Butyrylcholinesterase: 3D structure, catalytic mechanisms;Structure tridimensionnelle de la butyrylcholinestérase humaine: Hypothèses mécanistiques et ingéniérie de mutéines dégradant les composés organophosphorés

Annales Pharmaceutiques Francaises

Volumn 63, Issue 3, 2005, Pages 194-206

  Nachon, Fl ^a   Nicolet, Y ^b   Masson, P ^a  

^a CENTRE DE RECHERCHES   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

Acetylcholinesterase; Catalytic mechanism; Enzyme engineering; Enzymotherapy; Organophosphorus; Prophylaxis

Indexed keywords

CHOLINESTERASE; CHOLINESTERASE INHIBITOR; DYFLOS; NERVE GAS; ORGANOPHOSPHORUS COMPOUND;

AGING; CATALYSIS; DEALKYLATION; EMERGENCY TREATMENT; ENZYME BINDING; ENZYME ENGINEERING; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME THERAPY; HYDROLYSIS; INHIBITION KINETICS; INTOXICATION; NEUROTOXICITY; NONHUMAN; REVIEW; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING;

EID: 21344450367     PISSN: 00034509     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0003-4509(05)82274-6     Document Type: Review

References (32)

1. Masson P. Conception par génie biomoléculaire d'épurateurs catalytiques des agents organophosphorés in Entretiens Science et Défense Tome 2. Paris: DGA; 1998, 191-204.
2. Darvesh S, Hopkins DA, Geula C. Neurobiology of bytyrylcholinesterase. Nat Rev Neurosci 2003; 4: 131-8.
3. Mesulam MM, Guillozet A, Shaw P, Levey A, Duysen EG, Lockridge O. Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neurosci 2002; 110: 627-39.
4. Giacobini E. Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol Res 2004; 50: 433-40.
5. Kovarik Z, Simeon-Rudolf V. Interaction of human butyrylcholinesterase variants with bambuterol and terbutaline. J. Enz. Inhib. Med. Chem. 2004; 19: 113-7.
6. Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol Ther 1990; 47: 35-60.
7. Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL. Complete amino acid sequence of human serum cholinesterase. J. Biol. Chem. 1987; 262: 549-57.
8. Doctor BP. Butyrylcholinesterase: its use for prophylaxis of organophosphate exposure in Butyrylcholinesterase: its function and inhibitors. London & New York: Martin Dunitz (Giacobini E Ed); 2003, 163-77.
9. Ashani Y, Pistinner S. Estimation of the upper limit of human butyrylcholinesterase dose required for protection against organophosphates toxicity: a mathematically based toxicokinetic model. Toxicol Sci 2004; 77: 358-67.
10. Raveh L, Grauer E, Grunwald J, Cohen E, Ashani Y. The stoichiometry of protection against soman and VX toxicity in monkeys pretreated with human butyrylcholinesterase. Toxicol Appl Pharmacol 1997; 145: 43-53.
11. Broomfield CA, Maxwell DM, Solana RP, Castro CA, Finger AV, Lenz DE. Protection by butyrylcholinesterase against organophosphorus poisoning in nonhuman primates. J Pharmacol Exp Ther 1991; 259: 633-8.
12. Wolfe AD, Blick DW, Murphy MR, Miller SA, Gentry MK, Hartgraves SL et Doctor BP. Use of cholinesterases as pretreatment drugs for the protection of rhesus monkeys against soman toxicity. Toxicol Appl Pharmacol 1992; 117: 189-93.
13. Cesaroli DM, Griffiths EM, Doctor BP, Saxena A, Fedorko JM, Greig NH, Yu QS, Huang Y, Wilgus H, Karatzas CN, Koplovitz I et Lenz DE. In vitro and in vivo characterization of recombinant human butyrylcholinesterase (Protexia ™) as a potential nerve agent bioscavenger. Bioscience Review. Baltimore, May 2004.
14. Salamon R. Rapport de mission du groupe de travail chargé d'analyser les données sanitaires relatives aux anciens combattants français de la guerre du Golfe, 24 mai 2001. http://sante.gouv.fr/pdf/ rapport_salamon.pdf
15. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L et Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991; 253: 872-9.
16. Millard CB et Broomfield CA. A computer model of glycosylated human butyrylcholinesterase. Biochim Biophys Res Comm 1992; 189: 1280-6.
17. Millard CB, Lockridge O et Broomfield CA. Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 1995; 34: 15925-33.
18. Lockridge O, Blong RM, Masson P, Froment MT, Millard CB, Broomfield CA. A Single Amino Acid Substitution, Gly117His, Confers Phosphotriesterase (Organophosphorus Acid Anhydride Hydrolase) Activity on Human Butyrylcholinesterase. Biochemistry 1997; 36: 786-95.
19. Schopfer LM, Ticu-Boeck A, Broomfield CA et Lockridge O. Mutants of human butyrylcholinestetase with organophopshate hydrolase activity; evidence that His117 is a general base catalyst for hydrolysis of echothiophate. J Med Chem Def 2004; 2: 1-21.
20. Nachon F, Nicolet Y, Viguié N, Masson P, Fontecilla-Camps JC et Lockridge O. Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase. Eur J Biochem 2002; 269: 630-7.
21. Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC et Nachon F. Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products. J Biol Chem 2003; 278: 41141-7.
22. Nachon F, Masson P, Nicolet Y, Lockridge O et Fontecilla-Camps JC. Comparison of the structures of butyrylcholinesterase and acetylcholineterase in Butyrylcholinesterase: its function and inhibitors. London & New York: Martin Dunitz (Giacobini E Ed); 2003, 39-54.
23. Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I et Sussman JL. Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors. Protein Sci 2000; 9: 1063-72.
24. Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J et Sussman JL. Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc Natl Acad Sci USA 2000; 97: 623-8.
25. Bourne Y, Taylor P, Radic Z et Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003; 22: 1-12.
26. Masson P et Goasdoué JL. Evidence that the conformational stability of 'aged' organophosphate-inhibited cholinesterase is altered. Biochim Biophys Acta 1986; 869: 304-13.
27. Masson P, Cléry C, Guerra P, Redslob A, Albaret C et Fortier PL. Hydration change during the aging of phosphorylated human butyrylcholinesterase: importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures. Biochem J 1999; 343: 361-9.
28. Bourne Y, Hartmuth CK, Radic Z, Sharpless KB, Taylor P et Marchot P. Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation. Proc Natl Acad Sci USA 2004; 101: 1449-54.
29. Masson P, Legrand P, Bartels CF, Froment MT, Schopfer LM. et Lockridge O. Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 1997; 36: 2266-77.
30. Nachon F, Asojo OA, Borgstahl GEO, Masson P et Lockridge O. Role of water in aging of human butyrylcholinesterase inhibited by echothiophate. The crystal structure suggests two alternative mechanisms of aging. Biochemistry 2005, sous presse.
31. Doorn JA, Talley TT, Thompson CM et Richardson RJ. Probing the active sites of butyrylcholinesterase and cholesterol esterase with isomalathion: conserved stereoselective inactivation of serine hydrolases structurally related to acetylcholinesterase. Chem Res Toxicol 2001; 14: 807-13.
32. Masson P, Josse D, Lockridge O, Viguié N, Taupinus C, Buhler C. Enzymes hydrolyzing organophosphates as potential catalytic scavengers against organophosphate poisoning. J Physiol (Paris) 1998; 92: 357-62.