Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates

Biochemical Journal

Volumn 371, Issue 2, 2003, Pages 549-556

  Di Paolo, Maria Luisa ^a   Stevanato, Roberto ^b   Corazza, Alessandra ^c   Vianello, Fabio ^a   Lunelli, Lorenzo ^d   Scarpa, Marina ^d   Rigo, Adelio ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b CA' FOSCARI UNIVERSITY OF VENICE   (Italy)

^c UNIVERSITY OF UDINE   (Italy)

^d UNIVERSITY OF TRENTO   (Italy)

Author keywords

Amine oxidase; Electrostatic interactions; Enzyme function; Hydrophobic interactions; Ionic strength; Polyamine

Indexed keywords

AMINES; AMINO ACIDS; ELECTROSTATICS; HYDROPHOBICITY; IONIC STRENGTH; PH EFFECTS; SUBSTRATES;

POLYAMINES;

ENZYMES;

AMINE OXIDASE (FLAVIN CONTAINING); POLYAMINE;

ARTICLE; CATALYSIS; CATTLE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; HYDROPHOBICITY; IONIC STRENGTH; NONHUMAN; PH; PRIORITY JOURNAL; STEADY STATE;

AMINE OXIDASE (COPPER-CONTAINING); ANIMALS; BINDING SITES; CATTLE; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, THEORETICAL; SUBSTRATE SPECIFICITY;

BOS TAURUS; BOVINAE;

EID: 0037626151     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021055     Document Type: Article

References (47)

1. Petterson, G. (1985) Plasma amine oxidase. In Structure and Function of Amine Oxidases (Mondovi, B., ed.), pp. 105-120, CRC Press, Boca Raton, FL
2. Knowles, P. F. and Dooley, D. M. (1994) Amine oxidases. In Metal Ions in Biological Systems (Sigel, H. and Sigel, A., eds.), vol. 30, pp. 361-403, Dekker, New York
3. Klinman, J. P. and Mu, D. (1994) Quinoenzymes in biology. Annu. Rev. Biochem. 63, 299-344
4. Padiglia, A., Medda, R., Bellelli, A., Agostinelli, E., Morpurgo, L., Mondovì, B., Finazzi-Agrò, A. and Floris, G. (2001) The reductive and oxidative half-reactions and the role of copper ions in plant and mammalian copper-amine oxidases. Eur. J. Inorg. Chem. 1, 35-42
5. Farnun, M., Palcic, M. and Klinman, J. P. (1986) pH dependence of deuterium isotopic effects and tritium exchange in the bovine plasma amine oxidase reaction: a role for single base catalysis in amine oxidation and imine exchange. Biochemistry 25, 1898-1904
6. Hartmann, C., Brozovic, P. and Klinman, J. P. (1993) Spectroscopic detection of chemical intermediates in the reaction of para-substituted benzylamine with bovine serum amine oxidase. Biochemistry 32, 2234-2241
7. Bellelli, A., Finazzi-Agrò, A., Floris, G. and Brunori, M. (1991) On the mechanism and rate of substrate oxidation by amine oxidase from lentil seedlings. J. Biol. Chem. 266, 20654-20657
8. Medda, R., Padiglia, A., Pedersen, J. Z., Rotilio, G., Finazzi-Agrò, A. and Floris, G. (1995) The reaction mechanism of copper amine oxidase: detection of intermediates by the use of substrates and inhibitors. Biochemistry 34, 16375-16381
9. Medda, R., Padiglia, A., Bellelli, A., Sarti, P., Santanche, S., Finazzi-Agrò, A. and Floris, G. (1998) Intermediates in the catalytic cycle of lentil (Lens esculenta) seedling copper-containing amine oxidase. Biochem. J. 332, 431-437
10. Su, Q. and Klinman, J. P. (1998) Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase. Biochemistry 37, 12514-12525
11. Bellelli, A., Morpurgo, L., Mondoì, B. and Agostinelli, E. (2000) The oxidation and reduction reactions of bovine serum amine oxidase. A kinetic study. Eur. J. Biochem. 267, 3264-3269
12. Bisby, R. H., Johnson, A. S. and Parker, A. W. (2000) Radicals from one-electron oxidation of 4-aminoresorcinol: model of the active site radical intermediate in copper amine oxidase. J. Phys. Chem. 104, 5832-5839
13. De Vries, S., van Spanning, R. J. M. and Steinebach, V. (2000) A spectroscopic and kinetic study of Escherichia coli amine oxidase. J. Mol. Catal. B Enzymatic 8, 111-120
14. Bardsley, W. G., Hill, C. M. and Lobley, R. W. (1970) A reinvestigation of the substrate specificity of pig kidney diamine oxidase. Biochem. J. 117, 169-176
15. Bardsley, W. G. and Ashford, J. S. (1972) Inhibition of pig kidney diamine oxidase by substrate analogues. Biochem. J. 128, 253-263
16. Palcic, M. M. and Klinman, J. P. (1983) Isotopic probes yield microscopic constants: separation of binding energy from catalytic efficiency in the bovine plasma amine oxidase reaction. Biochemistry 22, 5957-5966
17. Hartmann, C. and Klinman, J. P. (1991) Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism. Biochemistry 30, 4605-4611
18. Equi, M. A., Cooper, A. and Robins, D. J. (1992) Chain-length dependence of oxidation of α-ω-diamines by diamine oxidase. J. Chem. Res. 8, 94-95
19. Stevanato, R., Mondovì, B., Befani, O., Scarpa, M. and Rigo, A. (1994) Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase. Biochem. J. 299, 317-320
20. Di Paolo, M. L., Vianello, F., Stevanato, R. and Rigo, A. (1995) Kinetic characterization of soybean seedling amine oxidase. Arch. Biochem. Biophys. 323, 329-334
21. Luhova, L., Slavik, L., Frebort, I., Sebela, M., Zajoncova, L. and Pec, P. (1996) Comparison of kinetic properties between plant and fungal amine oxidases. J. Enzyme Inhib. 10, 251-262
22. Cai, D. Y., Dove, J., Nakamura, N., SandersLoeher, J. and Klinman, J. P. (1997) Mechanism-based inactivation of a yeast methylamine oxidase mutant: implication for the functional role of the consensus sequence surrounding topaquinone. Biochemistry 36, 11472-11478
23. McGuirl, M. A. and Dooley, D. M. (1999) Copper-containing oxidases. Corr. Opin. Chem. Biol. 3, 138-144
24. Matsuzaki, R. and Tanizawa, K. (1998) Exploring a channel to the active site of copper/topaquinone-containig phenylethylamine oxidase by chemical modification and site-specific mutagenesis. Biochemistry 37, 13947-13957
25. Wilmot, C. M., Murray, J. M., Alton, G., Parsons, M. R., Convery, M. A., Blakeley, V., Corner, A. S., Palcic, M. M., Knowles, P. F., McPherson, M. J. and Phillips, S. E. V. (1997) Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half reaction. Biochemistry 36, 1608-1620
26. Vianello, F., Di Paolo, M. L., Stevanato, R. and Rigo, A. (1992) Isolation of amine oxidase from bovine plasma by a two-step procedure. Protein Expression Purif. 3, 362-367
27. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
28. Di Paolo, M. L., Scarpa, M. and Rigo, A. (1994) A sensitive spectrophotometry-based method for the determination of the rate of hydrogen peroxide generation in biological systems. J. Biochem. Biophys. Methods 28, 205-214
29. Oi, S., Inamasu, M. and Yasunobu, K. T. (1970) Mechanistic studies of beef plasma amine oxidase. Biochemistry 9, 3378-3383
30. Weiner, S. J., Kollmann, P. A., Case, D. A., Singh, U. C., Ghio, C., Alagona, G., Profeta, Jr, S. and Weiner, P. (1984) A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106, 765-784
31. Klinman, J. P. (1996) Mechanism whereby mononuclear copper proteins functionalize organic substrates. Chem. Rev. 96, 2541-2561
32. Davis, M. E., Madura, J. D., Luty, B. A. and McCammon, J. A. (1991) Electrostatics and diffusion of molecules in solution: simulation with the University of Houston Brownian Dynamics program. Comput. Phys. Commun. 62, 187-197
33. 13C-NMR chemical shift assignment of spermidine, spermine and homologs. Biophys. Chem. 17, 67-74
34. Weast, R. C. (1968/1969) CRC Handbook of Chemistry and Physics, 49th edn, pp. D87-D89, The Chemical Rubber Co., Cleveland, OH
35. Tipton, K. F. and Dixon, H. B. F. (1979) Effects of pH on enzymes. Methods Enzymol. 63, 183-233
36. Koudelka, G. B., Hansen, F. B. and Ettinger, M. J. (1985) Solvent isotope effects and the pH dependence of laccase activity under steady-state conditions. J. Biol. Chem. 260, 15561-15565
37. Fersth, A. (1985) Enzyme Structure and Mechanism, 2nd edn, W. H. Freeman and Co., New York
38. Di Paolo, M. L., Scarpa, M., Corazza, A., Stevanato, R. and Rigo, A. (2002) Binding of cations of group IA and IIA to bovine serum amine oxidase. Effect on the activity. Biophys. J. 83, 2231-2239
39. Costa, M. T., Rotilio, G., Finazzi Agrò, A., Valligiani, M. P. and Mondovì, B. (1971) On the active site of diamine oxidase: kinetic study. Arch. Biochem. Biophys. 147, 8-13
40. Leidler, K. and Bunting, P. (1973) The Chemical Kinetics of Enzyme Action, 2nd edn, pp. 52-53, Clarendon Press, Oxford
41. Kuchar, J. A. and Dooley, D. M. (2001) Cloning, sequence analysis, and characterization of the "Lysil Oxidase" from Pichia pastoris. J. Inorg. Biochem. 83, 193-204
42. Schwartz, B., Green, E. L., Sanders-Loehr, J. and Klinman, J. P. (1998) Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast. Biochemistry 37, 16591-16600
43. Plastino, J., Green, L. E., Sanders-Loehr, J. and Klinman, J. P. (1999) An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Harsenula polymorpha. Biochemistry 38, 8204-8216
44. Green, E. L., Nakamura, N., Dooley, D. M., Klinman, J. P. and Sanders-Loehr, J. (2002) Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases. Biochemistry 41, 687-696
45. Desser, H., Kleinberge, G. and Klaring, J. (1981) Plasma polyamine levels in patients with liver insufficiency. J. Clin. Chem. Clin. Biochem. 19, 159-164
46. Cohen, S. S. (1998) A Guide to the Polyamines, Oxford University Press, Oxford
47. Bachrach, U. (1985) Copper amine oxidases and amines as regulators of cellular processes. In Structure and Function of Amine Oxidases (Mondovi, B., ed.), pp. 5-20, CRC Press, Boca Raton, FL