Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1433, Issue 1-2, 1999, Pages 281-293

  Masson, Patrick ^a   Xie, Weihua ^b   Froment, Marie Thérèse ^a   Levitsky, Vladislav ^a   Fortier, Pierre Louis ^c   Albaret, Christine ^c   Lockridge, Oksana ^b  

^a CENTRE DE RECHERCHES   (France)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^c Delegation Generale pour l'Armement   (France)

Author keywords

Butyrylcholinesterase; Double mutant cycle; Peripheral anionic site; Substrate binding

Indexed keywords

BUTYRYLTHIOCHOLINE; CHOLINESTERASE; TETRAMETHYLAMMONIUM;

ARTICLE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME SUBSTRATE; HUMAN; HYDROLYSIS; MOLECULAR DYNAMICS; MUTANT; MUTATION; PRIORITY JOURNAL;

BINDING SITES; BUTYRYLCHOLINESTERASE; BUTYRYLTHIOCHOLINE; CHOLINESTERASE INHIBITORS; HUMANS; KINETICS; MUTATION; PROTEIN CONFORMATION; QUATERNARY AMMONIUM COMPOUNDS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 0032774638     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00115-6     Document Type: Article

References (49)

1. Massoulié J., Pezzementi L., Bon S., Krejci E., Vallette F.M. Prog. Neurobiol. 41:1993;31-91.
2. O. Lockridge, in: W. Kalow (Ed.), Pharmacogenetics of Drug Metabolism, Pergamon Press, New York, 1992, pp. 15-50.
3. Cashman J.R., Perotti B.Y.T., Berkman C.E., Lin J. Environ. Health Perspect. 104:1996;23-40.
4. Mattes C.E., Belendiuk G.W., Lynch T.J., Brady R.O., Dretchen K.L. Addict. Biol. 3:1998;171-188.
5. Nigg H.N., Ramos L.E., Graham E.M., Sterling J., Brown S., Cornell J.A. Fund. Appl. Toxicol. 33:1996;272-281.
6. Krasowski M.D., McGehee D.S., Moss J. Can. J. Anaesth. 44:1997;525-534.
7. B. Ballantyne, T.C. Marss, Clinical and Experimental Toxicology of Organophosphates and Carbamates, Butterworth/ Heinemann, London, 1992.
8. Millard C.B., Lockridge O., Broomfield C.A. Biochemistry. 37:1998;237-247.
9. Quinn D.M. Chem. Rev. 87:1987;955-979.
10. Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Science. 253:1991;872-879.
11. Harel M., Sussman J., Krejci E., Bon S., Chanal P., Massoulié J. Proc. Natl. Acad. Sci. USA. 89:1992;10827-10831.
12. Radic Z., Pickering N.A., Vellom D.C., Camp S., Taylor P. Biochemistry. 32:1993;12074-12084.
13. Ordentlich A., Barak D., Kronman C., Ariel N., Segal Y., Velan B., Shafferman A. J. Biol. Chem. 270:1995;2082-2091.
14. Masson P., Froment M.-Th., Bartels C., Lockridge O. Eur. J. Biochem. 235:1996;36-48.
15. Masson P., Legrand P., Bartels C.F., Froment M.-Th., Schopfer L.M., Lockridge O. Biochemistry. 36:1997;2266-2277.
16. Barak D., Kronman C., Ordentlich A., Ariel N., Bromberg A., Marcus D., Lazar A., Velan B., Shafferman A. J. Biol. Chem. 264:1994;6296-6305.
17. Mutero A., Pralavorio M., Simeon V., Fournier D. NeuroReport. 3:1992;39-42.
18. Nachon F., Ereth-Sabatier L., Loew D., Colas C., van Dorsselaer A., Goeldner M. Biochemistry. 37:1998;10507-10513.
19. Ordentlich A., Barak D., Chronman C., Flashner Y., Leitner M., Segall Y., Ariel N., Cohen S., Velan B., Shafferman A. J. Biol. Chem. 268:1993;17083-17095.
20. Eriksson H., Augustinsson K.-B. Biochim. Biophys. Acta. 567:1979;161-173.
21. Cauet G., Friboulet A., Thomas D. Biochem. Cell. Biol. 65:1987;529-535.
22. Szegletes T., Mallender W.D., Thomas P.J., Rosenberry T.L. Biochemistry. 38:1999;122-133.
23. Barak D., Ordentlich A., Bromberg A., Kronman C., Marcus D., Lazar A., Ariel N., Velan B., Shafferman A. Biochemistry. 34:1995;15444-15452.
24. Gibney G., Camp S., Dionne M., McPhee-Quigley K. Proc. Natl. Acad. Sci. USA. 87:1990;7546-7550.
25. Vellom D.C., Radic R., Li Y., Pickering N.A., Camp S., Taylor P. Biochemistry. 32:1993;12-17.
26. Saxena A., Redman A.M.G., Qian N., Lockridge O., Doctor B.P. Biochemistry. 36:1997;14642-14651.
27. Levitsky V., Weihua X., Froment M-T., Lockridge O., Masson P. Biochim. Biophys. Acta. 1429:1999;422-430.
28. Goodyer P., Mautner H.G. Biochem. Pharmacol. 16:1967;2044-2045.
29. Ellman G.L., Courtney K.D., Andreas V., Featherstone R.M. Biochem. Pharmacol. 7:1961;88-95.
30. Main A.R., Miles K.E., Braid P.E. Biochem. J. 78:1961;769-776.
31. Fraenkel-Conrat H. Methods Enzymol. 4:1957;247-273.
32. Baldwin R.L. Biophys. J. 71:1996;2056-2063.
33. Cornish-Bowden A. Biochem. J. 137:1974;143-144.
34. Mildvan A.S., Weber D.J. Arch. Biochem. Biophys. 294:1992;327-340.
35. Horovitz A. Folding Design. 1:1996;R121-R126.
36. DiCera E. Adv. Protein Chem. 51:1998;59-119.
37. Brooks C.L. III, Brünger A., Karplus M. Biopolymers. 24:1985;843-865.
38. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., Karplus M. J. Comp. Chem. 4:1983;187-217.
39. Jorgensen W.L., Chandrasekhar J., Madura J.D., Impey R.W., Klein M.L. J. Chem. Phys. 79:1983;926-935.
40. Nakagawa S., Yu H.A., Karplus M., Umeyama H. Proteins Struct. Funct. Genet. 16:1993;172-194.
41. Brünger A.T., Brooks C.L. III. Chem. Phys. Lett. 105:1984;495-500.
42. Ryckaert J.-P., Ciccotti G., Berendsen H.J.C.J. Comput. Phys. 23:1977;327-341.
43. Erdos E.G., Foldes F.F., Zsigmond E.K., Baart N., Zwartz J.A. Science. 128:1958;92-93.
44. Valentino R.J., Lockridge O., Eckerson H.W., LaDu B.N. Biochem. Pharmacol. 30:1981;1643-1649.
45. W.N. Aldridge, E. Reiner, Enzyme Inhibitors as Substrates, North-Holland, Amsterdam, 1972, p. 120.
46. Harel M., Quinn D.M., Nair H.K., Silman I., Sussman J.L. J. Am. Chem. Soc. 118:1996;2340-2346.
47. Ma J.C., Dougherty D.A. Chem. Rev. 97:1997;1303-1324.
48. P. Masson, C. Cléry, P. Guerra, P.-L. Fortier, C. Albaret, O. Lockridge, in: B.P. Doctor (Ed.), Structure and Function of Cholinesterases and Related Proteins, Plenum Press, New York, 1998, pp. 419-424.
49. P. Masson, C. Clery, P. Guerra, A. Redslob, C. Albaret, P.-L. Fortier, Biochem. J. (1999) in press.