Purification and Characterization of Methylamine Oxidase Induced in Aspergillus niger AKU 3302

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 1, 1999, Pages 125-134

  Frébort, Ivo ^a,b   Matsushita, Kazunobu ^a   Toyama, Hirohide ^a   Lemr, Karel ^a,b   Yamada, Mamoru ^a   Adachi, Osao ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

^b PALACKÝ UNIVERSITY   (Czech Republic)

Author keywords

Aspergillus niger; Copper topa quinone; Methylamine oxidase; Quinoprotein amine oxidase

Indexed keywords

AMINE DEHYDROGENASE; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS NIGER; BIOSYNTHESIS; DIMERIZATION; ENZYME INDUCTION; ENZYME SPECIFICITY; ENZYMOLOGY; FUNGAL GENE; GENETICS; ISOLATION AND PURIFICATION; KINETICS; MOLECULAR WEIGHT; PH; PROTEIN CONFORMATION; SPECTROPHOTOMETRY;

AMINO ACID SEQUENCE; ASPERGILLUS NIGER; DIMERIZATION; ENZYME INDUCTION; GENES, FUNGAL; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PROTEIN CONFORMATION; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY;

EID: 0032611774     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.125     Document Type: Article

References (43)

1. Mclntire, W. S. and Hartmann, C., Copper-containing amine oxidases. In “Principles and Applications of Quinoproteins”, ed. Davidson, V. L., Marcel Dekker Inc., New York, pp. 97-171 (1992).
2. Tabor, C. W., Tabor, H., and Rosenthal, S. M., Purification of amine oxidase from beef plasma. J. Biol. Chem., 208, 645-661 (1954).
3. Klinman, J. P., New quinocofactors in eukaryotes. J. Biol. Chem., 271, 27189-27192 (1996).
4. Mure, M. and Tanizawa, K., Chemical and biochemical characteristics of topa quinone. Biosci. Biolechnol. Biochem., 61, 410-417 (1997).
5. Frebort, I. and Adachi, O., Copper/quinone-containing amine oxidases, an exciting class of ubiquitous enzymes. J. Ferment. Bioeng., 80, 625-632 (1995).
6. Parsons, M. R., Convery, M. A., Wilmot, C. M., Yadav, K. D. S., Blakeley, V., Corner, A. S., Phillips, S. E. V., McPherson, M. J., and Knowles, P. F., Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure, 3, 1171-1184 (1995).
7. Kumar, V., Dooley, D. M., Freeman, H. C., Guss, J. M., Harvey, I., McGuirl, M. A., Wilce, M. C. J., and Zubak, V. M., Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution. Structure, 4, 943-955 (1996).
8. Wilce, M. C., Dooly, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., McIntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H., Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemisiry, 36, 16116-16133 (1997).
9. Yamada, H., Adachi, O., and Ogata, K., Amine oxidases of microorganisms. Part I. Formation of amine oxidase by fungi., Agric. Biol. Chem., 29, 117-123 (1965).
10. Adachi, O. and Yamada, H., Amine oxidases of microorganisms. Part VIII. Purification and properties of amine oxidase from Fusarium culmorum. Mem. Res. Inst. Food Sci., Kyoto Univ., 31, 10-18 (1970).
11. Yamada, H., Adachi, O., and Ogata, K., Amine oxidases of microorganisms. Part II. Purification and crystallization of amine oxidase of Aspergillus niger. Agric. Biol. Chem., 29, 649-654 (1965).
12. Yamada, H., Adachi, O., and Ogata, K., Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger. Agric. Biol. Chem., 29, 864-869 (1965).
13. Yamada, H., Adachi, O., and Ogata, K., Amine oxidases of microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger. Agric. Biol. Chem., 29, 912-917 (1965).
14. Frébort, I., Tamaki, H., Ishida, H., Peč, P., Luhová, L., Tsuno, H., Halata, M., Asano, Y., Kato, Y., Matsushita, K., Toyama, H., Kumagai, H., and Adachi, O., Two distinct quinoprotein amine oxidases are induced by n-butylamine in the mycelia of Aspergillus niger. Purification, characterization, cDNA cloning and sequencing. Eur. J. Biochem., 237, 225-265 (1996).
15. Schilling, B. and Lerch, K., Amine oxidases from Aspergillus niger, Identification of a novel flavin-dependent enzyme. Biochim. Biophys. Acta, 1243, 529-537 (1995).
16. Isobe, K., Tani, Y., and Yamada, H., Crystallization and characterization of agmatine oxidase from Penicillium chrysogenum. Agric. Biol. Chem., 46, 1353-1359 (1982).
17. Frébort, I., Matsushita, K., and Adachi, O., The fungus Gib-berella fujikuroi produces a copper/topaquinone-containing amine oxidase when induced by n-butylamine. Biochem. Mol. Biol. Int., 41, 11-23 (1997).
18. Yamada, H., Kumagai, H., Uwajima, T., and Ogata, K., Trimethylamine metabolism. Part I. Monomethylamine oxidase. Mem. Res. Inst. Food Sci., Kyoto Univ., 27, 1-14 (1966).
19. Isobe, K., Tani, Y., and Yamada, H., Crystallization and characterization of polyamine oxidase from Penicillium chrysogenum. Agric. Biol. Chem., 44, 2651-2658 (1980).
20. Isobe, K., Tani, Y., and Yamada, H., Crystallization and characterization of polyamine oxidase from Aspergillus terreus. Agric. Biol. Chem., 44, 2749-2751 (1980).
21. Kobayashi, Y. and Horikoshi, K., Purification and characterization of extracellular polyamine oxidase produced by Penicillium sp. no. PO-1. Biochim. Biophys. Acta, 705, 133-138 (1982).
22. + aldehyde dehydrogenases in amine degradation by filamentous fungi. J. Ferment. Bioeng., 84, 200-212 (1997).
23. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
24. Frébort, I., Haviger, A., and Pec, P., Employment of guaiacol for the determination of activities of enzymes generating hydrogen peroxide and for the determination of glucose in blood and urine. Biologia (Bratislava), 44, 729-737 (1989).
25. Houen, G. and Leonardsen, L., A specific peroxidase-coupled activity stain for diamine oxidases. Anal. Biochem., 204, 296-299 (1992).
26. Paz, M. A., Fluckiger, R., Boak, A., Kagan, H. M., and Gallop, P.M., Specific detection of quinoproteins by redox-cycling staining. J. Biol. Chem., 266, 689-692 (1991).
27. Chervenka, C. H., Determination of sedimentation rates. In “A Manual of Methods for the Analytical Ultracentrifuge,” ed. Chervenka, C. H., Spinco Division of Beckman Instruments Inc., Palo Alto, California, pp. 23-37 (1970).
28. Chervenka, C. H., Determination of molecular weights. In “A Manual of Methods for the Analytical Ultracentrifuge,” ed. Chervenka, C. H., Spinco Division of Beckman Instruments Inc., Palo Alto, California, pp. 39-67 (1970).
29. Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J., and Rutter, W. J., Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry, 18, 5294-5299 (1979).
30. Alwine, J. C., Kemp, D. J., and Stark, G. R., Method for detection of specific RNAs in agarose gels by transfer to diazoben-zyloxymethyl-paper and hybridization with DNA probes. Proc. Natl. Sci. U.S.A., 74, 5350-5354 (1977).
31. Radloff, R., Bauer, W., and Vinograd, J., A dye-buoyant-den-sity method for the detection and isolation of closed circular duplex DNA: The closed circular DNA in HeLa cells. Proc. Natl. Acad. Sci. U.S.A., 57, 1514-1521 (1967).
32. Maniatis, T., Jeffrey, A., and van de Sande, FI., Chain length determination of small double-stranded and single stranded DNA molecules by polyacrylamide gel electrophoresis. Biochemistry, 14, 3787-3794 (1975).
33. van Iersel, J., van der Meer, R. A., and Duine, J. A., Methyla-mine oxidase from Arthrobacter PI. A bacterial copper-quinoprotein amine oxidase. Eur. J. Biochem., 161, 415-419 (1986).
34. Haywood, G. W. and Large, P. J., Microbial oxidation of amines. Distribution, purification and properties of two prim-ary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. Biochem. J., 199, 187-201 (1981).
35. Green, J., Haywood, G. W., and Large, P. J., Serological differences between the multiple amine oxidases of yeast and comparison of the specificities of the purified enzymes from Candida uti-lis and Pichiapastoris. Biochem. J., 211, 481-493 (1983).
36. Zwart, K. B. and Harder, W., Regulation of metabolism of some alkylated amines in the yeast Candida utilis and Hansenula polymorpha. J. Gen. Microbiol., 129, 3157-3169 (1983).
37. Cai, D. and Klinman, J. P., Copper amine oxidase: Heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae. Biochemistry, 33, 7647-7653 (1994).
38. Cai, D. and Klinman, J. P., Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J. Biol. Chem., 269, 32039-32042 (1994).
39. Cai, D., Williams, N. K., and Klinman, J. P., Recent report of Hansenula copper amine oxidase. J. Biol. Chem., 272, 19277-19281 (1997).
40. Shinagawa, E., Matsushita, K., Nakashima, K., Adachi, O., and Ameyama, M., Crystallization and properties of amine de-hydrogense from Pseudomonas sp. Agric. Biol. Chem., 52, 2255-2263 (1988).
41. Adachi, O., Kubota, T., Hacisalihoglu, A., Toyama, H., Shinagawa, E., Duine, J. A., and Matsushita, K., Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Biosci. Biotechnol. Biochem., 62, 469-478 (1998).
42. Palcic, M. M. and Janes, S. M., Spectrophotometric detection of topa quinone, In “Methods in Enzymology”, ed. Klinman, J. P., Vol. 258, Academic press, Inc., New York, pp. 34-38 (1995).
43. Mure, M. and Klinman, J. P., Model studies of topa quinone: synthesis and characterization of topa quinone derivatives, In “Methods in Enzymology”, ed. Klinman, J. P., Vol. 258, Academic Press, Inc., New York, pp. 39-52 (1995).