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Acetylcholinesterase
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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
showSearch
PMC
articles
PubMed
articles
NCBI
proteins
ACHE
Available structures
PDB
Ortholog search: PDBe RCSB
showList 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
hideGene location (Human)
Chr.
Chromosome 7 (human)[1]
Band
7q22.1
Start
100,889,994 bp[1]
End
100,896,974 bp[1]
showGene location (Mouse)
Chr.
Chromosome 5 (mouse)[2]
Band
5 G2|5 76.32 cM
Start
137,287,519 bp[2]
End
137,294,466 bp[2]
hideRNA expression pattern

More reference expression data
showGene 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
[3] [4]
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 AChET
5.2 AChEH
5.3 AChER
6 Nomenclature
7 Inhibitors
8 See also
9 References
10 Further reading
11 External links
Enzyme structure and mechanism[edit]
AChe mechanism of action[5]
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.[6][7] 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.[8][9]
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.[10][11][12] All 14 amino acids in the aromatic gorge are highly conserved across different species.[13] Among the aromatic amino acids, tryptophan 84 is critical and its substitution with alanine results in a 3000-fold decrease in reactivity.[14] 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.[15]
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.[16] 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.[17][18]
Biological function[edit]
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.[19][20]
A cholinomimetic drug disrupts this process by acting as a cholinergic neurotransmitter that is impervious to acetylcholinesterase's lysing action.
Disease relevance[edit]
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.[21]
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.[22] 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.[23][24][25][26][27][28]
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.[29]
It has also been shown that the main active ingredient in cannabis, tetrahydrocannabinol, is a competitive inhibitor of acetylcholinesterase.[30]
Distribution[edit]
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.[31][32][33]
Acetylcholinesterase is also found on the red blood cell membranes, where different forms constitute the Yt blood group antigens.[34] 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[edit]
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 [35]. 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).[36]
AChET[edit]
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.
AChEH[edit]
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.[37]
AChER[edit]
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.[38]
Nomenclature[edit]
The nomenclatural variations of ACHE and of cholinesterases generally are discussed at Cholinesterase § Types and nomenclature.
Inhibitors[edit]
For acetylcholine esterase (AChE), reversible inhibitors are those that do not irreversibly bond to and deactivate AChE.[39] Drugs that reversibly inhibit acetylcholine esterase are being explored as treatments for Alzheimer's disease and myasthenia gravis, among others. Examples include tacrine and donepezil.[40]
See also[edit]
Molecular and Cellular Biology portal
Acetylcholinesterase inhibitor
Cholinesterases
References[edit]
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^ Jump up to: a b c GRCm38: Ensembl release 89: ENSMUSG00000023328 - Ensembl, May 2017
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Further reading[edit]
Silman I, Futerman AH (1988). "Modes of attachment of acetylcholinesterase to the surface membrane". Eur. J. Biochem. 170 (1–2): 11–22. doi:10.1111/j.1432-1033.1987.tb13662.x. PMID 3319614.
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I (1991). "Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein". Science. 253 (5022): 872–9. 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...87.9688S. 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...86.4715L. 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[edit]
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.
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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
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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
A
B
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)
show
v
t
e
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
B
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
C
D
Sphingomyelin phosphodiesterase
1
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
1
2A
2B
2C
RNase P
RNase A
1
2
3
4/5
RNase T1
RNA-induced silencing complex
either deoxy- or ribo-
Aspergillus nuclease S1
Micrococcal nuclease
show
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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)
show
v
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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
Authority control
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
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1991 World Championships in Athletics
From Wikipedia, the free encyclopedia
Jump to: navigation, search
3rd World Championships in Athletics
Host city
Tokyo, Japan
Nations participating
167
Athletes participating
1517
Dates
August 23 – September 1
Main venue
Olympic Stadium
< 1987 Rome
1993 Stuttgart >
The 3rd World Championships in Athletics, under the auspices of the International Association of Athletics Federations, were held in the Olympic Stadium in Tokyo, Japan between August 23 and September 1 and athletes from 167 countries participated in the event.[1]
The event is best-remembered for the men's long jump competition, when Carl Lewis made the best six-jump series in history, only to be beaten by Mike Powell, whose 8.95 metres (29.4 ft) jump broke Bob Beamon's long-standing world record from the 1968 Summer Olympics.
Contents
[hide]
1 Men's results
1.1 Track
1.2 Field
2 Women's results
2.1 Track
2.2 Field
3 Medal table by country
4 See also
5 References
Men's results[edit]
Track[edit]
1983 | 1987 | 1991 | 1993 | 1995
Games
Gold
Silver
Bronze
100 m
details Carl Lewis (USA) 9.86
(WR) Leroy Burrell (USA) 9.88
(PB) Dennis Mitchell (USA) 9.91
(PB)
200 m
details Michael Johnson (USA) 20.01 Frankie Fredericks (NAM) 20.34 Atlee Mahorn (CAN) 20.49
400 m
details Antonio Pettigrew (USA) 44.57 Roger Black (GBR) 44.62 Danny Everett (USA) 44.63
800 m
details Billy Konchellah (KEN) 1:43.99 José Luíz Barbosa (BRA) 1:44.24 Mark Everett (USA) 1:44.67
1500 m
details Noureddine Morceli (ALG) 3:32.84
(CR) Wilfred Kirochi (KEN) 3:34.84 Hauke Fuhlbrügge (GER) 3:35.28
5000 m
details Yobes Ondieki (KEN) 13:14.45
(CR) Fita Bayisa (ETH) 13:16.64 Brahim Boutayeb (MAR) 13:22.70
10,000 m
details Moses Tanui (KEN) 27:38.74 Richard Chelimo (KEN) 27:39.41 Khalid Skah (MAR) 27:41.74
Marathon
details Hiromi Taniguchi (JPN) 2:14:57 Hussein Ahmed Salah (DJI) 2:15:26 Steve Spence (USA) 2:15:36
110 m hurdles
details Greg Foster (USA) 13.06 Jack Pierce (USA) 13.06 Tony Jarrett (GBR) 13.25
400 m hurdles
details Samuel Matete (ZAM) 47.64 Winthrop Graham (JAM) 47.74
(NR) Kriss Akabusi (GBR) 47.86
(NR)
3000 m st.
details Moses Kiptanui (KEN) 8:12.59 Patrick Sang (KEN) 8:13.44 Azzedine Brahmi (ALG) 8:15.54
20 km walk
details Maurizio Damilano (ITA) 1:19:37
(CR) Mikhail Shchennikov (URS) 1:19:46 Yevgeniy Misyulya (URS) 1:20:22
50 km walk
details Aleksandr Potashov (URS) 3:53:09 Andrey Perlov (URS) 3:53:09 Hartwig Gauder (GER) 3:55:14
4 × 100 m relay
details United States (USA)
Andre Cason
Leroy Burrell
Dennis Mitchell
Carl Lewis
Michael Marsh* 37.50
(WR) France (FRA)
Max Morinière
Daniel Sangouma
Jean-Charles Trouabal
Bruno Marie-Rose 37.87 Great Britain (GBR)
Tony Jarrett
John Regis
Darren Braithwaite
Linford Christie 38.09
4 × 400 m relay
details Great Britain (GBR)
Roger Black
Derek Redmond
John Regis
Kriss Akabusi
Ade Mafe*
Mark Richardson* 2:57.53
(AR) United States (USA)
Andrew Valmon
Quincy Watts
Danny Everett
Antonio Pettigrew
Jeff Reynolds*
Mark Everett* 2:57.57 Jamaica (JAM)
Patrick O'Connor
Devon Morris
Winthrop Graham
Seymour Fagan
Howard Burnett* 3:00.10
WR world record | AR area record | CR championship record | GR games record | NR national record | OR Olympic record | PB personal best | SB season best | WL world leading (in a given season)
Note: * Indicates athletes who ran in preliminary rounds.
Field[edit]
1983 | 1987 | 1991 | 1993 | 1995
Games
Gold
Silver
Bronze
Long jump
details Mike Powell (USA) 8.95
(WR) Carl Lewis (USA) 8.91w Larry Myricks (USA) 8.42
Triple jump
details Kenny Harrison (USA) 17.78 Leonid Voloshin (URS) 17.75 Mike Conley (USA) 17.62
High jump
details Charles Austin (USA) 2.38
(CR) Javier Sotomayor (CUB) 2.36 Hollis Conway (USA) 2.36
Pole vault
details Sergey Bubka (URS) 5.95
(CR) István Bagyula (HUN) 5.90 Maksim Tarasov (URS) 5.85
Shot put
details Werner Günthör (SUI) 21.67 Lars Arvid Nilsen (NOR) 20.75 1 Aleksandr Klimenko (URS) 20.34
Discus throw
details Lars Riedel (GER) 66.20 Erik de Bruin (NED) 65.82 Attila Horváth (HUN) 65.32
Hammer throw
details Yuriy Sedykh (URS) 81.70 Igor Astapkovich (URS) 80.94 Heinz Weis (GER) 80.44
Javelin throw
details Kimmo Kinnunen (FIN) 90.82 Seppo Räty (FIN) 88.12 Vladimir Sasimovich (URS) 87.08
Decathlon
details Dan O'Brien (USA) 8812
(CR) Mike Smith (CAN) 8549 Christian Schenk (GER) 8394
WR world record | AR area record | CR championship record | GR games record | NR national record | OR Olympic record | PB personal best | SB season best | WL world leading (in a given season)
Note: 1 – Georg Andersen of Norway originally won the silver medal in the shot put, but was disqualified after he tested positive for steroids.[2]
Women's results[edit]
Track[edit]
1983 | 1987 | 1991 | 1993 | 1995
Games
Gold
Silver
Bronze
100 m
details Katrin Krabbe (GER) 10.99 Gwen Torrence (USA) 11.03 Merlene Ottey (JAM) 11.06
200 m
details Katrin Krabbe (GER) 22.09 Gwen Torrence (USA) 22.16 Merlene Ottey (JAM) 22.21
400 m
details Marie-José Pérec (FRA) 49.13 Grit Breuer (GER) 49.42 Sandra Myers (ESP) 49.78
800 m
details Liliya Nurutdinova (URS) 1:57.50 Ana Fidelia Quirot (CUB) 1:57.55 Ella Kovacs (ROU) 1:57.58
1500 m
details Hassiba Boulmerka (ALG) 4:02.21 Tetyana Samolenko-Dorovskikh (URS) 4:02.58 Lyudmila Rogachova (URS) 4:02.72
3000 m
details Tetyana Samolenko-Dorovskikh (URS) 8:35.82 Yelena Romanova (URS) 8:36.06 Susan Sirma (KEN) 8:39.41
(AR)
10,000 m
details Liz McColgan (GBR) 31:14.31 Zhong Huandi (CHN) 31:35.08 Wang Xiuting (CHN) 31:35.99
Marathon
details Wanda Panfil (POL) 2:29:53 Sachiko Yamashita (JPN) 2:29:57 Katrin Dörre (GER) 2:30:10
100 m hurdles
details Ludmila Narozhilenko (URS) 12.59 Gail Devers (USA) 12.63 Nataliya Grygoryeva (URS) 12.69
400 m hurdles
details Tatyana Ledovskaya (URS) 53.11
(CR) Sally Gunnell (GBR) 53.16
NR Janeene Vickers (USA) 53.47
10 km walk
details Alina Ivanova (URS) 42:57
(CR) Madelein Svensson (SWE) 43:13 Sari Essayah (FIN) 43:13
4 × 100 m relay
details Jamaica (JAM)
Dahlia Duhaney
Juliet Cuthbert
Beverly McDonald
Merlene Ottey
Merlene Frazer*
41.94 Soviet Union (URS)
Natalya Kovtun
Galina Malchugina
Yelena Vinogradova
Irina Privalova 42.20 Germany (GER)
Grit Breuer
Katrin Krabbe
Sabine Richter
Heike Drechsler 42.33
4 × 400 m relay
details Soviet Union (URS)
Tatyana Ledovskaya
Lyudmila Dzhigalova
Olga Nazarova
Olha Vladykina-Bryzhina
Anna Chuprina* 3:18.43 United States (USA)
Rochelle Stevens
Diane Dixon
Jearl Miles
Lillie Leatherwood
Natasha Kaiser-Brown* 3:20.15 Germany (GER)
Uta Rohländer
Katrin Krabbe
Christine Wachtel
Grit Breuer
Annett Hesselbarth*
Katrin Schreiter* 3:21.25
WR world record | AR area record | CR championship record | GR games record | NR national record | OR Olympic record | PB personal best | SB season best | WL world leading (in a given season)
Note: * Indicates athletes who ran in preliminary rounds.
Field[edit]
1983 | 1987 | 1991 | 1993 | 1995
Games
Gold
Silver
Bronze
Long jump
details Jackie Joyner-Kersee (USA) 7.32 Heike Drechsler (GER) 7.29 Larysa Berezhna (URS) 7.11
High jump
details Heike Henkel (GER) 2.05 Yelena Yelesina (URS) 1.98 Inha Babakova (URS) 1.96
Shot put
details Huang Zhihong (CHN) 20.83 Natalya Lisovskaya (URS) 20.29 Svetlana Krivelyova (URS) 20.16
Discus throw
details Tsvetanka Khristova (BUL) 71.02 Ilke Wyludda (GER) 69.12 Larisa Mikhalchenko (URS) 68.26
Javelin throw
details Xu Demei (CHN) 68.78 Petra Meier (GER) 68.68 Silke Renk (GER) 66.80
Heptathlon
details Sabine Braun (GER) 6672 Liliana Năstase (ROU) 6493 Irina Belova (URS) 6448
WR world record | AR area record | CR championship record | GR games record | NR national record | OR Olympic record | PB personal best | SB season best | WL world leading (in a given season)
Note: * Indicates athletes who only ran in the preliminary round and also received medals.
Medal table by country[edit]
Rank
Nation
Gold
Silver
Bronze
Total
1. United States 10 8 8 26
2. Soviet Union 9 9 11 29
3. Germany 5 4 8 17
4. Kenya 4 3 1 8
5. Great Britain 2 2 3 7
6. China 2 1 1 4
7. Algeria 2 0 1 3
8. Jamaica 1 1 3 5
9. Finland 1 1 1 3
10= France 1 1 0 2
10= Japan 1 1 0 2
12= Bulgaria 1 0 0 1
12= Italy 1 0 0 1
12= Poland 1 0 0 1
12= Switzerland 1 0 0 1
12= Zambia 1 0 0 1
17. Cuba 0 2 0 2
18= Canada 0 1 1 2
18= Hungary 0 1 1 2
18= Romania 0 1 1 2
21= Brazil 0 1 0 1
21= Djibouti 0 1 0 1
21= Ethiopia 0 1 0 1
21= Namibia 0 1 0 1
21= Netherlands 0 1 0 1
21= Norway 0 1 0 1
21= Sweden 0 1 0 1
28. Morocco 0 0 2 2
29. Spain 0 0 1 1
Total
43
43
43
129
See also[edit]
1991 in athletics (track and field)
References[edit]
Jump up ^ "iaaf.org - Osaka 2007 - History". Archived from the original on 2009-05-10. Retrieved 2009-04-03.
Jump up ^ Track and Field. LA Times (1991-09-13). Retrieved on 2011-06-22.
IAAF 1991
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IAAF World Road Relay Championships
Retrieved from "https://en.wikipedia.org/w/index.php?title=1991_World_Championships_in_Athletics&oldid=796499996"
Categories:
1991 in athletics (track and field)
1991 World Championships in Athletics
1991 in Japanese sport
Sports competitions in Tokyo
International athletics competitions hosted by Japan
World Championships in Athletics
August 1991 sports events
September 1991 sports events
1990s in Tokyo
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values: Category:1991 in athletics (track and field)

values: Category:1991 World Championships in Athletics

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values: Category:World Championships in Athletics

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values: بطولة العالم لألعاب القوى 1991 – Arabic

values: Campionat del Món d'atletisme de 1991 – Catalan

values: Mistrovství světa v atletice 1991 – Czech

values: Leichtathletik-Weltmeisterschaften 1991 – German

values: 1991. aasta kergejõustiku maailmameistrivõistlused – Estonian

values: Campeonato Mundial de Atletismo de 1991 – Spanish

values: مسابقات جهانی دو و میدانی ۱۹۹۱ – Persian

values: Championnats du monde d'athlétisme 1991 – French

values: 1991년 세계 육상 선수권 대회 – Korean

values: Svjetsko prvenstvo u atletici 1991. – Croatian

values: Campionati del mondo di atletica leggera 1991 – Italian

values: אליפות העולם באתלטיקה 1991 – Hebrew

values: 1991 m. Pasaulio lengvosios atletikos čempionatas – Lithuanian

values: 1991-es atlétikai világbajnokság – Hungarian

values: Wereldkampioenschappen atletiek 1991 – Dutch

values: 1991年世界陸上競技選手権大会 – Japanese

values: Campionat del Mond d'atletisme de 1991 – Occitan

values: Mistrzostwa Świata w Lekkoatletyce 1991 – Polish

values: Campeonato Mundial de Atletismo de 1991 – Portuguese

values: Чемпионат мира по лёгкой атлетике 1991 – Russian

values: Svetovno prvenstvo v atletiki 1991 – Slovenian

values: Светско првенство у атлетици на отвореном 1991. – Serbian

values: Yleisurheilun maailmanmestaruuskilpailut 1991 – Finnish

values: Världsmästerskapen i friidrott 1991 – Swedish

values: 1991 Dünya Atletizm Şampiyonası – Turkish

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