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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Mus musculus and UniProt Accession P21836

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     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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Select one or more organisms in this record:
This record set is specific for:
Mus musculus
UNIPROT: P21836
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
AcCholE, ACE, ACE-1, AcE1, ace1a, ace1b, ACE2, ace2-type acetylcholinesterase, ace3, ace4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AcCholE
-
-
-
-
acetyl beta-methylcholinesterase
-
-
-
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acetylcholine esterase
-
-
-
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acetylcholine hydrolase
-
-
-
-
acetylthiocholinesterase
-
-
-
-
choline esterase I
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-
-
-
cholinesterase
-
-
-
-
esterase, acetyl choline
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-
-
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true cholinesterase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetylcholine + H2O = choline + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
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transacetylation
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-
-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylcholine acetylhydrolase
Acts on a variety of acetic esters; also catalyses transacetylations.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-81-1
-
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
-
-
-
-
?
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
acetylthiocholine iodide + H2O
thiocholine iodide + acetate
show the reaction diagram
alkyl methylphosphonfluoridate + H2O
?
show the reaction diagram
-
oxime-assisted catalysis of organophosphates by AChE, mechanism, reaction system, overview
-
-
?
butyrylthiocholine + H2O
thiocholine + butyrate
show the reaction diagram
S-acetylthiocholine + H2O
acetate + thiocholine
show the reaction diagram
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detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
S-acetylthiocholine iodide + H2O
acetate + thiocholine iodide
show the reaction diagram
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detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
succinyldicholine + H2O
2 choline + succinate
show the reaction diagram
-
-
-
-
?
additional information
?
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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
-
-
-
-
?
acetylcholine + H2O
acetate + choline
show the reaction diagram
acetylcholine + H2O
choline + acetate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aluminium chloride
-
activates the enzyme in vitro and in vivo after oral treatment
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclosarin
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-
fenamiphos
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an organophosphorus compound and insecticide
russian VX
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-
Tabun
-
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(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
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E2020, acetylcholinesterase inhibitor used in treatment of Alzheimer's diaease, inhibition kinetics
1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide
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2,2-dichlorovinyl dimethyl phosphate
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i.e. DDVP, reversible, detailed kinetic analysis
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
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i.e. 2-PAM, reversible, detailed kinetic analysis
3,3-dimethylbutyl methylphosphonyl thiocholine
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-
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
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i.e. HI-6, reversible, detailed kinetic analysis
4-ketoamyltrimethylammonium
-
binding structure analysis
4-O-methylhonokiol
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isolated from ethanol extract of Magnolia officinalis. 4-O-methylhonokiol also dose-dependently attenuates the scopolamine-induced increase of AChE activity in the cortex and hippocampus of mice
Acetylcholine
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substrate inhibition
aflatoxin B1
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50% inhibition at 0.031 mM by increase of Km-value and decrease of vmax-value. Partial recativation by 2-aldoxime, i.e. 2-PAM, pyridin-2-aldoxime 1-methoiodide
bambuterol
-
a specific and stereoselective inhibitor of butyrylcholinesterase, which is about 8000times faster inhibted than acetylcholinesterase. AChE wild-type enzyme, and mutants F297I/Y337A and F295L/F297I/Y337A show a deviation from linearity, either enzymes are inhibited by racemate or enantiomers, indicating the presence of reversible enzyme-inhibitor complex, overview
batimastat
-
-
BW248c51
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i.e. 1,5-bis(4-allyldimethyl-ammoniumphenyl)pentane-3-one dibromide, specific inhibition of AChE
BW284c51
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50% inhibition at 0.000021 mM
choline
-
product inhibition, binding structure analysis
cycloheptyl methylphosphonyl thiocholine
-
SP and RP enantiomers
diisopropyl fluorophosphate
-
nerve agent, binding structure, overview
donepezil
edrophonium
-
-
EDTA
-
-
eserine
-
-
fasciculin
-
fenamiphos
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an organophosphorous-based insecticide, binding structure, overview
galanthamine
huperzine
-
binds at the base of the active site gorge, has no effect on the mobility of reporter groups attached to L76C and Y124C, increases the mobility of reporter groups attached to E81C and E84C
Insulin
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AChE activity in detergent soluble fraction of scopolamine amnesic mice is inhibited by donepezil, insulin and melatonin with varying extent in different brain regions, whereas AChE activity in salt soluble fraction is not much affected, overview
-
isopropyl methylphosphonyl thiocholine
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SP and RP enantiomers
m-(N,N,N-trimethylammonio)-trifluoroacetophenone
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binding structure analysis
Melatonin
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AChE activity in detergent soluble fraction of scopolamine amnesic mice is inhibited by donepezil, insulin and melatonin with varying extent in different brain regions, whereas AChE activity in salt soluble fraction is not much affected, overview
methamidophos
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an organophosphorous-based insecticide, binding structure, overview
methyl (3-{4-[({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}propyl)phosphonofluoridate
-
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methyl (3-{4-[({[6-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}propyl)phosphonofluoridate
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methyl (4-{4-[({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}butyl)phosphonofluoridate
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methyl (4-{4-[({[6-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl}amino)methyl]-1H-1,2,3-triazol-1-yl}butyl)phosphonofluoridate
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methyl paraoxon
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reversible binding to a site on acetylcholinesterase distinct from the active site reduces their subsequent capacity to phosphorylate the active site, probably by steric hindrance or allosteric modification of the active site
methyl [3-(4-{[(4-{(E)-[4-(dimethylamino)phenyl]diazenyl}benzoyl)amino]methyl}-1H-1,2,3-triazol-1-yl)propyl]phosphonofluoridate
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methyl [3-(4-{[(pyren-2-ylsulfonyl)amino]methyl}-1H-1,2,3-triazol-1-yl)propyl]phosphonofluoridate
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methyl [4-(4-{[(4-{(E)-[4-(dimethylamino)phenyl]diazenyl}benzoyl)amino]methyl}-1H-1,2,3-triazol-1-yl)butyl]phosphonofluoridate
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methyl [4-(4-{[(pyren-2-ylsulfonyl)amino]methyl}-1H-1,2,3-triazol-1-yl)butyl]phosphonofluoridate
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methyl {3-[4-({[(6-methoxy-2-oxo-2H-chromen-3-yl)carbonyl]amino}methyl)-1H-1,2,3-triazol-1-yl]propyl}phosphonofluoridate
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methyl {4-[4-({[(6-methoxy-2-oxo-2H-chromen-3-yl)carbonyl]amino}methyl)-1H-1,2,3-triazol-1-yl]butyl}phosphonofluoridate
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methylorganophosphonates
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the Sp-enantiomer is more reactive
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muscarine
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treatment with 0.01 mM muscarine leads to a 20% decrease in enzyme activity in SN-56 cells
O-O-dimethyl-O-(2,2-dichlorovinyl)phosphate
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phosphorylates the active site serine
paraoxon
RP cycloheptyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can only poorly be reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
RP-3,3-dimethylbutyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can only poorly be reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
RP-isopropyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
sarin
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nerve agent, binding structure, overview
SP-3,3-dimethylbutyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
SP-cycloheptyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
SP-isopropyl methylphosphonyl thiocholine
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phosphonylates the enzyme, wild-type enzyme and mutant enzymes can be partially reactivated by 1-(2'-hydroxyiminomethyl-1'-pyridinium)-3-(4''-carbamoyl-1''-pyridinium)-2-oxapropane dichloride or 2-(hydroxyiminomethyl)-1-methylpyridinium iodide
succinyldicholine
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substrate inhibition, binding structure analysis
Tabun
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an organophosphorous inhibitor
tacrine
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tea polyphenol
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up to 60% inhibition of enzyme
TFK+
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analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview
TFK0
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analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview
trifluoroacetophenone
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inhibits Y124C mutant slower than the wild-type enzyme
VX (nerve agent)
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i.e. O-ethyl S-2-isopropylaminoethyl methylphosphonothiolate, nerve agent, binding structure, overview
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aluminium lactate
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activates the enzyme in vitro and in vivo after oral treatment
Carbachol
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0.01 mM carbachol leads to a significant increase in enzyme activity in SH-SY5Y cells; a 15 min pretreatment of the cells at 37°C with 0.01 mM atropine completely ablates the carbachol-induced increase in enzyme activity
presenilin 1
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PS1, required for enzyme activity in the brain, overview. PS1-deficient mice show upregulation of AChE activity in major cholinergic cell nuclei and in cortical and thalamic regions responsible for selective attention and visuomotor coordination, as well as limbic structures with related regions involved in cognition, arousal, emotion, and plasticit, overview
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Scopolamine
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induces and increase of AChE activity in the cortex and hippocampus of mice
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 2.36
Acetylcholine
0.04 - 2.5
acetylthiocholine
0.054 - 0.19
acetylthiocholine iodide
0.093
butyrylthiocholine
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pH 7.0, 22°C, recombinant wild-type enzyme
additional information
additional information
-
ligand binding kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 4350
Acetylcholine
2330 - 3170
acetylthiocholine iodide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000004 - 0.0087
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
0.15 - 1.7
2-((Z)-(hydroxyimino)methyl)-1-methylpyridinium chloride
0.046 - 0.36
4-(aminocarbonyl)-1-(((2-((Z)-(hydroxyimino)methyl)pyridinium-1-yl)methoxy)methyl)pyridinium dichloride
0.023
4-ketoamyltrimethylammonium
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pH 7.0, 22°C, recombinant wild-type enzyme
1.4
choline
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pH 7.0, 22°C, recombinant wild-type enzyme
0.021
succinyldicholine
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pH 7.0, 22°C, recombinant wild-type enzyme
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000012
4-O-methylhonokiol
Mus musculus
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pH 7.4, 25°C
0.000135
tacrine
Mus musculus
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pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7700
-
-
additional information
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enzyme activity in wild-type and PS1/A246E transgenic mice, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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assay at
7
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assay at
7.4
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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recombinant enzyme
Manually annotated by BRENDA team
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first enzyme appearance in the developing cervical loops of the enamel organ, but does not appear in the enamel knot, overview
Manually annotated by BRENDA team
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dental, inner enamel epithelium except cervical-loop area in inscisors and neonatal mice, not in the outer enamel epithelium, temporospatial localization of enzyme activity in the dental epithelium during mouse tooth development, overview
Manually annotated by BRENDA team
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normal and dystrophic heart
Manually annotated by BRENDA team
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forebrain cholinergic neurons
Manually annotated by BRENDA team
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inner enamel epithelium except cervical-loop area in inscisors and neonatal mice, temporospatial localization of enzyme activity in the dental epithelium during mouse tooth development, AChE localization in mandibular and maxillary tooth buds, also in the enamel-free area, but weakly in the dental papilla and its neural elements, and not in the outer enamel epithelium, stellate reticulum, and ameloblasts, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme anchorage in the membrane is established via the proline rich membrane anchor transmembrane protein
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ACES_MOUSE
614
0
68169
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
monomer, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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sedimentation analysis
monomer
-
truncated enzyme
additional information
-
primary and tertiary structure determination and anaylsis, the active site gorge forms asterically confined environment
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme bound to inhibitor fenamiphos and oxime-based reactivators [(E)-[1-[(4-carbamoylpyridin-1-ium-1-yl)methoxymethyl]pyridin-2-ylidene]methyl]-oxoazanium dichloride, and 1,7-heptylene-bis-N,N0-2-pyridiniumaldoxime dichloride, mixture of 0.001 ml 20 mg/ml AChE with 0.001 ml well solution containing 28% PEG750MME and 0.1mM HEPES, pH 7.0-7.2, saturated with fenamiphos, for 22-25 h, crystals are soakened in inhibitor solution, X-ray diffraction structure determination and analysis at 2.4-2.7 A resolution
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enzyme in complex with inhibitors, nerve agents and organophosphorous-based insecticides, in aged and non-aged forms, the non-aged complexes are generated by crystal soaking methods, by slow equilibration of crystals in X-buffer composed of 28% v/v PEG monomethyl ether 750, and 100 mM HEPES, pH 7.0, prior to data collection, X-buffer is supplemented with the appropriate organophosphorous compound at a concentration of 10 mM for sarin, VX, and diisopropyl fluorophosphate and 100 mM for methamidophos and fenamifos, the solution is subsequently added to the equilibrated crystals in several portions during different periods, aged forms establish during several weeks, X-ray diffraction structure determination and anaylsis at 2.5-2.9 A resolution, modelling
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in complex with tabun, prior and after intramolecular dealkylation or deamidation reaction caused by tabun and called aging. Nonaged tabun conjugate induces a structural change at H447 that uncouples the catalytic triad. In aged tabun conjugate, side chains of H447 and F338 are reversed to the conformation of the apo structure of enzyme
-
purified wild-type enzyme and mutant S203A in complex with substrates acetylcholine, acetylthiocholine, succinyldicholine, and butyrylthiocholine, and two nonhydrolyzable substrate analogues (m-N,N,N-trimethylammonio)-trifluoroacetophenone and 4-ketoamyltrimethylammonium, by hanging drop vapor diffusion at 4°C, using a protein-to-well solution ratio of 1:1, with well solution containing 25–32% v/v P550MME or P600 in either 60-100 mM HEPES or sodium acetate, pH 6.5-pH 8.0, he TMTFA-mAChE complex is formed in solution using apo-mAChE at 5.0 mg/ml, and a 3-fold molar excess of the ligand over the enzyme, concentrated prior to crystallization, the other seven complexes are generated by crystal soaking, carried out at 4 °C in 0.02 ml sitting drops made of well solution supplemented with the 250 mM ligand and polyethylene glycol up to 35%, X-ray diffraction structure determination and anaylsis at 2.05-2.65 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A262C
D74N
-
altered Ki for E2020
F295A/Y337A
-
mutant retains hydrolytic activity
F295L
F295L/F297I/Y337A
-
mutant enzyme can be partially reactivated after phosphonylation
F295L/Y337A
F296L/F297I/Y337A
-
site-directed mutagenesis, the mutant shows a 14fold decreased inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
F297I
F297I/Y337A
H287C
H447I
-
inhibitor TFK+ binding to the H447I mutant proceeds with a different reaction mechanism from the wild-type enzyme. A water molecule takes over the role of His447 and participates in the bond breaking and forming as a charge relayer. Unlike in the wild-type mAChE case, Glu334, a conserved residue from the catalytic triad, acts as a catalytic base in the reaction
S203A
-
site-directed mutagenesis of the catalytic site residue, inactive mutant
W286A
W86A
-
altered Ki for E2020
Y124C
Y124C-acrylodan
-
mutant retains hydrolytic activity
Y124C-benzyl
-
mutant retains hydrolytic activity
Y124C-N(CH3)3+
-
mutant with increased Km
Y124C-NH3+
-
mutant with increased Km
Y124C-SO3-
-
mutant retains hydrolytic activity
Y124Q
Y337A
Y337A/E202Q/F295A
-
mutant retains hydrolytic activity
Y337A/F295A/F297A
-
4fold increased Km
Y337A/F295L/F297I
-
mutant retains hydrolytic activity
Y337A/F295L/Y338A
-
no substrate inactivation
Y337A/F338A
Y337F
-
altered Ki for E2020
Y72N/Y124N/W286R
-
altered Ki for E2020
Y72N/Y124Q/Y337A
-
site-directed mutagenesis, the mutant shows an altered inhibition rate with inhibitor bambuterol compared to the wild-type enzyme
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant soluble wild-type and mutant enzymes from HEK-293 cells by by affinity chromatography with elution using either propidium diiodide or SCh dichloride, followed by dialysis
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally truncated enzyme in HEK-293 cells
-
expression of soluble wild-type and mutant enzymes in HEK-293 cells
-
truncated at position 548
-
truncated form terminated at position 548, expressed in HEK-293 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
AChE, when conjugated with organophosphorous compounds, is employed as a template for socalled click-chemistry, freeze-frame synthesis of nucleophilic reactivating agents that could potentially prove useful in AChE reactivation at the target site as well as in catalytic scavenging of organophosphates in plasma, overview
medicine
-
chronic administration of tea polyphenol significantly reverses scopolamine-induced retention deficits in both step-through passive avoidance and spontaneous alternation behavioural tasks. Additionally, tea polyphenol inhibits enzyme activity and may be useful in treatment of Alzheimer’s disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bourne, Y.; Taylor, P.; Bougis, P.E.; Marchot, P.
Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly
J. Biol. Chem.
274
2963-2970
1999
Mus musculus
Manually annotated by BRENDA team
Marchot, P.; Ravelli, R.B.G.; Raves, M.L.; Bourne, Y.; Vellom, D.C.; Kanter, J.; Camp, S.; Sussman, J.L.; Taylor, P.
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin
Protein Sci.
5
672-679
1996
Mus musculus
Manually annotated by BRENDA team
Gomez, J.L.; Moral-Naranjo, M.T.; Compoy, F.J.; Vidal, C.J.
Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart
J. Neurosci. Res.
56
295-306
1999
Mus musculus
Manually annotated by BRENDA team
Kovarik, Z.; Radic, Z.; Berman, H.A.; Simeon-Rudolf, V.; Reiner, E.; Taylor, P.
Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates
Biochem. J.
373
33-40
2003
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Kovarik, Z.; Radic, Z.; Berman, H.A.; Simeon-Rudolf, V.; Reiner, E.; Taylor, P.
Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates
Biochemistry
43
3222-3229
2004
Mus musculus
Manually annotated by BRENDA team
Zatta, P.; Ibn-Lkhayat-Idrissi, M.; Zambenedetti, P.; Kilyen, M.; Kiss, T.
In vivo and in vitro effects of aluminum on the activity of mouse brain acetylcholinesterase
Brain Res. Bull.
59
41-45
2002
Mus musculus
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
Gomez, J.L.; Nieto-Ceron, S.; Campoy, F.J.; Munoz-Delgado, E.; Vidal, C.J.
Purification and properties of hydrophilic dimers of acetylcholinesterase from mouse erythrocytes
Int. J. Biochem. Cell Biol.
35
1109-1118
2003
Mus musculus
Manually annotated by BRENDA team
Kua, J.; Zhang, Y.; McCammon, J.A.
Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach
J. Am. Chem. Soc.
124
8260-8267
2002
Mus musculus
Manually annotated by BRENDA team
Boyd, A.E.; Marnett, A.B.; Wong, L.; Taylor, P.
Probing the active center gorge of acetylcholinesterase by fluorophores linked to substituted cysteines
J. Biol. Chem.
275
22401-22408
2000
Mus musculus
Manually annotated by BRENDA team
Shi, J.; Boyd, A.E.; Radic, Z.; Taylor, P.
Reversibly bound and covalently attached ligands induce conformational changes in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase
J. Biol. Chem.
276
42196-42204
2001
Mus musculus
Manually annotated by BRENDA team
Shi, J.; Tai, K.; McCammon, J.A.; Taylor, P.; Johnson, D.A.
Nanosecond dynamics of the mouse acetylcholinesterase Cys69-Cys96 omega loop
J. Biol. Chem.
278
30905-30911
2003
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Kardos, S.A.; Sultatos, L.G.
Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase
Toxicol. Sci.
58
118-126
2000
Mus musculus
Manually annotated by BRENDA team
Kovarik, Z.; Ciban, N.; Radic, Z.; Simeon-Rudolf, V.; Taylor, P.
Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP
Biochem. Biophys. Res. Commun.
342
973-978
2006
Mus musculus
Manually annotated by BRENDA team
Ekstrom, F.; Akfur, C.; Tunemalm, A.K.; Lundberg, S.
Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase
Biochemistry
45
74-81
2006
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Kim, H.K.; Kim, M.; Kim, S.; Kim, M; Chung, J.H.
Effects of green tea polyphenol on cognitive and acetylcholinesterase activities
Biosci. Biotechnol. Biochem.
68
1977-1979
2004
Mus musculus
Manually annotated by BRENDA team
Cometa, M.F.; Lorenzini, P.; Fortuna, S.; Volpe, M.T.; Meneguz, A.; Palmery, M.
In vitro inhibitory effect of aflatoxin B1 on acetylcholinesterase activity in mouse brain
Toxicology
206
125-135
2005
Mus musculus
Manually annotated by BRENDA team
Hoernberg, A.; Tunemalm, A.K.; Ekstroem, F.
Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state
Biochemistry
46
4815-4825
2007
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Bourne, Y.; Radic, Z.; Sulzenbacher, G.; Kim, E.; Taylor, P.; Marchot, P.
Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding
J. Biol. Chem.
281
29256-29267
2006
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Ko, S.O.; Kim, T.H.; Lee, H.K.; Lee, J.C.; Cho, E.S.
Temporospatial localization of acetylcholinesterase activity in the dental epithelium during mouse tooth development
Life Sci.
81
1235-1240
2007
Mus musculus
Manually annotated by BRENDA team
Taylor, P.; Kovarik, Z.; Reiner, E.; Radic, Z.
Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure
Toxicology
233
70-78
2007
Mus musculus
Manually annotated by BRENDA team
Bosak, A.; Gazic, I.; Vinkovic, V.; Kovarik, Z.
Amino acid residues involved in stereoselective inhibition of cholinesterases with bambuterol
Arch. Biochem. Biophys.
471
72-76
2008
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Agrawal, R.; Tyagi, E.; Shukla, R.; Nath, C.
Effect of insulin and melatonin on acetylcholinesterase activity in the brain of amnesic mice
Behav. Brain Res.
189
381-386
2008
Mus musculus
Manually annotated by BRENDA team
Papandreou, M.A.; Dimakopoulou, A.; Linardaki, Z.I.; Cordopatis, P.; Klimis-Zacas, D.; Margarity, M.; Lamari, F.N.
Effect of a polyphenol-rich wild blueberry extract on cognitive performance of mice, brain antioxidant markers and acetylcholinesterase activity
Behav. Brain Res.
198
352-358
2009
Mus musculus
Manually annotated by BRENDA team
Pavlov, V.A.; Parrish, W.R.; Rosas-Ballina, M.; Ochani, M.; Puerta, M.; Ochani, K.; Chavan, S.; Al-Abed, Y.; Tracey, K.J.
Brain acetylcholinesterase activity controls systemic cytokine levels through the cholinergic anti-inflammatory pathway
Brain Behav. Immun.
23
41-45
2009
Mus musculus
Manually annotated by BRENDA team
Vignaud, A.; Fougerousse, F.; Mouisel, E.; Guerchet, N.; Hourde, C.; Bacou, F.; Butler-Browne, G.S.; Chatonnet, A.; Ferry, A.
Genetic inactivation of acetylcholinesterase causes functional and structural impairment of mouse soleus muscles
Cell Tissue Res.
333
289-296
2008
Mus musculus
Manually annotated by BRENDA team
Cheng, Y.H.; Cheng, X.L.; Radi?, Z.; McCammon, J.A.
Acetylcholinesterase: mechanisms of covalent inhibition of H447I mutant determined by computational analyses
Chem. Biol. Interact.
175
196-199
2008
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Jazi, R.; Lalonde, R.; Qian, S.; Strazielle, C.
Regional brain evaluation of acetylcholinesterase activity in PS1/A246E transgenic mice
Neurosci. Res.
63
106-114
2009
Mus musculus
Manually annotated by BRENDA team
Hoernberg, A.; Artursson, E.; Waerme, R.; Pang, Y.P.; Ekstroem, F.
Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: reactivation involving flipping of the His447 ring to form a reactive Glu334-His447-oxime triad
Biochem. Pharmacol.
79
507-515
2010
Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Guo, L.; Suarez, A.I.; Braden, M.R.; Gerdes, J.M.; Thompson, C.M.
Inhibition of acetylcholinesterase by chromophore-linked fluorophosphonates
Bioorg. Med. Chem. Lett.
20
1194-1197
2010
Electrophorus electricus, Mus musculus
Manually annotated by BRENDA team
Bhattacharjee, A.K.; Kuca, K.; Musilek, K.; Gordon, R.K.
In silico pharmacophore model for tabun-inhibited acetylcholinesterase reactivators: a study of their stereoelectronic properties
Chem. Res. Toxicol.
23
26-36
2010
Mus musculus
Manually annotated by BRENDA team
Kakinuma, Y.; Furihata, M.; Akiyama, T.; Arikawa, M.; Handa, T.; Katare, R.G.; Sato, T.
Donepezil, an acetylcholinesterase inhibitor against Alzheimers dementia, promotes angiogenesis in an ischemic hindlimb model
J. Mol. Cell. Cardiol.
48
680-693
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Lee, Y.K.; Yuk, D.Y.; Kim, T.I.; Kim, Y.H.; Kim, K.T.; Kim, K.H.; Lee, B.J.; Nam, S.Y.; Hong, J.T.
Protective effect of the ethanol extract of Magnolia officinalis and 4-O-methylhonokiol on scopolamine-induced memory impairment and the inhibition of acetylcholinesterase activity
J. Nat. Med.
63
274-282
2009
Mus musculus
Manually annotated by BRENDA team
Artursson, E.; Andersson, P.O.; Akfur, C.; Linusson, A.; Boerjegren, S.; Ekstroem, F.
Catalytic-site conformational equilibrium in nerve-agent adducts of acetylcholinesterase: possible implications for the HI-6 antidote substrate specificity
Biochem. Pharmacol.
85
1389-1397
2013
Homo sapiens, Mus musculus, Mus musculus (P21836)
Manually annotated by BRENDA team
Hicks, D.A.; Makova, N.Z.; Nalivaeva, N.N.; Turner, A.J.
Characterisation of acetylcholinesterase release from neuronal cells
Chem. Biol. Interact.
203
302-308
2013
Mus musculus
Manually annotated by BRENDA team
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