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Showing drug card for Acetylcholine (DB03128)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2008-08-26 15:24:27
Primary Accession Number DB03128
Secondary Accession Number
  • EXPT00412
Name Acetylcholine
Drug Type
  • Experimental
  • Small Molecule
Description A neurotransmitter. Acetylcholine in vertebrates is the major transmitter at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system. It is generally not used as an administered drug because it is broken down very rapidly by cholinesterases, but it is useful in some ophthalmological applications. [PubChem]
Synonyms Not Available
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name 2-acetyloxyethyl-trimethylazanium
Chemical Formula C7H16NO2
Chemical Structure Structure
CAS Registry Number 51-84-3
InChI Identifier InChI=1/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1
InChI Key OIPILFWXSMYKGL-UHFFFAOYAY
KEGG Drug Not Available
KEGG Compound C01996 Link Image
PubChem Compound 187 Link Image
PubChem Substance 5093 Link Image
ChEBI ID 15355 Link Image
PharmGKB ID Not Available
HET ID ACH Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 146.2074
Monoisotopic Molecular Weight 146.1181
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.36e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP -2.90 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.13 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 2ACE Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC(=O)OCC[N+](C)(C)C
Canonical SMILES CC(=O)OCC[N+](C)(C)C
Drug Category
  • Acetylcholinesterase inhibitor
  • Cholinergic Agents
  • Vasodilator Agents
ATC Codes Not Available
AHFS Codes Not Available
Indication Not Available
Pharmacology Not Available
Mechanism of Action Not Available
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References Not Available
Organisms Affected Not Available
Targets
  1. Acetylcholinesterase
Drug Target 1 [top]
Target 1 ID 2549
Target 1 Name Acetylcholinesterase
Target 1 Synonyms
  1. AChE
  2. Acetylcholinesterase precursor
  3. EC 3.1.1.7
Target 1 Gene Name Not Available
Target 1 Protein Sequence >Acetylcholinesterase precursor 
MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPP
VGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNI
WVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALH
GSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLF
RRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEW
NVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGF
SKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHN
VICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYT
AEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQ
MCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF
Target 1 Number of Residues 595
Target 1 Molecular Weight 65907
Target 1 Theoretical pI 6.00
Target 1 GO Classification
Function
carboxylesterase activity
acetylcholinesterase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
carboxylic ester hydrolase activity
cholinesterase activity
Process
physiological process
metabolism
cellular metabolism
neurotransmitter metabolism
acetylcholine metabolism
acetylcholine catabolism
acetylcholine catabolism in synaptic cleft
Component
Not Available
Target 1 General Function Lipid transport and metabolism
Target 1 Specific Function Rapidly hydrolyzes choline released into the synapse. May be involved in cell-cell interactions
Target 1 Pathways
Name SMPDB Link KEGG Link
Glycerophospholipid metabolism map00564 Link Image
Target 1 Reactions
  • acetylcholine + H2O = choline + acetate
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-21
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 736320 Link Image
Target 1 UniProtKB/Swiss-Prot ID P04058 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ACES_TORCA Link Image
Target 1 PDB ID 1ODC Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • GPI- anchor. Isoform T:Cell membrane
  • Isoform H:Cell membrane
  • lipid-anchor
  • peripheral membrane pro
Target 1 Gene Sequence >1791 bp 
ATGAACCTGCTGGTCACCTCTTCGCTGGGCGTGCTTCTGCACTTGGTCGTCCTGTGCCAG
GCGGACGATCACTCTGAGCTCCTGGTCAACACCAAGTCGGGAAAAGTCATGGGAACAAGA
GTCCCAGTCCTCTCCAGCCACATCAGCGCTTTCCTGGGGATTCCCTTTGCCGAGCCTCCA
GTTGGGAACATGAGGTTCAGGAGACCTGAGCCCAAGAAACCGTGGTCGGGAGTCTGGAAC
GCTTCCACCTATCCCAACAACTGCCAGCAGTACGTTGACGAGCAGTTCCCTGGATTTTCA
GGTTCAGAGATGTGGAATCCGAACAGAGAGATGAGTGAGGACTGTTTGTACCTCAACATT
TGGGTGCCTTCTCCGAGGCCGAAGAGTACAACCGTCATGGTGTGGATCTACGGAGGCGGT
TTCTACAGCGGGTCCTCGACGTTGGACGTCTACAATGGGAAATACCTTGCCTACACCGAG
GAGGTGGTGCTGGTCTCTCTGAGCTACCGGGTGGGCGCTTTTGGTTTTCTCGCCCTCCAC
GGCAGCCAGGAGGCACCAGGAAATGTGGGCCTCCTGGACCAGAGGATGGCACTGCAGTGG
GTGCACGACAACATCCAGTTCTTCGGCGGGGACCCCAAGACGGTGACCATCTTCGGAGAG
AGTGCCGGCGGCGCCTCTGTCGGCATGCACATTCTCTCCCCGGGGAGCCGAGACCTCTTC
CGCCGGGCCATCCTTCAGAGCGGCTCGCCCAATTGCCCGTGGGCGTCTGTCTCTGTTGCT
GAAGGCCGCAGGAGGGCGGTCGAGCTGGGAAGAAACCTCAACTGTAACCTCAACAGCGAC
GAAGAGCTCATCCACTGTCTGAGGGAAAAGAAGCCTCAGGAGTTGATTGACGTGGAGTGG
AATGTCCTTCCCTTTGACAGTATCTTCAGGTTCTCCTTCGTTCCCGTCATCGATGGGGAA
TTCTTCCCAACCTCCCTGGAATCTATGTTGAACTCTGGCAACTTCAAGAAGACTCAGATC
TTACTGGGAGTCAACAAGGACGAGGGCTCGTTTTTCCTCTTGTACGGAGCGCCGGGTTTC
AGCAAGGACTCTGAAAGCAAAATCTCTCGGGAAGACTTCATGTCAGGGGTCAAGCTAAGC
GTTCCCCACGCCAATGACTTAGGGTTGGACGCTGTCACGCTACAGTACACAGACTGGATG
GATGACAACAATGGTATAAAGAACAGAGATGGATTGGACGACATCGTAGGGGACCACAAC
GTCATATGCCCCTTGATGCACTTTGTTAACAAGTACACCAAGTTTGGCAATGGCACCTAC
CTGTACTTCTTCAACCACCGAGCCTCAAACCTGGTGTGGCCGGAGTGGATGGGCGTCATC
CACGGCTATGAGATTGAGTTCGTCTTCGGGCTGCCTCTGGTGAAGGAGCTGAACTACACA
GCGGAGGAGGAAGCGCTGAGCCGGAGGATAATGCATTACTGGGCGACATTCGCAAAGACT
GGAAACCCAAACGAACCCCACTCACAGGAGAGCAAATGGCCTCTCTTCACTACCAAGGAG
CAGAAATTTATTGACCTCAACACAGAACCCATGAAAGTCCACCAGCGACTCCGAGTTCAG
ATGTGCGTGTTCTGGAACCAGTTCCTCCCCAAGCTCCTCAACGCCACAGAGACCATTGAT
GAGGCAGAACGCCAGTGGAAGACGGAGTTTCATCGGTGGAGTTCCTACATGATGCACTGG
AAGAACCAATTTGACCACTACAGCAGACACGAGAGCTGTGCTGAGCTGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs Not Available
Target 1 General References
  1. Bartolucci C, Perola E, Cellai L, Brufani M, Lamba D: "Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase. Biochemistry. 1999 May 4;38(18):5714-9. [PubMed Link Image]
  2. Millard CB, Kryger G, Ordentlich A, Greenblatt HM, Harel M, Raves ML, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL: Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level. Biochemistry. 1999 Jun 1;38(22):7032-9. [PubMed Link Image]
  3. Kryger G, Silman I, Sussman JL: Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs. Structure. 1999 Mar 15;7(3):297-307. [PubMed Link Image]
  4. Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL: Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution. FEBS Lett. 1999 Dec 17;463(3):321-6. [PubMed Link Image]
  5. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I: Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872-9. [PubMed Link Image]
  6. Kreienkamp HJ, Weise C, Raba R, Aaviksaar A, Hucho F: Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6117-21. [PubMed Link Image]
  7. Gibney G, Camp S, Dionne M, MacPhee-Quigley K, Taylor P: Mutagenesis of essential functional residues in acetylcholinesterase. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7546-50. [PubMed Link Image]
  8. Maulet Y, Camp S, Gibney G, Rachinsky TL, Ekstrom TJ, Taylor P: Single gene encodes glycophospholipid-anchored and asymmetric acetylcholinesterase forms: alternative coding exons contain inverted repeat sequences. Neuron. 1990 Feb;4(2):289-301. [PubMed Link Image]
  9. Schumacher M, Maulet Y, Camp S, Taylor P: Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase. J Biol Chem. 1988 Dec 15;263(35):18979-87. [PubMed Link Image]
  10. Gibney G, MacPhee-Quigley K, Thompson B, Vedvick T, Low MG, Taylor SS, Taylor P: Divergence in primary structure between the molecular forms of acetylcholinesterase. J Biol Chem. 1988 Jan 25;263(3):1140-5. [PubMed Link Image]
  11. 3753747 Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor SS, Friedmann T, Taylor P: Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature. 1986 Jan 30-Feb 5;319(6052):407-9.
  12. 3759980 MacPhee-Quigley K, Vedvick TS, Taylor P, Taylor SS: Profile of the disulfide bonds in acetylcholinesterase. J Biol Chem. 1986 Oct 15;261(29):13565-70.
  13. 3900071 MacPhee-Quigley K, Taylor P, Taylor S: Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences. J Biol Chem. 1985 Oct 5;260(22):12185-9.
  14. 8257440 Mehlert A, Varon L, Silman I, Homans SW, Ferguson MA: Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica. Biochem J. 1993 Dec 1;296 ( Pt 2):473-9.
  15. 8597567 Bucht G, Hjalmarsson K: Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored form. Biochim Biophys Acta. 1996 Feb 8;1292(2):223-32.
  16. 8747462 Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL: Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Structure. 1995 Dec 15;3(12):1355-66.
  17. 8989325 Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL: Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A. Nat Struct Biol. 1997 Jan;4(1):57-63.
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.