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Information on EC 3.1.1.7 - acetylcholinesterase and Organism(s) Drosophila melanogaster and UniProt Accession P07140
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3.1.1.7 acetylcholinesteraseIUBMB Comments
Acts on a variety of acetic esters; also catalyses transacetylations.
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Word Map
- 3.1.1.7
-
cholinergic
- alzheimer
- nerve
- butyrylcholinesterase
-
organophosphate
-
pesticide
- hippocampus
-
neurotoxicity
- dementia
- erythrocyte
- deficit
-
organophosphorus
-
insecticide
-
muscarinic
- donepezil
- synaptic
-
neuroprotective
- cerebral
- acetyltransferase
- fiber
-
maze
- cortical
-
innervation
-
poison
- cholinesterases
-
nicotinic
-
neurotransmitter
- neuromuscular
- neurodegenerative
- atropine
- axon
- oxime
- carbamate
-
chat
-
histochemistry
-
amyloid
-
morris
-
neurochemical
-
monoamine
- synapses
-
intoxication
- chlorpyrifos
- striatum
-
neurotransmission
-
postsynaptic
- forebrain
- carboxylesterase
-
antidote
-
parasympathetic
- biotechnology
- synthesis
- analysis
- pharmacology
- medicine
- diagnostics
-
anticholinergic
- environmental protection
- drug development
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ache, acetylcholinesterase, acetylcholine esterase, acetyl cholinesterase, hache, eeache, ache1, huache, tcache, membrane-bound acetylcholinesterase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AcCholE
-
-
-
-
acetyl beta-methylcholinesterase
-
-
-
-
acetylcholine esterase
-
-
-
-
acetylcholine hydrolase
-
-
-
-
acetylthiocholinesterase
-
-
-
-
AChE
choline esterase I
-
-
-
-
cholinesterase
-
-
-
-
esterase, acetyl choline
-
-
-
-
true cholinesterase
-
-
-
-
AChE
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetylcholine + H2O = choline + acetate
mathematical modelling of mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9000-81-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetylthiocholine iodide + H2O
acetate + thiocholine iodide
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
S-acetylthiocholine + H2O
acetate + thiocholine
-
detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB
-
-
?
additional information
?
-
active site structure and substrate channels of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
active site structure and substrate channels of wild-type and mutant enzymes, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-ketoamyl trimethyl ammonium iodide
-
nonhydrolysable substrate analogue, mechanism of substrate inhibition
rivastigmine
-
trade name: Exelon, carbamylates the enzyme, enzyme reactivates spontaneous at a slow rate
Urea
-
the stability of the immobilized recombinant enzyme is 2.7fold increased compared to the soluble recombinant enzyme
additional information
the interaction between AChE and silver nanoparticles (AgNPs) leads not only to a decrease in AChE activity, but also to a reduction in the crystallinity and stability of AgNPs. The circular dichroism demonstrates that the secondary structure of AChE also declines after 30 min of incubation with AgNPs at 37°C. Smaller AgNPs result in size increments after interaction with enzymes, while the larger ones show size decrements
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
substrate binding kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
substrate binding kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACES_DROME
649
0
71785
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
contains glycolipid anchor, components glucosamine and ethanolamine
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W83A
mutational enlarging of a channel located at the bottom of the active site gorge in the Drosophila enzyme. Mutation of Trp83 to Ala or Glu widens the channel from 5 A to 9 A. The kinetics of substrate hydrolysis and the effect of ligands that close the main entrance, overview. In mutant W83A ligands that close the main entrance do not inhibit substrate hydrolysis because the traffic can pass via an alternative route
W83E
mutational enlarging of a channel located at the bottom of the active site gorge in the Drosophila enzyme. Mutation of Trp83 to Ala or Glu widens the channel from 5 A to 9 A. The kinetics of substrate hydrolysis and the effect of ligands that close the main entrance, overview. In mutant W83E ligands that close the main entrance do not inhibit substrate hydrolysis because the traffic can pass via an alternative route
D375A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
D375G
E237A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E237G
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E237Q
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69I
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69K
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69L
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69W
E69Y
F330A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330C
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330G
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330H
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330I
F330L
F330S
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330V
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330W
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330Y
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F371A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F371G
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F371Y
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F77S
-
more than 5% of wild-type activity, kinetics of substrate inhibition
G265A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
G368A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
I161K
-
more than 5% of wild-type activity, kinetics of substrate inhibition
I161T
-
more than 5% of wild-type activity, kinetics of substrate inhibition
L328A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
L328F
M153A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
R70V
V182L
-
more than 5% of wild-type activity, kinetics of substrate inhibition
V318A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
V318D
W271G
-
more than 5% of wild-type activity, kinetics of substrate inhibition
W321A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
W321L
W83A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
W83E
-
more than 5% of wild-type activity, shift of inhibition towards higher substrate concentration
W83Y
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y162A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y324A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y370A
Y370C
-
more than 5% of wild-type activity, shift of inhibition towards higher substrate concentration
Y370F
Y370L
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y370P
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y370S
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y374A
Y71A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y71D
Y71K
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y73A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y73Q
additional information
D375G
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69W
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
E69W
-
more than 5% of wild-type activity, kinetics of substrate inhibition
E69Y
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
E69Y
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330I
-
more than 5% of wild-type activity, kinetics of substrate inhibition
F330L
-
more than 5% of wild-type activity, kinetics of substrate inhibition
L328F
-
more than 5% of wild-type activity, kinetics of substrate inhibition
R70V
-
more than 5% of wild-type activity, kinetics of substrate inhibition
V318D
-
more than 5% of wild-type activity, kinetics of substrate inhibition
W321L
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
W321L
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y370A
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
Y370A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y370F
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
Y370F
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y374A
-
more than 5% of wild-type activity, kinetics of substrate inhibition
Y71D
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
Y71D
-
more than 5% of wild-type activity, shift of inhibition towards higher substrate concentration
Y73Q
-
increased sensitivity for carbaryl, malaoxon, omethoate and paraoxon
Y73Q
-
more than 5% of wild-type activity, kinetics of substrate inhibition
additional information
-
soluble truncated enzyme mutants, mathematical modelling of reaction mechanism
additional information
-
immobilization of AChE on preactivated perlite, a porous silica matrix, by silanization and glutaraldehyde treatment, the immobilization leads to 30% reduced specific activity and improved enzyme stability, e.g. against urea, acetonitrile and temperature, immobilized enzymes retain 80% of its initial activity after 16 consecutive reactor batch cycles, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
the stability of the immobilized recombinant enzyme is 8.7fold increased compared to the soluble recombinant enzyme
60
-
the stability of the immobilized recombinant enzyme is 17.7fold increased compared to the soluble recombinant enzyme
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitril
-
the stability of the immobilized recombinant enzyme is 1.7fold increased compared to the soluble recombinant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme by procainamide affinity chromatography and desalting gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in eukaryote cells using the baculovirus transfection system
AChE expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method
-
expression of C-terminally truncated enzyme in Spodoptera frugiperda IPLB-Sf21 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gnagey, A.L.; Forte, M.; Rosenberry, T.L.
Isolation and characterization of acetylcholinesterase from Drosophila
J. Biol. Chem.
262
13290-13298
1987
Drosophila melanogaster
Chaabihi, H.; Founier, D.; Fedon, Y.; Bossy, J.P.; Ravallec, M.; Devauchelle, G.; Cerutti, M.
Biochemical characterization of Drosophila melanogaster acetylcholinesterase expressed by recombinant baculoviruses
Biochem. Biophys. Res. Commun.
203
734-742
1994
Drosophila melanogaster
Pralavorio, M.; Fournier, D.
Drosophila acetylcholinesterase: Characterization of different mutants resistant to insecticides
Biochem. Genet.
30
77-83
1991
Drosophila melanogaster, Drosophila melanogaster MH19
Villatte, F.; Marcel, V.; Estrada-Mondaca, S.; Fournier, D.
Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides
Biosens. Bioelectron.
13
157-164
1998
Caenorhabditis elegans, Drosophila melanogaster, Electrophorus electricus, Torpedo sp.
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
Boublik, Y.; Saint-Aguet, P.; Lougarre, A.; Arnaud, M.; Villatte, F.; Estrada-Mondaca, S.; Fournier, D.
Acetylcholinesterase engineering for detection of insecticide residues
Protein Eng.
15
43-50
2002
Drosophila melanogaster
Stojan, J.; Golicnik, M.; Fournier, D.
Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism
Biochim. Biophys. Acta
1703
53-61
2004
Drosophila melanogaster
Stojan, J.; Brochier, L.; Alies, C.; Colletier, J.P.; Fournier, D.
Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
Eur. J. Biochem.
271
1364-1371
2004
Drosophila melanogaster
Barshan-Tashnizi, M.; Ahmadian, S.; Niknam, K.; Torabi, S.F.; Ranaei-Siadat, S.O.
Covalent immobilization of Drosophila acetylcholinesterase for biosensor applications
Biotechnol. Appl. Biochem.
52
257-264
2008
Drosophila melanogaster
Nachon, F.; Stojan, J.; Fournier, D.
Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel
FEBS J.
275
2659-2664
2008
Drosophila melanogaster (P07140), Drosophila melanogaster
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