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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Bos taurus and UniProt Accession P23795

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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:
Bos taurus
UNIPROT: P23795
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
acetylcholinesterase
-
AcCholE
-
-
-
-
acetyl beta-methylcholinesterase
-
-
-
-
acetyl cholinesterase
-
-
acetylcholine esterase
-
-
-
-
acetylcholine hydrolase
-
-
-
-
acetylthiocholinesterase
-
-
-
-
choline esterase I
-
-
-
-
cholinesterase
-
-
-
-
esterase, acetyl choline
-
-
-
-
true cholinesterase
-
-
-
-
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
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
-
-
-
?
acetylcholine + H2O
?
show the reaction diagram
-
inactivation of transmitter substance operating in cholinergic neurotransmission
-
-
?
acetylcholine + H2O
acetate + choline
show the reaction diagram
-
-
-
-
?
acetylcholine + H2O
choline + acetate
show the reaction diagram
-
-
-
-
?
acetylcholine iodide + H2O
acetate + choline iodide
show the reaction diagram
-
-
-
-
?
acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
-
-
-
-
?
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
aryl-acyl-amides + H2O
?
show the reaction diagram
-
-
-
-
?
butyrylthiocholine + H2O
butyrate + thiocholine
show the reaction diagram
-
-
-
-
?
Leu + Arg
Tyr + Gly
show the reaction diagram
-
-
-
?
Leu + Met
substance P
show the reaction diagram
-
-
-
?
neuropeptides + H2O
?
show the reaction diagram
-
degradation
-
-
?
Phe + Leu
Gly + Gly + Gly
show the reaction diagram
-
-
-
?
propionylthiocholine + H2O
propanoate + thiocholine
show the reaction diagram
-
-
-
-
?
[leu5] enkephalin + H2O
Tyr + Leu
show the reaction diagram
-
-
-
?
[met5] enkephalins + H2O
Tyr + Met
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
acetylthiocholine + H2O
thiocholine + acetate
show the reaction diagram
-
-
-
?
acetylcholine + H2O
?
show the reaction diagram
-
inactivation of transmitter substance operating in cholinergic neurotransmission
-
-
?
acetylcholine + H2O
acetate + choline
show the reaction diagram
-
-
-
-
?
acetylcholine + H2O
choline + acetate
show the reaction diagram
-
-
-
-
?
neuropeptides + H2O
?
show the reaction diagram
-
degradation
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetylthiocholine
the enzyme AChE is inhibited by high concentrations of substrate
chlorpyrifos
an anti-cholinesterase organophosphate insecticide used in the production of food derived from animal, fruit and horticultural origin. The therapeutic treatment of castrated male bovines treated with chlorpyrifos, applied by pour-on according to the manufacturer's instructions, does not cause changes in the variables evaluated, i.e. total proteins, liver enzymes, urea, and creatinine
(+)-2-carene
-
50% inhibition at 0.90 mM
(+)-3-carene
-
50% inhibition at 0.20 mM
(+)-alpha-pinene
-
50% inhibition at 0.4 mM
(+)-borneol
-
1 mM, 22.2% inhibition
(+)-Camphor
-
1 mM, 26.4% inhibition
(+)-cis-verbenol
-
1 mM, 17.7% inhibition
(+)-fenchol
-
1 mM, 37.7% inhibition
(+)-fenchone
-
1 mM, 23.3 inhibition
(+)-trans-myrtanol
-
1 mM, 37.15% inhibition
(-)-alpha-pinene
-
50% inhibition at 0.44 mM
(-)-beta-pinene
-
1 mM, 48.5% inhibition
(-)-borneol
-
1 mM, 22.6% inhibition
(-)-Camphor
-
1 mM, 21.2% inhibition
(-)-fenchone
-
1 mM, 28.2% inhibition
(-)-myrtenol
-
1 mM, 15.0% inhibition
(-)-trans-myrtanol
-
1 mM, 37.4% inhibition
(-)-verbenone
-
1 mM, 12.6% inhibition
1,5-Bis(4-allyldimethylammonium phenyl)pentan-3-one
-
-
1alpha,2alpha,6beta, 8alpha,15-pentaacetoxy-9beta-benzoyloxy-beta-agarofuran
-
-
1alpha,2alpha,6beta,8alpha-tetraacetoxy-9beta-benzoyloxy-15-hydroxy-beta-agarofuran
-
-
1alpha,2alpha,6beta-triacetoxy-9beta-benzoyloxy-15-hydroxy-beta-agarofuran
-
-
1alpha,2alpha,6beta-triacetoxy-9beta-benzoyloxy-8alpha,15-dihydroxy-beta-agarofuran
-
-
1alpha,6beta,8alpha-triacetoxy-9beta-furoyloxy-beta-agarofuran
-
IC50 is 0.0029 mg/ml
1alpha-acetoxy-6beta,9beta-difuroyloxy-4beta-hydroxy-beta-agarofuran
-
-
2-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
-
2-chlorophenyl 1-methylhydrazinecarboxylate
-
-
3-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
-
3-chlorophenyl 1-methylhydrazinecarboxylate
-
-
3-N,N-diethylaminophenyl-N'-(1-alkyl) carbamates
-
inhibit quickly by carbamoylation
3-N,N-diethylaminophenyl-N'-(1-butyl) carbamate
-
-
3-N,N-diethylaminophenyl-N'-(1-ethyl) carbamate
-
-
3-N,N-diethylaminophenyl-N'-(1-hexyl) carbamate
-
-
3-N,N-diethylaminophenyl-N'-(1-octyl) carbamate
-
-
3-N,N-diethylaminophenyl-N'-(1-propyl) carbamate
-
-
4-chlorophenyl 1,2-dimethylhydrazinecarboxylate
-
-
4-chlorophenyl 1-methylhydrazinecarboxylate
-
-
6beta,8alpha-diacetoxy-9beta-furoyloxy-1alpha-hydroxy-beta-agarofuran
-
-
galanthamine
-
-
hexamethonium
-
-
lidocain
-
-
lycoparin C
-
an alkaloid from Lycopodium casuarinoides, NMR structure determination and analysis, overview
mahanimbine
-
i.e. 3, 5-dimethyl-3-(4-methylpent-3-enyl)-11H-pyrano [5,6-a] carbazole, IC50 is 0.03 g/ml, isolated from the petroleum ether extract of the leaves of Murraya koenigii, an Indian medical plant
phenyl 1,2-dimethylhydrazinecarboxylate
-
-
phenyl 1-methylhydrazinecarboxylate
-
-
physostigmine
-
-
rivastigmin
-
-
sevin
-
-
Trigonelline
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
acetylthiocholine
-
1.78
butyrylthiocholine
-
-
0.137
propionylthiocholine
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5300
acetylthiocholine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
(+)-2-carene
-
25°C
0.03
(+)-3-carene
-
25°C
0.15
(+)-alpha-pinene
-
25°C
1.92
(+)-fenchol
-
25°C
2.03
(+)-fenchone
-
25°C
0.17
(-)-alpha-pinene
-
25°C
1.1
(-)-beta-pinene
-
25°C
1.99
(-)-fenchone
-
25°C
additional information
additional information
-
inhibition kinetics, value of carbamoylation inhibition
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33
1alpha,2alpha,6beta, 8alpha,15-pentaacetoxy-9beta-benzoyloxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.12
1alpha,2alpha,6beta,8alpha-tetraacetoxy-9beta-benzoyloxy-15-hydroxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.26
1alpha,2alpha,6beta-triacetoxy-9beta-benzoyloxy-15-hydroxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.4
1alpha,2alpha,6beta-triacetoxy-9beta-benzoyloxy-8alpha,15-dihydroxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.74
1alpha-acetoxy-6beta,9beta-difuroyloxy-4beta-hydroxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.74
6beta,8alpha-diacetoxy-9beta-furoyloxy-1alpha-hydroxy-beta-agarofuran
Bos taurus
-
pH 7.6, 22°C
0.00127 - 0.1
galanthamine
0.025
lycoparin C
Bos taurus
-
-
0.233
Trigonelline
Bos taurus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135.7
-
enzyme immobilized on FSM-16
187.7
-
enzyme immobilized on MCM-41, which shows catalytic activity as well of 47.36 nmol/min/mg
193.2
-
free enzyme
3.5
-
-
372
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.6
-
assay at
8
-
assay at
8.25
-
Triton-solubilized enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
22
-
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
matrix
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
acetylcholinesterase (AChE) is mainly present in erythrocytes, typically hydrolyzes acetylthiocholine (ATC) and is inhibited by excessive substrate. In cattle, 90% of cholinesterase enzyme activity is represented by AChE in erythrocytes with very low plasma BChE values
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACES_BOVIN
613
0
67664
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
-
non-denaturing PAGE
250000
-
gel filtration
77000
-
2 * 77000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 77000, SDS-PAGE
monomer or dimer
-
dependent on purification method
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
glycoprotein
-
four N-glycans
sialoprotein
-
-
side-chain modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
catalytic activity of acetylcholinesterase immobilized on mesoporous molecular sieves, efficiency of different materials, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
more than 75% activity retained after 5 min, pI-specific-phospholipase C-solubilized
60
-
more than 90% loss of activity after 5 min, Triton X-100-solubilized
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
circulatory retention of heterologous AChE in non-human primates is dependent on sialic acid content of the enzyme. AChE without sialic acid residues is rapidly eliminated from the circulation.
-
labile to freezing, glycerol stabilizes
-
Triton X-100 and Tween 20 stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 8 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of T-subunit in HEK-293 cells
expressed in HEK-293 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beauregard, G.; Roufogalis, B.D.
Involvement of calcium ions in the properties of cardiolipin-associated erythrocyte acetylcholinesterase
Biochim. Biophys. Acta
557
102-111
1979
Bos taurus
Manually annotated by BRENDA team
Grossmann, H.; Lieflaender, M.
Acetylcholinesterase aus Rindererythrozyten. Reinigung und Eigenschaften des mit und ohne Triton X-100 solubilisierten Enzyms
Z. Naturforsch. C
34
721-725
1979
Bos taurus
Manually annotated by BRENDA team
Taguchi, R.; Suzuki, K.; Nakabayashi, T.; Ikezawa, H.
Acetylcholinesterase release from mammalian erythrocytes by phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis and characterization of the released enzyme
J. Biochem.
96
437-446
1984
Bos taurus
Manually annotated by BRENDA team
Brodbeck, U.
Multiple molecular forms of acetylcholinesterase and their possible role in the degradation of neurohormones
Colloq. Ges. Biol. Chem. Mosbach
36
22-32
1985
Bos taurus, Gallus gallus, Rattus norvegicus, Torpedo sp.
-
Manually annotated by BRENDA team
Ott, P.
Membrane acetylcholinesterases: purification, molecular properties and interactions with amphiphilic environments
Biochim. Biophys. Acta
822
375-392
1985
Bos taurus, Gallus gallus, Homo sapiens, Rattus norvegicus, Torpedo sp.
Manually annotated by BRENDA team
Taguchi, R.; Ikezawa, H.
Properties of bovine erythrocyte acetylcholinesterase solubilized by phosphatidylinositol-specific phospholipase C
J. Biochem.
102
803-811
1987
Bos taurus
Manually annotated by BRENDA team
Ralston, J.S.; Rush, R.S.; Doctor, B.P.; Wolfe, A.D.
Acetylcholinesterase from fetal bovine serum. Purification and characterization of soluble G4 enzyme
J. Biol. Chem.
260
4312-4318
1985
Bos taurus
Manually annotated by BRENDA team
Mendelson, I.; Kronman, C.; Ariel, N.; Shafferman, A.; Velan, B.
Bovine acetylcholinesterase: cloning, expression and characterization
Biochem. J.
334
251-259
1998
Bos taurus (P23795), Bos taurus
Manually annotated by BRENDA team
Hannesson, H.H.; DeVries, G.H.
Properties of acetylcholinesterase in axolemma-enriched fractions isolated from bovine splenic nerve
J. Neurosci. Res.
27
84-88
1990
Bos taurus
Manually annotated by BRENDA team
Nichol, C.P.; Roufogalis, B.D.
Influence of associated lipid on the properties of purified bovine erythrocyte acetylcholinesterase
Biochem. Cell Biol.
69
154-162
1991
Bos taurus
Manually annotated by BRENDA team
Liao, J.; Boschetti, N.; Mortensen, V.; Jensen, S.P.; Koch, C.; Norgaard-Petersen, B.; Brodbeck, U.
Characterization of salt-soluble forms of acetylcholinesterase from bovine brain
J. Neurochem.
63
1446-1453
1994
Bos taurus
Manually annotated by BRENDA team
Schmidt-Dannert, C.; Kalisz, H.M.; Safarik, I.; Schmid, R.D.
Improved properties of bovine erythrocyte acetylcholinesterase, isolated by papain cleavage
J. Biotechnol.
36
231-237
1994
Bos taurus
Manually annotated by BRENDA team
Cohen, O.; Kronman, C.; Velan, B.; Shafferman, A.
Amino acid domains control the circulatory residence time of primate acetylcholinesterases in rhesus macaques (Macaca mulatta)
Biochem. J.
378
117-128
2004
Bos taurus, Homo sapiens, Macaca mulatta (Q67BC1), Macaca mulatta (Q67BC2), Macaca mulatta
Manually annotated by BRENDA team
Miyazawa, M.; Yamafuji, C.
Inhibition of acetylcholinesterase activity by bicyclic monoterpenoids
J. Agric. Food Chem.
53
1765-1768
2005
Bos taurus
Manually annotated by BRENDA team
Rosales-Hernandez, M.C.; Mendieta-Wejebe, J.E.; Correa-Basurto, J.; Vazquez-Alcantara, J.I.; Terres-Rojas, E.; Trujillo-Ferrara, J.
Catalytic activity of acetylcholinesterase immobilized on mesoporous molecular sieves
Int. J. Biol. Macromol.
40
444-448
2007
Bos taurus
Manually annotated by BRENDA team
Zdrazilova, P.; Stepankova, S.; Komersova, A.; Vranova, M.; Komers, K.; Cegan, A.
Kinetics of 13 new cholinesterase inhibitors
Z. Naturforsch. C
61
611-617
2006
Bos taurus, Electrophorus electricus
Manually annotated by BRENDA team
Hirasawa, Y.; Kato, E.; Kobayashi, J.; Kawahara, N.; Goda, Y.; Shiro, M.; Morita, H.
Lycoparins A-C, new alkaloids from Lycopodium casuarinoides inhibiting acetylcholinesterase
Bioorg. Med. Chem.
16
6167-6171
2008
Bos taurus
Manually annotated by BRENDA team
Satheeshkumar, N.; Mukherjee, P.K.; Bhadra, S.; Saha, B.P.
Acetylcholinesterase enzyme inhibitory potential of standardized extract of Trigonella foenum graecum L. and its constituents
Phytomedicine
17
292-295
2010
Bos taurus
Manually annotated by BRENDA team
Kumar, N.S.; Mukherjee, P.K.; Bhadra, S.; Saha, B.P.; Pal, B.C.
Acetylcholinesterase inhibitory potential of a carbazole alkaloid, mahanimbine, from Murraya koenigii
Phytother. Res.
24
629-631
2010
Bos taurus
Manually annotated by BRENDA team
Alarcon, J.; Astudillo, L.; Gutierrez, M.
Inhibition of acetylcholinesterase activity by dihydro-beta-agarofuran sesquiterpenes isolated from Chilean Celastraceae
Z. Naturforsch. C
63
853-856
2009
Bos taurus
Manually annotated by BRENDA team
Ferre, D.M.; Lentini, V.R.; Romano, R.R.; Luduena, H.R.; Jotallan, P.J.; Gorla, N.B.M.
Reference values for acetyl and butyrylcholinesterases in cattle under actual management conditions, hepatic and renal function by application of chlorpyrifos
J. Environ. Sci. Health B
53
191-198
2018
Bos taurus (P23795)
Manually annotated by BRENDA team