Acetylcholinesterase - wikipedia Acetylcholinesterase A gene or the protein it encodes in various Animalia including humans `` ACHE '' redirects here. For other uses, see Ache. acetylcholinesterase Acetylcholinesterase catalyzes the hydrolysis of acetylcholine to acetate ion and choline Identifiers EC number 3.1. 1.7 CAS number 9000 - 81 - 1 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO show Search PMC articles PubMed articles NCBI proteins ACHE Available structures PDB Ortholog search : PDBe RCSB show List of PDB id codes 4EY7, 4PQE, 1F8U, 3LII, 4BDT, 4M0E, 4M0F, 1VZJ, 2X8B, 1B41, 4EY4, 4EY5, 4EY6, 4EY8, 5FOQ, 5HF9, 5HF6, 5FPQ, 5HF8, 5HFA Identifiers Aliases ACHE, AChE, acetylhydrolase, acetylcholinesterase ( Yt blood group ), ACEE, ARN - YT, acetylcholinesterase ( Cartwright blood group ), true cholinesterase ( dated synonym ) External IDs MGI : 87876 HomoloGene : 543 GeneCards : ACHE hide Gene location ( Human ) Chr. Chromosome 7 ( human ) Band 7q22. 1 Start 100,889,994 bp End 100,896,974 bp show Gene location ( Mouse ) Chr. Chromosome 5 ( mouse ) Band 5 G2 5 76.32 cM Start 137,287,519 bp End 137,294,466 bp hide RNA expression pattern More reference expression data show Gene ontology Molecular function protein homodimerization activity collagen binding acetylcholine binding serine hydrolase activity carboxylic ester hydrolase activity amyloid - beta binding cholinesterase activity protein self - association protein binding laminin binding hydrolase activity ACHE Cellular component Golgi apparatus membrane plasma membrane synapse basal lamina extracellular region cell surface cell junction perinuclear region of cytoplasm anchored component of membrane cell nucleus synaptic cleft extracellular space neuromuscular junction Biological process muscle organ development receptor internalization neurotransmitter biosynthetic process negative regulation of synaptic transmission, cholinergic amyloid precursor protein metabolic process protein tetramerization acetylcholine catabolic process nervous system development neurotransmitter catabolic process DNA replication cell adhesion retina development in camera - type eye response to wounding positive regulation of protein secretion osteoblast development synapse assembly phosphatidylcholine biosynthetic process regulation of receptor recycling cell proliferation acetylcholine catabolic process in synaptic cleft neurotransmitter receptor biosynthetic process Sources : Amigo / QuickGO Orthologs Species Human Mouse Entrez 43 11423 Ensembl ENSG00000087085 ENSMUSG00000023328 UniProt P22303 P21836 RefSeq ( mRNA ) NM_000665 NM_001282449 NM_001302621 NM_001302622 NM_015831 NM_001290010 NM_009599 RefSeq ( protein ) NP_000656 NP_001269378 NP_001289550 NP_001289551 NP_001276939 NP_033729 Location ( UCSC ) Chr 7 : 100.89 -- 100.9 Mb Chr 5 : 137.29 -- 137.29 Mb PubMed search Wikidata View / Edit Human View / Edit Mouse Acetylcholinesterase ( HGNC symbol ACHE ; EC 3.1. 1.7 ), also known as AChE or acetylhydrolase, is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and of some other choline esters that function as neurotransmitters. AChE is found at mainly neuromuscular junctions and in chemical synapses of the cholinergic type, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. Contents 1 Enzyme structure and mechanism 2 Biological function 3 Disease relevance 4 Distribution 5 AChE gene 5.1 AChE 5.2 AChE 5.3 AChE 6 Nomenclature 7 Inhibitors 8 See also 9 References 10 Further reading 11 External links Enzyme structure and mechanism AChe mechanism of action AChE is a hydrolase that hydrolyzes choline esters. It has a very high catalytic activity -- each molecule of AChE degrades about 25000 molecules of acetylcholine ( ACh ) per second, approaching the limit allowed by diffusion of the substrate. The active site of AChE comprises 2 subsites -- the anionic site and the esteratic subsite. The structure and mechanism of action of AChE have been elucidated from the crystal structure of the enzyme. The anionic subsite accommodates the positive quaternary amine of acetylcholine as well as other cationic substrates and inhibitors. The cationic substrates are not bound by a negatively charged amino acid in the anionic site, but by interaction of 14 aromatic residues that line the gorge leading to the active site. All 14 amino acids in the aromatic gorge are highly conserved across different species. Among the aromatic amino acids, tryptophan 84 is critical and its substitution with alanine results in a 3000-fold decrease in reactivity. The gorge penetrates halfway through the enzyme and is approximately 20 angstroms long. The active site is located 4 angstroms from the bottom of the molecule. The esteratic subsite, where acetylcholine is hydrolyzed to acetate and choline, contains the catalytic triad of three amino acids : serine 200, histidine 440 and glutamate 327. These three amino acids are similar to the triad in other serine proteases except that the glutamate is the third member rather than aspartate. Moreover, the triad is of opposite chirality to that of other proteases. The hydrolysis reaction of the carboxyl ester leads to the formation of an acyl - enzyme and free choline. Then, the acyl - enzyme undergoes nucleophilic attack by a water molecule, assisted by the histidine 440 group, liberating acetic acid and regenerating the free enzyme. Biological function During neurotransmission, ACh is released from the presynaptic neuron into the synaptic cleft and binds to ACh receptors on the post-synaptic membrane, relaying the signal from the nerve. AChE, also located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACh. The liberated choline is taken up again by the pre-synaptic neuron and ACh is synthesized by combining with acetyl - CoA through the action of choline acetyltransferase. A cholinomimetic drug disrupts this process by acting as a cholinergic neurotransmitter that is impervious to acetylcholinesterase 's lysing action. Disease relevance Main article : Acetylcholinesterase inhibitor For a cholinergic neuron to receive another impulse, ACh must be released from the ACh receptor. This occurs only when the concentration of ACh in the synaptic cleft is very low. Inhibition of AChE leads to accumulation of ACh in the synaptic cleft and results in impeded neurotransmission. Mechanism of Inhibitors of AChE Irreversible inhibitors of AChE may lead to muscular paralysis, convulsions, bronchial constriction, and death by asphyxiation. Organophosphates ( OP ), esters of phosphoric acid, are a class of irreversible AChE inhibitors. Cleavage of OP by AChE leaves a phosphoryl group in the esteratic site, which is slow to be hydrolyzed ( on the order of days ) and can become covalently bound. Irreversible AChE inhibitors have been used in insecticides ( e.g., malathion ) and nerve gases for chemical warfare ( e.g., Sarin and Soman ). Carbamates, esters of N - methyl carbamic acid, are AChE inhibitors that hydrolyze in hours and have been used for medical purposes ( e.g., physostigmine for the treatment of glaucoma ). Reversible inhibitors occupy the esteratic site for short periods of time ( seconds to minutes ) and are used to treat of a range of central nervous system diseases. Tetrahydroaminoacridine ( THA ) and donepezil are FDA - approved to improve cognitive function in Alzheimer 's disease. Rivastigmine is also used to treat Alzheimer 's and Lewy body dementia, and pyridostigmine bromide is used to treat myasthenia gravis. An endogenous inhibitor of AChE in neurons is Mir - 132 microRNA, which may limit inflammation in the brain by silencing the expression of this protein and allowing ACh to act in an anti-inflammatory capacity. It has also been shown that the main active ingredient in cannabis, tetrahydrocannabinol, is a competitive inhibitor of acetylcholinesterase. Distribution AChE is found in many types of conducting tissue : nerve and muscle, central and peripheral tissues, motor and sensory fibers, and cholinergic and noncholinergic fibers. The activity of AChE is higher in motor neurons than in sensory neurons. Acetylcholinesterase is also found on the red blood cell membranes, where different forms constitute the Yt blood group antigens. Acetylcholinesterase exists in multiple molecular forms, which possess similar catalytic properties, but differ in their oligomeric assembly and mode of attachment to the cell surface. AChE gene In mammals, acetylcholinesterase is encoded by a single AChE gene while some invertebrates have multiple acetylcholinesterase genes. Note higher vertebrates also encode a closely related paralog BCHE ( butyrylcholinesterase ) with 50 % amino acid identity to ACHE. Diversity in the transcribed products from the sole mammalian gene arises from alternative mRNA splicing and post-translational associations of catalytic and structural subunits. There are three known forms : T ( tail ), R ( read through ), and H ( hydrophobic ). AChE The major form of acetylcholinesterase found in brain, muscle, and other tissues, known as is the hydrophilic species, which forms disulfide - linked oligomers with collagenous, or lipid - containing structural subunits. In the neuromuscular junctions AChE expresses in asymmetric form which associates with ColQ or subunit. In the central nervous system it is associated with PRiMA which stands for Proline Rich Membrane anchor to form symmetric form. In either case, the ColQ or PRiMA anchor serves to maintain the enzyme in the intercellular junction, ColQ for the neuromuscular junction and PRiMA for synapses. AChE The other, alternatively spliced form expressed primarily in the erythroid tissues, differs at the C - terminus, and contains a cleavable hydrophobic peptide with a PI - anchor site. It associates with membranes through the phosphoinositide ( PI ) moieties added post-translationally. AChE The third type has, so far, only been found in Torpedo sp. and mice although it is hypothesized in other species. It is thought to be involved in the stress response and, possibly, inflammation. Nomenclature The nomenclatural variations of ACHE and of cholinesterases generally are discussed at Cholinesterase § Types and nomenclature. Inhibitors For acetylcholine esterase ( AChE ), reversible inhibitors are those that do not irreversibly bond to and deactivate AChE. 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Bibcode : 1991Sci... 253... 872S. doi : 10.1126 / science. 1678899. PMID 1678899. Soreq H, Seidman S ( 2001 ). `` Acetylcholinesterase -- new roles for an old actor ''. Nature Reviews Neuroscience. 2 ( 4 ) : 294 -- 302. doi : 10.1038 / 35067589. PMID 11283752. Shen T, Tai K, Henchman RH, McCammon JA ( 2003 ). `` Molecular dynamics of acetylcholinesterase ''. Acc. Chem. Res. 35 ( 6 ) : 332 -- 40. doi : 10.1021 / ar010025i. PMID 12069617. Pakaski M, Kasa P ( 2003 ). `` Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein ''. Current drug targets. CNS and neurological disorders. 2 ( 3 ) : 163 -- 71. doi : 10.2174 / 1568007033482869. PMID 12769797. Meshorer E, Soreq H ( 2006 ). `` Virtues and woes of AChE alternative splicing in stress - related neuropathologies ''. Trends Neurosci. 29 ( 4 ) : 216 -- 24. doi : 10.1016 / j. tins. 2006.02. 005. PMID 16516310. Ehrlich G, Viegas - Pequignot E, Ginzberg D, Sindel L, Soreq H, Zakut H ( 1992 ). `` Mapping the human acetylcholinesterase gene to chromosome 7q22 by fluorescent in situ hybridization coupled with selective PCR amplification from a somatic hybrid cell panel and chromosome - sorted DNA libraries ''. Genomics. 13 ( 4 ) : 1192 -- 7. doi : 10.1016 / 0888 - 7543 ( 92 ) 90037 - S. PMID 1380483. Spring FA, Gardner B, Anstee DJ ( 1992 ). `` Evidence that the antigens of the Yt blood group system are located on human erythrocyte acetylcholinesterase ''. Blood. 80 ( 8 ) : 2136 -- 41. PMID 1391965. Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D ( 1992 ). `` Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding ''. J. Biol. Chem. 267 ( 25 ) : 17640 -- 8. PMID 1517212. Getman DK, Eubanks JH, Camp S, Evans GA, Taylor P ( 1992 ). `` The human gene encoding acetylcholinesterase is located on the long arm of chromosome 7 ''. Am. J. Hum. Genet. 51 ( 1 ) : 170 -- 7. PMC 1682883. PMID 1609795. Li Y, Camp S, Rachinsky TL, Getman D, Taylor P ( 1992 ). `` Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue - specific expression ''. J. Biol. Chem. 266 ( 34 ) : 23083 -- 90. PMID 1744105. Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A ( 1992 ). `` The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys - 580 -- -- Ala mutant ''. J. Biol. Chem. 266 ( 35 ) : 23977 -- 84. PMID 1748670. Soreq H, Ben - Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman - Hurwitz J, Lev - Lehman E, Ginzberg D, Lipidot - Lifson Y ( 1991 ). `` Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C - rich attenuating structure ''. Proceedings of the National Academy of Sciences of the United States of America. 87 ( 24 ) : 9688 -- 92. Bibcode : 1990PNAS... 87.9688 S. doi : 10.1073 / pnas. 87.24. 9688. PMC 55238. PMID 2263619. Chhajlani V, Derr D, Earles B, Schmell E, August T ( 1989 ). `` Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase ''. FEBS Lett. 247 ( 2 ) : 279 -- 82. doi : 10.1016 / 0014 - 5793 ( 89 ) 81352 - 3. PMID 2714437. Lapidot - Lifson Y, Prody CA, Ginzberg D, Meytes D, Zakut H, Soreq H ( 1989 ). `` Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells : correlation with various leukemias and abnormal megakaryocytopoiesis ''. Proceedings of the National Academy of Sciences of the United States of America. 86 ( 12 ) : 4715 -- 9. Bibcode : 1989PNAS... 86.4715 L. doi : 10.1073 / pnas. 86.12. 4715. PMC 287342. PMID 2734315. Bazelyansky M, Robey E, Kirsch JF ( 1986 ). `` Fractional diffusion - limited component of reactions catalyzed by acetylcholinesterase ''. Biochemistry. 25 ( 1 ) : 125 -- 30. doi : 10.1021 / bi00349a019. PMID 3954986. Gaston SM, Marchase RB, Jakoi ER ( 1982 ). `` Brain ligatin : a membrane lectin that binds acetylcholinesterase ''. J. Cell. Biochem. 18 ( 4 ) : 447 -- 59. doi : 10.1002 / jcb. 1982.240180406. PMID 7085778. Ordentlich A, Barak D, Kronman C, Ariel N, Segall Y, Velan B, Shafferman A ( 1995 ). `` Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase ''. J. Biol. Chem. 270 ( 5 ) : 2082 -- 91. doi : 10.1074 / jbc. 270.5. 2082. PMID 7836436. Maruyama K, Sugano S ( 1994 ). `` Oligo - capping : a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides ''. Gene. 138 ( 1 -- 2 ) : 171 -- 4. doi : 10.1016 / 0378 - 1119 ( 94 ) 90802 - 8. PMID 8125298. Ben Aziz - Aloya R, Sternfeld M, Soreq H ( 1994 ). `` Promoter elements and alternative splicing in the human ACHE gene ''. Prog. Brain Res. 98 : 147 -- 53. doi : 10.1016 / s0079 - 6123 ( 08 ) 62392 - 4. PMID 8248502. Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM ( 1993 ). `` Molecular and Cellular Biology of Cholinesterases ''. Prog. Brain Res. 41 ( 1 ) : 31 -- 91. doi : 10.1016 / 0301 - 0082 ( 93 ) 90040 - Y. PMID 8321908. External links ATSDR Case Studies in Environmental Medicine : Cholinesterase Inhibitors, Including Insecticides and Chemical Warfare Nerve Agents U.S. Department of Health and Human Services Proteopedia Acetylcholinesterase Proteopedia AChE_inhibitors_and_substrates Proteopedia AChE_inhibitors_and_substrates_ ( Part_II ) Proteopedia AChE bivalent inhibitors AChE_bivalent_inhibitors AChE bivalent inhibitors Acetylcholinesterase : A gorge - ous enzyme -- PDBe Acetylcholinesterase -- RCSB PDB Human ACHE genome location and ACHE gene details page in the UCSC Genome Browser. PDB gallery 1b41 : HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN - II, GLYCOSYLATED PROTEIN 1f8u : CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM PEPTIDE FASCICULIN - II 1vzj : STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE : FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT - HANDED POLYPROLINE HELIX Enzymes involved in neurotransmission monoamine histidine → histamine anabolism : Histidine decarboxylase catabolism : Histamine N - methyltransferase Diamine oxidase tyrosine → dopamine → epinephrine anabolism : Tyrosine hydroxylase Aromatic L - amino acid decarboxylase Dopamine beta - hydroxylase Phenylethanolamine N - methyltransferase catabolism : Catechol - O - methyl transferase Monoamine oxidase glutamate → GABA anabolism : Glutamate decarboxylase catabolism : 4 - aminobutyrate transaminase tryptophan → serotonin → melatonin Tryptophan hydroxylase Aromatic L - amino acid decarboxylase Aralkylamine N - acetyltransferase Acetylserotonin O - methyltransferase arginine → NO Nitric oxide synthase ( NOS1, NOS2, NOS3 ) choline → Acetylcholine anabolism : Choline acetyltransferase catabolism : Cholinesterase ( Acetylcholinesterase, Butyrylcholinesterase ) Hydrolase : esterases ( EC 3.1 ) 3.1. 1 : Carboxylic ester hydrolases Cholinesterase Acetylcholinesterase Butyrylcholinesterase Pectinesterase 6 - phosphogluconolactonase PAF acetylhydrolase Lipase Bile salt - dependent Gastric / Lingual Pancreatic Lysosomal Hormone - sensitive Endothelial Hepatic Lipoprotein Monoacylglycerol Diacylglycerol Phospholipase A1 A2 Cutinase PETase 3.1. 2 : Thioesterase Palmitoyl protein thioesterase Ubiquitin carboxy - terminal hydrolase L1 4 - hydroxybenzoyl - CoA thioesterase 3.1. 3 : Phosphatase Alkaline phosphatase ALPI ALPL ALPP Acid phosphatase ( Prostatic ) / Tartrate - resistant acid phosphatase / Purple acid phosphatases Nucleotidase Glucose 6 - phosphatase Fructose 1, 6 - bisphosphatase Calcineurin Protein phosphatase PP2A OCRL Pyruvate dehydrogenase phosphatase Fructose 6 - P, 2 - kinase : fructose 2, 6 - bisphosphatase PTEN Phytase Beta - propeller phytase Inositol - phosphate phosphatase IMPA1, IMPA2, IMPA3 Protein phosphatase : Protein tyrosine phosphatase Protein serine / threonine phosphatase Dual - specificity phosphatase 3.1. 4 : Phosphodiesterase Autotaxin Phospholipase Sphingomyelin phosphodiesterase PDE1 PDE2 PDE3 PDE4A / PDE4B PDE5 Lecithinase ( Clostridium perfringens alpha toxin ) Cyclic nucleotide phosphodiesterase 3.1. 6 : Sulfatase arylsulfatase Arylsulfatase A Arylsulfatase B Arylsulfatase E Steroid sulfatase Galactosamine - 6 sulfatase Iduronate - 2 - sulfatase N - acetylglucosamine - 6 - sulfatase Nuclease ( includes deoxyribonuclease and ribonuclease ) 3.1. 11 - 16 : Exonuclease Exodeoxyribonuclease RecBCD Exoribonuclease Oligonucleotidase 3.1. 21 - 31 : Endonuclease Endodeoxyribonuclease Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease Endoribonuclease RNase III RNase H 2A 2B 2C RNase P RNase A 4 / 5 RNase T1 RNA - induced silencing complex either deoxy - or ribo - Aspergillus nuclease S1 Micrococcal nuclease Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics Types EC1 Oxidoreductases ( list ) EC2 Transferases ( list ) EC3 Hydrolases ( list ) EC4 Lyases ( list ) EC5 Isomerases ( list ) EC6 Ligases ( list ) Acetylcholine metabolism and transport modulators Enzyme ( modulators ) ChAT Inhibitors : 1 - ( - Benzoylethyl ) pyridinium 2 - ( α - Naphthoyl ) ethyltrimethylammonium 3 - Chloro - 4 - stillbazole 4 - ( 1 - Naphthylvinyl ) pyridine Acetylseco hemicholinium - 3 Acryloylcholine AF64A B115 BETA CM - 54,903 N, N - Dimethylaminoethylacrylate N, N - Dimethylaminoethylchloroacetate AChE Inhibitors : Reversible : Carbamates : Aldicarb Aminocarb Bendiocarb Bufencarb Carbaryl Carbendazim Carbetamide Carbofuran Carbosulfan Chlorbufam Chloropropham Dimetilan Ethienocarb Ethiofencarb Fenobucarb Formetanate Formparanate Methiocarb Methomyl Metolcarb Miotine Oxamyl Phenmedipham Pinmicarb Pirimicarb Propamocarb Propham Propoxur Thiofanox ; Stigmines : Distigmine Eptastigmine Ganstigmine Neostigmine Phenserine Physostigmine Pyridostigmine Quilostigmine Rivastigmine Terestigmine ; Others : Acotiamide Ambenonium Caffeine Donepezil EA - 3990 EA - 4056 Edrophonium Galantamine Huperzine A Ipidacrine Itopride Ladostigil Minaprine Octamethylene - bis ( 5 - dimethylcarbamoxyisoquinolinium bromide ) T - 1123 Tacrine Zanapezil Irreversible : Organophosphates : Acephate Anatoxin - a ( S ) Azinphos - ethyl Azinphos - methyl BAY - 29952 Bensulide Cadusafos Carbophenothion Chlorethoxyfos Chlorfenvinphos Chlorpyrifos Chlorpyrifos - methyl Coumaphos Cyanophos Cyclosarin Demephion Demeton Demeton - S - methyl Dialifor Diazinon Dichlorvos Dicrotophos Diisopropyl fluorophosphate Diisopropylphosphate Dimefox Dimethoate Dimethyl 4 - ( methylthio ) phenyl phosphate Dioxathion Disulfoton EA - 2192 EA - 3148 Echothiophate Endothion Ethion Ethoprop Fenamiphos Fenitrothion Fenthion Fluorotabun Fonofos Formothion Fosthiazate GV Hexaethyl tetraphosphate Isofluorophate Isoxathion Leptophos Malaoxon Malathion Methamidophos Methidathion Methyl phenkapton Metrifonate Mevinphos Monocrotophos Naled Novichok agent Omethoate Oxydemeton - methyl Paraoxon Parathion Parathion - methyl Phorate Phosalone Phosfolan Phosmet Phosphamidon Phoxim Pirimiphos - methyl Profenofos Prothoate Sarin Soman Tabun Tebupirimfos Temefos Terbufos Tetrachlorvinphos Tetraethyl pyrophosphate Triazofos Tribufos Trichlorfon Trichloronate Tricresyl phosphate VE VG VM VP VS VR VX ; Others : Demecarium Fasciculins ( green mamba toxins ) ( 1, 2, 3, 4 ) Onchidal ( Onchidella binneyi ) Methanesulfonyl fluoride Unsorted : α - Pinene α - Viniferin Affinine Affinisine Arisugacin A Bulbocapnine Conodurine Coronaridine Corydaline Corynoline Crimidine Cyclanoline Cymserine Harmaline Kobophenol A Lactucopicrin Lycorine Phosacetim Rosmarinic acid Stercuronium iodide Taspine Tetrahydrocannabinol Ungeremine Ungiminorine Dimethylcarbamoyl fluoride Reactivators : Asoxime chloride Methoxime Obidoxime Pralidoxime Trimedoxime bromide BChE Inhibitors : Affinine Affinisine Conodurine Cymserine Ladostigil Profenamine ( ethopropazine ) Rivastigmine Tacrine ZINC - 12613047 Many of the other AChE inhibitors listed above Transporter ( modulators ) CHT Inhibitors : Hemicholinium - 3 ( hemicholine ) Triethylcholine Enhancers : Coluracetam VAChT Inhibitors : Vesamicol Release ( modulators ) Inhibitors SNAP - 25 inactivators : Botulinum toxin ( A, C, E ) VAMP inactivators : Botulinum toxin ( B, D, F, G ) Others : Bungarotoxins ( β - bungarotoxin, γ - bungarotoxin ) Enhancers LPHN agonists : α - Latrotoxin Others : Atracotoxin ( e.g., robustoxin, versutoxin ) Crotoxin See also : Receptor / signaling modulators Muscarinic acetylcholine receptor modulators Nicotinic acetylcholine receptor modulators GND : 4129688 - 6 LCCN : sh92004641 Retrieved from `` https://en.wikipedia.org/w/index.php?title=Acetylcholinesterase&oldid=860512472 '' Categories : Genes on human chromosome 7 Acetylcholine EC 3.1. 1 Hidden categories : Articles with short description Wikipedia articles with GND identifiers Wikipedia articles with LCCN identifiers Talk Search Contents About Wikipedia Български Bosanski Català Čeština Cymraeg Dansk Deutsch Español Euskara فارسی Français 한국어 Italiano עברית Magyar Nederlands Norsk Polski Русский Simple English Slovenščina Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska Türkçe Українська Tiếng Việt 粵語 中文 22 more Edit links This page was last edited on 21 September 2018, at 04 : 43 ( UTC ). 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Question: what is the role of acetylcholinesterase in the neuromuscular junction
Answer: to terminate synaptic transmission