0.175
(-)-huperzine A
pH 7, 25°C
0.334
(-)-huperzine B
pH 7, 25°C
0.0005
(-)-S-3-[1-(dimethylamino)ethyl]phenol
pH 7.5, 25°C
0.00001112
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
pH 7.0, 22°C
0.00002986
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one
pH 7.0, 22°C
0.0183
7-O-galloyl-D-sedoheptulose
pH and temperature not specified in the publication
0.01004
loganin
pH and temperature not specified in the publication
0.01332
morroniside
pH and temperature not specified in the publication
0.027
[1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine iodide
pH 7.0, 20°C
0.0000031
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
pH 8, 25°C
0.11
buxamine-B
-
-
0.0055
buxamine-C
-
-
0.0002
galanthamine
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002606
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000133
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000288
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000844
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000914
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000045
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000553
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-6-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000298
1-benzyl-3-[4-(4-benzylpiperazin-1-yl)butyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000559
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.00039
1-[3-(4-benzylpiperazin-1-yl)propyl]-3-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.00054
1-[5-(5-nitro-1H-indazol-3-yl)thiophen-3-yl]ethanone
Tetronarce californica
-
0.0008
2-(2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl)phenol
Tetronarce californica
pH 8.0, 25°C
0.0011
2-[2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Tetronarce californica
pH 8.0, 25°C
0.0015
2-[2-(4-methylphenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Tetronarce californica
pH 8.0, 25°C
0.0387
3,3'-demethyl-grossamide
Tetronarce californica
pH 7.8, 25°C
0.0462
3,3'-demethyl-heliotropamide
Tetronarce californica
pH 7.8, 25°C
0.0000133
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000204
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000275
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000716
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.001374
3-benzyl-1-[3-(4-benzylpiperazin-1-yl)propyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000051
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.00004
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000094
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.001283
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[2,3-e]pyrazin-5(4H)-one
Tetronarce californica
-
0.000514
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[3,2-e]pyrazin-5(4H)-one
Tetronarce californica
-
0.000093
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Tetronarce californica
-
0.000015
5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.000527
5-[(1-benzylpiperidin-4-yl)methoxy]-1-methylpyrrolo[1,2-a]thieno[2,3-e]pyrazine
Tetronarce californica
-
0.000423
5-[(1-benzylpiperidin-4-yl)methoxy]pyrrolo[1,2-a]thieno[3,2-e]pyrazine
Tetronarce californica
-
0.000183
5-[4-(4-benzylpiperazin-1-yl)butyl]-7-phenyl-1,5-dihydro-4H-furo[2,3-b]pyrrolo[2,3-d]pyridin-4-one
Tetronarce californica
-
0.0105
7-O-galloyl-D-sedoheptulose
Tetronarce californica
pH and temperature not specified in the publication
0.00045
Berberine
Tetronarce californica
pH and temperature not specified in the publication
0.00006
ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.00276
galantamine
Tetronarce californica
pH 7.8, 25°C
0.00033
loganin
Tetronarce californica
pH and temperature not specified in the publication
0.00395
morroniside
Tetronarce californica
pH and temperature not specified in the publication
0.216
N-trans-caffeoyltyramine
Tetronarce californica
pH 7.8, 25°C
0.0000053
sodium 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.00182
galanthamine
Tetronarce californica
-
-
0.00016
N-(14-methylallyl)norgalanthamine
Tetronarce californica
-
-
0.00018
N-allylnorgalanthamine
Tetronarce californica
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is glycosylphosphatidylinositol-anchored
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
key amino acid differences at functional sites among AChEs of Torpedo californica, Tetranychus urticae, and Pardosa pseudoannulata, evolutionary relationships, overview
physiological function
acetylcholinesterase (AChE) is an important neurotransmitter hydrolase in invertebrate and vertebrate nervous systems. The number of AChEs is various among invertebrate species, with different functions including the classical role in terminating synaptic transmission and other non-classical roles
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACES_TETCF
586
0
65906
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structure PDB ID 4ey4
complex with rivastigmine or (-)-S-3-[1-(dimethylamino)ethyl]phenol, hanging drop vapor diffusion method
complexed with (-)-huperzine B and (+)-huperzine A
enzyme in complex with inhibitors (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one and (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one, ligands dissolved in 100 mM DMSO, soaking of native crystals at 4°C for 24 h, in a solution containing 2 mM (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one or (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one, 30% PEG 200, 8% DMSO, and 100 mM MES at pH 6.2, X-ray diffraction structure determination and analysis at 2.17.A and 2.25 A resolution, respectively
in complex with aflatoxin
native enzyme by hanging-drop vapour diffusion method, 4°C, 11.5 mg/ml protein, mother liquor is 32% PEG 200 in 0.15 M MES, pH 5.8-6.2, soaking of crystals at 4°C in mother liquor at pH 6.0, containing either 0.5 mM OTMA for 24 h in 5 ml soaking solution, 20 mM TCh for 12 h in 5 ml soaking solution, 500 mM ATCh for 40 min in 1.5 ml soaking solution, or 20 mM ATCh for 12 h in 200 ml soaking solution, X-ray diffraction structure determination and anaylsis at 2.0-2.7 A resolution
purified enzyme with bound bis-(-)-nor-meptazinol derivative 3,3'-[nonane-1,9-diylbis[(3S)-3-ethylazepane-1,3-diyl]]diphenol, trigonal crystals of the enzyme are soaked for 20 h at 4°C in 0.002 ml of 1 mM 5h dissolved in the crystallization solution containing 40% PEG 200 v/v, 150 mM MES, pH 7.4, by hanging drop procedure, X-ray diffraction structure determination and analysis at 2.7 A resolution
purified enzyme, hangingdrop vapour-diffusion method, 4°C, 11.5 mg/ml protein, the mother liquor contains 32% PEG 200, 0.15 M MES, pH 5.8-6.2, soaking of the crystals in the dark for 12 h at 4°C in mother liquor containing 5 mM [1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine iodide, pH 6.0, X-ray diffraction structure determination and anaylsis at 2.4 A resolution
trigonal and orthorhombic crystals in complex with inhibitor (RS)-tacrine(10)-hupyridone
X-ray diffraction crystal structure determination at 1.8 A resolution, crystal structure analysis of ligand-complexed enzyme and of native enzyme side-chain conformations accessed by molecular dynamics simulations, structure comparisons, overview
crystal structure analysis, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C310A
site-directed mutagenesis, the mutant shows altered sulfhydryl reagents binding and inactivation, overview
C310A/C466A
site-directed mutagenesis, the mutant shows altered sulfhydryl reagents binding and inactivation, overview
C310A/F312I
site-directed mutagenesis, the mutant shows altered sulfhydryl reagents binding and inactivation, overview
C466A
site-directed mutagenesis, the mutant shows altered sulfhydryl reagents binding and inactivation, overview
E199D
site-directed mutagenesis, the substrate inhibition is abolished in the mutant enzyme
E202Q
-
structure analysis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme by affinity chromatography on a mono-(aminocaproyl)-p-aminophenyltrimethylammonium-containing resin
native enzyme from electric organ by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in COS-7 cells
gene ache, sequence comparisons and phylogenetic analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dvir, H.; Jiang, H.L.; Wong, D.M.; Harel, M.; Chetrit, M.; He, X.C.; Jin, G.Y.; Yu, G.L.; Tang, X.C.; Silman, I.; Bai, D.L.; Sussman, J.L.
X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: Structural evidence for an active site rearrangement
Biochemistry
41
10810-10818
2002
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Bar-On, P.; Millard, C.B.; Harel, M.; Dvir, H.; Enz, A.; Sussman, J.L.; Silman, I.
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug Rivastigmine
Biochemistry
41
3555-3564
2002
Drosophila melanogaster, Homo sapiens, Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
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
Mus musculus, Tetronarce californica
Manually annotated by BRENDA team
Khalid, A.; Azim, M.K.; Parveen, S.; Atta ur, R.; Choudhary, M.I.
Structural basis of acetylcholinesterase inhibition by triterpenoidal alkaloids
Biochem. Biophys. Res. Commun.
331
1528-1532
2005
Tetronarce californica
Manually annotated by BRENDA team
Haviv, H.; Wong, D.M.; Greenblatt, H.M.; Carlier, P.R.; Pang, Y.P.; Silman, I.; Sussman, J.L.
Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase
J. Am. Chem. Soc.
127
11029-11036
2005
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Colletier, J.P.; Royant, A.; Specht, A.; Sanson, B.; Nachon, F.; Masson, P.; Zaccai, G.; Sussman, J.L.; Goeldner, M.; Silman, I.; Bourgeois, D.; Weik, M.
Use of a caged analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography
Acta Crystallogr. Sect. D
63
1115-1128
2007
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Colletier, J.P.; Fournier, D.; Greenblatt, H.M.; Stojan, J.; Sussman, J.L.; Zaccai, G.; Silman, I.; Weik, M.
Structural insights into substrate traffic and inhibition in acetylcholinesterase
EMBO J.
25
2746-2756
2006
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Pezzementi, L.; Rowland, M.; Wolfe, M.; Tsigelny, I.
Inactivation of an invertebrate acetylcholinesterase by sulfhydryl reagents: the roles of two cysteines in the catalytic gorge of the enzyme
Invert. Neurosci.
6
47-55
2006
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Weiner, L.; Shnyrov, V.L.; Konstantinovskii, L.; Roth, E.; Ashani, Y.; Silman, I.
Stabilization of Torpedo californica acetylcholinesterase by reversible inhibitors
Biochemistry
48
563-574
2009
Tetronarce californica
Manually annotated by BRENDA team
Berkov, S.; Codina, C.; Viladomat, F.; Bastida, J.
N-Alkylated galanthamine derivatives: potent acetylcholinesterase inhibitors from Leucojum aestivum
Bioorg. Med. Chem. Lett.
18
2263-2266
2008
Tetronarce californica
Manually annotated by BRENDA team
Nawaz, S.A.; Umbreen, S.; Kahlid, A.; Ansari, F.L.; Choudhary, M.I.
Structural insight into the inhibition of acetylcholinesterase by 2,3,4, 5-tetrahydro-1, 5-benzothiazepines
J. Enzyme Inhib. Med. Chem.
23
206-212
2008
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Nemukhin, A.V.; Lushchekina, S.V.; Bochenkova, A.V.; Golubeva, A.A.; Varfolomeev, S.D.
Characterization of a complete cycle of acetylcholinesterase catalysis by ab initio QM/MM modeling
J. Mol. Model.
14
409-416
2008
Tetronarce californica
Manually annotated by BRENDA team
Xu, Y.; Colletier, J.P.; Jiang, H.; Silman, I.; Sussman, J.L.; Weik, M.
Induced-fit or preexisting equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase and implications for structure-based drug design
Protein Sci.
17
601-605
2008
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Soriano, E.; Samadi, A.; Chioua, M.; Rios, C.D.; Marco-Contelles, J.
Molecular modelling, synthesis and acetylcholinesterase inhibition of ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Bioorg. Med. Chem. Lett.
20
2950-2953
2010
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Sopkova-de Oliveira Santos, J.; Lesnard, A.; Agondanou, J.H.; Dupont, N.; Godard, A.M.; Stiebing, S.; Rochais, C.; Fabis, F.; Dallemagne, P.; Bureau, R.; Rault, S.
Virtual screening discovery of new acetylcholinesterase inhibitors issued from CERMN chemical library
J. Chem. Inf. Model.
50
422-428
2010
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Paz, A.; Xie, Q.; Greenblatt, H.M.; Fu, W.; Tang, Y.; Silman, I.; Qiu, Z.; Sussman, J.L.
The crystal structure of a complex of acetylcholinesterase with a bis-(-)-nor-meptazinol derivative reveals disruption of the catalytic triad
J. Med. Chem.
52
2543-2549
2009
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Sanson, B.; Colletier, J.P.; Xu, Y.; Lang, P.T.; Jiang, H.; Silman, I.; Sussman, J.L.; Weik, M.
Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations
Protein Sci.
20
1114-1118
2011
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team
Meirer, K.; Glatzel, D.; Kretschmer, S.; Wittmann, S.K.; Hartmann, M.; Bloecher, R.; Angioni, C.; Geisslinger, G.; Steinhilber, D.; Hofmann, B.; Fuerst, R.; Proschak, E.
Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase
Molecules
22
45
2016
Pardosa pseudoannulata (A0A1B1FIV8), Pardosa pseudoannulata (A0A1B1FIW0), Pardosa pseudoannulata (A0A1B1FIW2), Pardosa pseudoannulata (A0A1B1FIZ1), Pardosa pseudoannulata (V5QQC6), Tetronarce californica (P04058), Homo sapiens (P22303), Tetranychus urticae (Q86CZ4)
Manually annotated by BRENDA team
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
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Lalut, J.; Santoni, G.; Karila, D.; Lecoutey, C.; Davis, A.; Nachon, F.; Silman, I.; Sussman, J.; Weik, M.; Maurice, T.; Dallemagne, P.; Rochais, C.
Novel multitarget-directed ligands targeting acetylcholinesterase and sigma1 receptors as lead compounds for treatment of Alzheimers disease synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase
Eur. J. Med. Chem.
162
234-248
2018
Tetronarce californica (P04058), Tetronarce californica, Homo sapiens (P22303)
Manually annotated by BRENDA team
Yan, X.; Tang, J.; dos Santos Passos, C.; Nurisso, A.; Simoes-Pires, C.A.; Ji, M.; Lou, H.; Fan, P.
Characterization of lignanamides from hemp (Cannabis sativa L.) seed and their antioxidant and acetylcholinesterase inhibitory activities
J. Agric. Food Chem.
63
10611-10619
2015
Tetronarce californica (P04058)
Manually annotated by BRENDA team
Caliandro, R.; Pesaresi, A.; Cariati, L.; Procopio, A.; Oliverio, M.; Lamba, D.
Kinetic and structural studies on the interactions of Torpedo californica acetylcholinesterase with two donepezil-like rigid analogues
J. Enzyme Inhib. Med. Chem.
33
794-803
2018
Tetronarce californica (P04058), Tetronarce californica
Manually annotated by BRENDA team