5,655
Views
99
CrossRef citations to date
0
Altmetric
Research Article

Acetylcholinesterases – the structural similarities and differences

, , , &
Pages 417-424 | Received 06 Dec 2006, Accepted 29 Mar 2007, Published online: 04 Oct 2008

References

  • Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM. Molecular and cellular biology of cholinesterases. Progr Neurobiol 1993; 41: 31–91
  • Patočka J, Kuča K, Jun D. Acetylcholinesterase and butyrylcholinesterase — important enzymes in human body. Acta Medica 2004; 47(4)215–228
  • Quinn DM. Acetylcholinesterase - enzyme structure, reaction dynamics, and virtual transition-states. Chem Rev 1987; 87(5)955–979
  • Nolte HJ, Rosenberry TL, Neumann E. Effective charge on acetylcholinesterase active-sited determined from the ionic-strength dependence of association rate constants with cationic ligands. Biochemistry 1980; 19(16)3705–3711
  • Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL. An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc Natl Acad Sci USA 1993; 90: 5128–5132
  • Sussman J, Harel M, Frolow F, Oefner C, Goldman A, Toker R, Silman I. Atomic structure of acetylcholinesterase from torpedo califonica — a prototypic acetylcholine-binding protein. Science 1991; 253(5022)872–879
  • Hougton PJ, Ren Y, Howes MJ. Acetylcholinesterase inhibitors from plants and fungi. Nat Prod Rep 2006; 23: 181–199
  • Singh AK. Molecular properties and inhibition kinetics of acetylcholinesterase obtained from rat brain and cockroach ganglion. Toxicol Ind Health 1990; 6(6)551–570
  • Needleman SB, Wunch ChD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970; 48: 443–453
  • Feng DF, Doolittle FR. Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J Mol Evol 1987; 25: 351–360
  • Thompson JD, Higgins DG, Gibson TJ. Clustal-W - Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22: 4673
  • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997; 25(24)4876–4882
  • Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The protein data bank. Nucleic Acids Res 2000; 28(1)235–242
  • Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL. Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr 2000; 56(D)1385–1394
  • Bourne Y, Taylor P, Radic Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003; 22(1)1–12
  • Harel M, Weik M, Silman I, Sussman JL. Native Acetylcholinesterase (E.C. 3.1.1.7) from torpedo californica at 1.8A resolution. To be Published.
  • Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL. Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors. Protein Sci 2000; 2(6)1063–1072
  • Bairoch A, Apweiler R, Wu CH, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Natale DA, O'Donovan C, Redaschi N, Yeh LS. The universal protein resource (UniProt). Nucleic Acids Res 2005; 33: D154–D159
  • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 1997; 18(15)2714–2723
  • Swiss-Pdb Viewer URL: http://www.expasy.org/spdbv/.
  • Kuca K, Cabal J, Kassa J. In vitro reactivation of sarin-inhibited brain acetylcholinesterase from different species by various oximes. J Enz Inhib Med Chem 2005; 20(3)227–232
  • Sali A, Blundell TL. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 1993; 234(3)779–815

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.