Overlapping drug interaction sites of human butyrylcholinesterase dissected by site-directed mutagenesis

Molecular Pharmacology

Volumn 50, Issue 6, 1996, Pages 1423-1431

  Loewenstein Lichtenstein, Yael ^a,c   Glick, David ^a   Gluzman, Nelly ^a   Sternfeld, Meira ^a   Zakut, Haim ^b   Soreq, Hermona ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b TEL AVIV UNIVERSITY   (Israel)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ANION; ASPARTIC ACID; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; CINCHOCAINE; COCAINE; GLYCINE; SOLANINE; SUXAMETHONIUM; TACRINE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DRUG BINDING SITE; DRUG PROTEIN BINDING; ENZYME ACTIVE SITE; GENETIC PREDISPOSITION; HETEROZYGOTE; LIGAND BINDING; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; XENOPUS LAEVIS;

ANIMALS; BENZENAMINIUM, 4,4'-(3-OXO-1,5-PENTANEDIYL)BIS(N,N-DIMETHYL-N-2-PROPENYL-), DIBROMIDE; BUTYRYLCHOLINESTERASE; CHOLINESTERASE INHIBITORS; HUMANS; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; TACRINE; XENOPUS LAEVIS;

EID: 0030478155     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (35)

1. Prody, C. A., D. Zevin-Sonkin, A. Gnatt, O. Goldberg, and H. Soreq. Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc. Natl. Acad. Sci. USA 84:3555-3559 (1987).
2. Loewenstein-Lichtenstein, Y., M. Schwarz, D. Glick, B. Nørgaard-Pedersen, H. Zakut, and H. Soreq. Genetic predisposition to adverse consequences of anti-cholinesterases in "atypical" BCHE carriers. Nat. Med. 1:1082-1085 (1995).
3. Whittaker, M. Cholinesterases. Karger, Basel (1986).
4. Soreq, H., and H. Zakut. Cholinesterases and Anticholinesterases. Academic Press, San Diego (1993).
5. Sussman, J. L., M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, and I. Silman. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science (Washington D. C.) 253:872-879 (1991).
6. Harel, M., I. Schalk, L. Ehret-Sabatier, F. Bouet, M. Goeldner, C. Hirth, P. Axelsen, I. Silman, and J. L. Sussman. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA 90:9031-9035 (1993).
7. Harel, M., J. L. Sussman, E. Krejci, S. Bon, P. Chanal, J. Massoulie, and I. Silman. Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis. Proc. Natl. Acad. Sci. USA 89:10827-10831 (1992).
8. McGuire, M. C., C. P. Noguiera, C. P. Bartels, H. Lightstone, A. Hajra, A. F. L. van der Spek, O. Lockridge and B. N. La Du. Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant of human serum cholinesterase. Proc. Natl. Acad, Sci. USA 86:953-957 (1989).
9. Neville, L. F., A. Gnatt, R. Padan, S. Seidman, and H. Soreq. Anionic site interactions in human butyrylcholinesterase disrupted by two adjacent single point mutations. J. Biol. Chem. 265:20735-20739 (1990).
10. Neville, L. F., A. Gnatt, Y. Loewenstein, S. Seidman, G. Ehrlich, and H. Soreq. Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE. EMBO J. 11:1641-1649 (1992).
11. Soreq, H., A. Gnatt, Y. Loewenstein, and L. F. Neville, Excavations into the active-site gorge of cholinesterases. Trends Biochem. Sci. 17:353-358 (1992)
12. Taylor, P., and Z. Radic. The cholinesterases: from genes to proteins. Annu. Rev. Pharmacol. Toxicol. 34:281-320 (1994).
13. Schwarz, M., D. Glick, Y. Loewenstein, and H. Soreq. Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons. Pharmacol. Ther. 67:283-322 (1995).
14. Loewenstein, Y., A. Gnatt, L. F. Neville, and H. Soreq. A chimeric human cholinesterase: identification of interaction sites responsible for sensitivity to acetyl- or butyrylcholinesterase-specific ligands. J. Mol. Biol. 234:289-296 (1993).
15. Kieffer, B., M. Goeldner, C. Hirth, R. Aebersold, and J.-Y. Chang. Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammonium. FEBS Lett. 202:91-96 (1986).
16. Kreienkamp, H.-J., C. Weise, R. Raba, A. Aaviksaar, and F. Hucho. Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom. Proc. Natl. Acad. Sci. USA 88:6117-6121 (1991).
17. Shafferman, A., C. Kronman, Y. Flashner, M. Leitner, A. Ordentlich, Y. Gozes, S. Cohen, N. Ariel, D. Barak, M. Harel, I. Silman, J. L. Sussman, and B. Velan. Mutagenesis of human acetylcholinesterase, identification of residues involved in catalytic activity and in polypeptide folding. J. Biol. Chem. 267:17640-17648 (1992).
18. Ordentlich, A., D. Barak, C. Kronman, Y. Flashner, M. Leitner, N. Ariel, S. Cohen, B. Velan, and A. Shafferman. Dissection of the human acetylcholinesterase active center determinants of suhstrate specificity: identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket. J. Biol. Chem. 268:17083-17095 (1993).
19. Barak, D., C. Kronman, A. Ordentlich, N. Ariel, A. Bromberg, D. Marcus, A. Lazar, B. Velan, and A. Shafferman. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core. J. Biol. Chem. 264:6296-6305 (1994).
20. Taylor, P, and S. Lappi. Interaction of fluorescent probes with acetylcholinesterase: the site and specificity of propidium binding. Biochemistry 14:1989-1997 (1975).
21. Shafferman, A., B. Velan, A. Ordentlich, C. Kronman, H. Grosfeld, M. Leitner, Y. Flashner, S. Cohen, D. Barak, and N. Ariel. Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center. EMBO J. 11:3651-3658 (1992).
22. Radic, Z., R. Duran, D. C. Vellom, Y. Li, C. Cervenansky, and P. Taylor. Site of fasciculin interactions with acetylcholinesterase. J. Biol. Chem. 269:11233-11239 (1994).
23. Shafferman, A., A. Ordentlich, D. Barak, C. Kronman, N. Ariel, M. Leitner, Y. Segall, A. Bromberg, S. Reuveny, D. Marcus, T. Bino, A. Lazar, S. Cohen, and B. Velan. Molecular aspects of catalysis and of allosteric regulation of acetylcholinesterases, in Enzymes of the Cholinesterase Family (D. M. Quinn, A. S. Balasubramanian, B. P. Doctor, and P. Taylor, eds. ). Plenum Press, New York, 189-196 (1995).
24. Schwarz, M., Y. Loewenstein-Lichtenstein, D. Glick, J. Liao, B. Norgaard-Pedersen, and H. Soreq. Successive organophosphate inactivation and oxime reactivation reveals distinct responses of recombinant human cholinesterase variants. Mol. Brain Res. 31:101-110 (1995).
25. Gilson, J. K., T. P. Straatsma, J. A. McCammon, D. R. Ripoll, C. H. Faerman, P. H. Axelsen, I. Silman, and J. L. Sussman. Open "back door" in a molecular dynamics simulation of acetylcholinesterase. Science (Washington D. C.) 263:1276-1278 (1994).
26. Gnatt, A., Y. Loewenstein, A. Yaron, M. Schwarz, and H. Soreq. Site-directed mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions. J. Neurochem. 62:749-755 (1994).
27. Hobbiger, R., and A. W. Peck. Hydrolysis of suxamethonium by different types of plasma. Br. J. Pharmacol 37:258-271 (1969).
28. Ollis, D. L., E. Cheah, M. Cygler, B. Dijkstra, F. Frolow, S. M. Franken, M. Harel, S. J. Remington, I. Silman, J. Shrag, J. L. Sussman, K. H. G. Verschueren, and A. Goldman. The α/β hydrolase fold. Protein Eng. 5:197-211 (1992).
29. Fry, P. C. Biological Data Analysis: A Practical Approach. Oxford University Press, Oxford (1993).
30. Bourne, Y., P. Taylor, and P. Marchot. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 83:503-512 (1995).
31. Masson, P., M. T. Froment, C. Bartels, and O. Lockridge. Peripheral anionic site of wild-type and mutant human butyrylcholinesterase, in Enzymes of the Cholinesterase Family (D. M. Quinn, A. S. Balasubramanian, B. P. Doctor, and P. Taylor, eds.). Plenum Press, New York, 230-231 (1995).
32. Radic, Z., N. A. Pickering, D. C. Vellom, S. Camp, and P. Taylor. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 32:12074-12084 (1993).
33. Ordentlich, A., D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman. Contribution of aromatic moieties of tyrosine 133 and of anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. J. Biol. Chem. 270:2083-2091 (1995).
34. Millard, C. B., O. Lockridge, and C. A. Broomfield. Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 34:15925-15933 (1995).
35. Kronman, C., A. Ordentlich, D. Barak, B. Velan, and A. Shafferman. The "back door" hypothesis for product clearance in acetylcholinesterase challenged by site-directed mutagenesis. J. Biol. Chem. 269:27819-27822 (1994).