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22-AUGUST-2008 06:13:22 - Acetylcholinesterase For other uses, see American College of Healthcare Executives. Acetylcholinesterase Yt blood group PDB rendering based on 1b41. Proteopedia Acetylcholinesterase. Available structures: 1b41, 1f8u, 1vzj Identifiers Symbols AChE; ARAChE; N-AChE; YT External IDs OMIM: 100740 MGI: 87876 HomoloGene: 543 Gene ontology Molecular function: beta-amyloid binding acetylcholinesterase activity cholinesterase activity carboxylesterase activity collagen binding hydrolase activity serine hydrolase activity acetylcholine binding protein homodimerization activity laminin-1 binding Cellular component: extracellular region basal lamina Golgi apparatus membrane synapse perinuclear region of cytoplasm Biological process: acetylcholine catabolic process in synaptic cleft osteoblast development DNA replication cell adhesion synaptogenesis muscle development cell proliferation response to wounding negative regulation of synaptic transmission, cholinergic amyloid precursor protein metabolic process positive regulation of protein secretion RNA expression pattern More reference expression data Orthologs Human Mouse Entrez 43 11423 Ensembl ENSG00000087085 ENSMUSG00000023328 Uniprot P22303 Q543Z1 Refseq NM_000665 mRNA NP_000656 protein NM_009599 mRNA NP_033729 protein Location Chr 7: 100.33 - 100.33 Mb Chr 5: 137.52 - 137.52 Mb Pubmed search 1 2 Acetylcholinesterase Yt blood group, also known as AChE, is a human enzyme coded for by a gene. Acetylcholinesterase hydrolyzes the neurotransmitter acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms, which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single AChE gene; and the structural diversity in the gene products arises from alternative mRNA splicing and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle, and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively-spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide PI moieties added post-translationally.1 Acetylcholinesterase is the target of nerve gases. The agents blocks the function of acetylcholinesterase and thus causes interminable muscle contraction throughout the body. Contents 1 See also 2 References 3 Further reading 4 External links See also Acetylcholinesterase inhibitor Cholinesterase enzyme References ^ Entrez Gene: ACHE acetylcholinesterase Yt blood group. Further reading Silman I, Futerman AH 1988. Modes of attachment of acetylcholinesterase to the surface membrane.. Eur. J. Biochem. 170 1-2: 11-22. PMID 3319614. Soreq H, Seidman S 2001. Acetylcholinesterase--new roles for an old actor.. Nat. Rev. Neurosci. 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. 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. 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, et al. 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. 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, et al. 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, et al. 1992. The human gene encoding acetylcholinesterase is located on the long arm of chromosome 7.. Am. J. Hum. Genet. 51 1: 170-7. PMID 1609795. Li Y, Camp S, Rachinsky TL, et al. 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, et al. 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, et al. 1991. Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.. Proc. Natl. Acad. Sci. U.S.A. 87 24: 9688-92. PMID 2263619. Chhajlani V, Derr D, Earles B, et al. 1989. Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase.. FEBS Lett. 247 2: 279-82. PMID 2714437. Lapidot-Lifson Y, Prody CA, Ginzberg D, et al. 1989. Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells: correlation with various leukemias and abnormal megakaryocytopoiesis.. Proc. Natl. Acad. Sci. U.S.A. 86 12: 4715-9. PMID 2734315. Bazelyansky M, Robey E, Kirsch JF 1986. Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase.. Biochemistry 25 1: 125-30. 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, et al. 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. 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. 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. PMID 8248502. External links Proteopedia Acetylcholinesterase ATSDR Case Studies in Environmental Medicine: Cholinesterase Inhibitors, Including Pesticides and Chemical Warfare Nerve Agents U.S. Department of Health and Human Services This article on a gene on chromosome 7 is a stub. v d e Hydrolase: esterases EC 3.1 3.1.1: Carboxylic ester hydrolases Cholinesterase Acetylcholinesterase, Butyrylcholinesterase - Pectinesterase - 6-phosphogluconolactonase - PAF acetylhydrolase Lipase Gastric/Lingual, Pancreatic, Lysosomal, Hormone-sensitive, Endothelial, Hepatic, Lipoprotein, Monoacylglycerol, Diacylglycerol Phospholipase A1, A2, B 3.1.2: Thioesterase Palmitoyl thioesterase - Ubiquitin carboxy-terminal hydrolase L1 3.1.3: Phosphatase Alkaline phosphatase - Acid phosphatase Prostatic/Tartrate resistant acid phosphatase/Purple acid phosphatases - Nucleotidase - Glucose 6-phosphatase - Fructose 1,6-bisphosphatase - Calcineurin - Phosphoprotein phosphatase PP2A - OCRL - Pyruvate dehydrogenase phosphatase - Fructose 2,6-bisphosphatase - Protein tyrosine phosphatase - PTEN 3.1.4: Phosphodiesterase Autotaxin - Phospholipase C, D - Sphingomyelin phosphodiesterase - PDE1 - PDE2 - PDE3 - PDE5 3.1.6: Sulfatase Arylsulfatase B - Steroid sulfatase - Galactosamine-6 sulfatase - Arylsulfatase A - Iduronate-2-sulfatase - N-acetylglucosamine-6-sulfatase other Nuclease v d e Metabolism: amino acid metabolism - neurotransmitter enzymes histidine→histamine anabolism: Histidine decarboxylase catabolism: Histamine N-methyltransferase - Amine 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 aminotransferase - 4-aminobutyrate transaminase tryptophan→serotonin→melatonin Tryptophan hydroxylase - Aromatic L-amino acid decarboxylase - Acetylserotonin O-methyltransferase arginine→NO Nitric oxide synthase NOS1, NOS2A, NOS3 choline→Acetylcholine anabolism: Choline acetyltransferase catabolism: Cholinesterase Acetylcholinesterase, Butyrylcholinesterase see also intermediates Retrieved from http://en..org/wiki/Acetylcholinesterase Categories: Genes on chromosome 7 | Human proteins | Chromosome 7 gene stubs Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages Dansk Deutsch Español Nederlands ‪Norsk bokmÃ¥l‬ Polski РуÑ?Ñ?кий Suomi Türkçe This page was last modified on 12 August 2008, at 18:03
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