Purification of beef kidney d-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1431, Issue 1, 1999, Pages 212-222

  Negri, Armando ^a   Tedeschi, Gabriella ^a   Ceciliani, Fabrizio ^a   Ronchi, Severino ^a  

^a UNIVERSITY OF MILAN   (Italy)

Author keywords

D Amino acid; D Aspartate; D Aspartate oxidase; Flavoprotein; N Methyl D aspartate; Redox potential

Indexed keywords

DEXTRO AMINO ACID; DEXTRO ASPARTATE OXIDASE; DEXTRO ASPARTIC ACID; EXCITATORY AMINO ACID RECEPTOR; FLAVOPROTEIN; N METHYL DEXTRO ASPARTIC ACID; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; COW; ENZYME CONFORMATION; ENZYME PURIFICATION; ESCHERICHIA COLI; KIDNEY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

AMINO ACID OXIDOREDUCTASES; ANIMALS; APOENZYMES; CATTLE; D-ASPARTATE OXIDASE; ESCHERICHIA COLI; EXCITATORY AMINO ACID AGONISTS; EXCITATORY AMINO ACID ANTAGONISTS; GENE EXPRESSION; KIDNEY; OXIDATION-REDUCTION; SUBSTRATE SPECIFICITY;

EID: 0032913359     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00027-8     Document Type: Article

References (39)

1. Corrigan J.J. D-Amino acids in animals. Science. 164:1969;142-149.
2. Dunlop D.S., Neidle A., Hale D.Mc., Dunlop D.M., Lajtha A. The presence of free D-aspartic acid in rodents and man. Biochem. Biophys. Res. Commun. 141:1986;27-32.
3. Bada J.L. In vivo racemization in mammalian proteins. Methods Enzymol. 106:1984;98-116.
4. Schell M.J., Cooper O.B., Snyder S.H. D-Aspartate localizations imply neuronal and neuroendocrine roles. Proc. Natl. Acad. Sci. USA. 94:1997;2013-2018.
5. Lee J.-A., Homma H., Sakai K., Fukushima T., Santa T., Tashiro K., Iwatsubo T., Yoshikawa M., Imai K. Immunohistochemical localization of D-aspartate in rat pineal gland. Biochem. Biophys. Res. Commun. 231:1997;505-508.
6. Sakai K., Homma H., Lee J.-A., Fukushima T., Santa T., Tashiro K., Iwatsubo T., Imai K. D-Aspartic acid localization during postnatal development of rat adrenal gland. Biochem. Biophys. Res. Commun. 235:1997;433-436.
7. Kera Y., Aoyama H., Matsumura H., Hasegawa A., Nagasaki H., Yamada R.-h. Presence of free D-glutamate and D-aspartate in rat tissues. Biochim. Biophys. Acta. 1243:1995;282-286.
8. Hashimoto A., Nishikawa T., Oka T., Hayashi T., Takahashi K. Widespread distribution of free D-aspartate in rat periphery. FEBS Lett. 331:1993;4-8.
9. Fisher G.H., D'Aniello A., Vetere A., Cusano G.P., Chàvez M., Petrucelli L. Quantification of D-aspartate in normal and Alzheimer brains. Neurosci. Lett. 143:1992;215-218.
10. Nagata Y., Akino T., Ohno K., Kataoka Y., Ueda T., Sakurai T., Shiroshita K.-I., Yasuda T. Free D-amino acids in human plasma in relation to senescence and renal diseases. Clin. Sci. 73:1987;105-108.
11. Man E.H. Dietary D-amino acids. Annu. Rev. Nutr. 7:1987;209-225.
12. Watkins J.C., Olverman H.J. Agonists and antagonists for excitatory amino acids receptors. Trends Neurosci. 10:1987;265-272.
13. Meadows K.N., Petrusz P., Brewer F., Hicks T.P. Antibodies to glutamate, aspartate and glycyl-D-aspartate reversibly suppress stimulus-evoked, extracellularly recorded responses in slices of rat neocortex. Neurosci. Lett. 215:1996;141-144.
14. Negri A., Massey V., Williams C.H. Jr. D-Aspartate oxidase from beef kidney. J. Biol. Chem. 262:1987;10026-10034.
15. Negri A., Massey V., Williams C.H. Jr., Schopfer L.M. The kinetic mechanism of beef kidney D-aspartate oxidase. J. Biol. Chem. 263:1988;13557-13563.
16. Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S. The primary structure of the flavoenzyme D-aspartate oxidase from beef kidney. J. Biol. Chem. 267:1992;11865-11871.
17. Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., Tenchini M.L., Ronchi S. cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex. Biochem. J. 322:1997;729-735.
18. Setoyama C., Miura R. Structural and functional characterization of the human brain D-aspartate oxidase. J. Biochem. 121:1997;798-803.
19. Massey V., Hemmerich P. Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Biochemistry. 17:1978;9-17.
20. V. Massey, A simple method for the determination of redox potentials, in: B. Curti, S. Ronchi, G. Zanetti (Eds.), Flavins and Flavoproteins 1990, Walter de Gruyter, Berlin, 1991, pp. 59-66.
21. Minnaert K. Measurement of the equilibrium constant of the reaction between cytochrome c and cytochrome a. Biochim. Biophys. Acta. 110:1965;42-56.
22. Laemmli U.K. Cleavage of the structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
23. Massey V., Muller F., Feldberg R., Schuman M., Sullivan P.A., Howell L.G., Mayhew S.G., Matthews R.G., Foust G.P. The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity. J. Biol. Chem. 244:1969;3999-4006.
24. W.N. Clark, Oxidation Reduction Potentials of Organic Systems, Williams and Wilkins, Baltimore, MD, 1960.
25. Kurzban G.P., Howarth J., Palmer G., Strobel H.W. NADPH-cytochrome P-450 reductase. Physical properties and redox behaviour in the absence of the FAD moiety. J. Biol. Chem. 265:1990;12272-12279.
26. Einarsdottir G.H., Stankovich M.T., Tu S.-C. Studies of electron-transfer properties of salicylate hydroxylase from Pseudomonas cepacia and effects of salicylate and benzoate binding. Biochemistry. 27:1988;3277-3285.
27. Dixon M., Kenworthy P. D-Aspartate oxidase of kidney. Biochim. Biophys. Acta. 146:1967;54-76.
28. Tedeschi G., Negri A., Ceciliani F., Ronchi S., Vetere A., D'Aniello G., D'Aniello A. Properties of the flavoenzyme D-aspartate oxidase from Octopus vulgaris. Biochim. Biophys. Acta. 1207:1994;217-222.
29. Rinaldi A., Pellegrino M., Crifò C., de Marco C. Oxidation of meso-diaminosuccinic acid, a possible natural substrate for D-aspartate oxidase. Eur. J. Biochem. 117:1981;635-638.
30. B. Curti, S. Ronchi, M.P. Simonetta, D- and L- amino acid oxidases, in: F. Muller (Ed.), Chemistry and Biochemistry of Flavoenzymes, vol. III, CRC Press, Boca Raton, FL, 1991, pp. 69.S-94.S.
31. Van den Berghe-Snorek, M.T. Stankovich, Thermodynamic control of D-amino acid oxidase by benzoate binding, J. Biol. Chem. 260 (1985) 3373-3379.
32. M.T. Stankovich, Redox properties of flavins and flavoproteins, in: F. Muller (Ed.), Chemistry and Biochemistry of Flavoenzymes, vol. I, CRC Press, Boca Raton, FL, 1991, pp. 401-425.
33. Tedeschi G., Zetta L., Negri A., Mortarino M., Ceciliani F., Ronchi S. Redox potentials and quinone reductase activity of L-aspartate oxidase from E. coli. Biochemistry. 36:1997;16221-16230.
34. Mortarino M., Negri A., Tedeschi G., Simonic T., Duga S., Gassen G.H., Ronchi S. L-Aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur. J. Biochem. 239:1996;418-426.
35. Tedeschi G., Negri A., Mortarino M., Ceciliani F., Simonic T., Faotto L., Ronchi S. L-Aspartate oxidase from Escherichia coli. II. Interaction with C4-dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity. Eur. J. Biochem. 239:1996;427-433.
36. D'Aniello A., D'Onofrio G., Pischetola M., D'Aniello G., Vetere A., Petrucelli L., Fisher G.H. Biological role of D-amino acid oxidase and D-aspartate oxidase. J. Biol. Chem. 268:1993;26941-26949.
37. Foster J.W., Moat A.G. Nicotinamide adenine nucleotide biosynthesis and Pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev. 44:1980;83-105.
38. Sato M., Inoue F., Kanno N., Sato Y. The occurrence of N-methyl-D-aspartic acid in muscle extracts of the blood shell, Scapharca broughtonii. Biochem. J. 241:1987;309-311.
39. Benesi H.A., Hildebrand J.H. A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. J. Am. Chem. Soc. 71:1949;2703-2707.