참고문헌
- Aceto, A., Caccuri, M., Sacchetta, P., Bucciarelli, T., Dragani, B., Rosato, N., Federici, G. and Di IIio, C. (1992) Dissociation and unfolding of Pi-class glutathione transferase. Biochem. J. 285, 241-245.
- Achee, F. M., Chervenka, C. H., Smith, R. A and Yasunobu, K. T. (1968) Amine oxidase. XII. The association and dissociation and number of subunits of beef plasma amine oxidase. Biochemistry 7, 4329-4335. https://doi.org/10.1021/bi00852a027
- Agostinelli, E., De Matteis, G., Sinibaldi, A., Mondovi, B. and Morpurgo, L. (1997) Reactions of the oxidized organic cofactor in copper-depleted bovine serum amine oxidase. Biochem. J. 324, 497-501.
- Bai, J. H., Wang, H. J., Liu, D. S. and Zhou, H. M. (1997) Kinetics of thermal inactivation of lactate dehydrogenase from rabbit muscle. J. Protein Chem. 16, 801-807. https://doi.org/10.1023/A:1026320001709
- Befani, O., Shiozaki, T. S., Turini, P., Gerosa, P. and Mondovi, B. (1995) Inhibition of diamine oxidase activity by metronidazole. Biochem. Biophys. Res. Commun. 212, 589-594. https://doi.org/10.1006/bbrc.1995.2010
- Buffoni, F. (1995) Semicarbazide-sensitive amine oxidases: some biochemical properties and general considerations. Prog. Brain. Res. 106, 323-331. https://doi.org/10.1016/S0079-6123(08)61228-5
- Canals, A., Pous, J., Guasch, A., Benito, A, Ribo, M., Vilanova, M. and Coll, M. (2001) The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization. Structure (Camb) 9, 967-976. https://doi.org/10.1016/S0969-2126(01)00659-1
- Cooper, R. A., Knowles, P. F., Brown, D. E., McGuirl, M. A. and Dooley, D. M. (1992) Evidence for copper and 3,4,6- trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12. Biochem. J. 288, 337-340.
- De Francesco, R., Pastore, A, Vecchio, G. and Cortese, R. (1991) Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB 1. Biochemistry 30, 143-147. https://doi.org/10.1021/bi00215a021
- Engel, J. and Kammerer, R. A. (2000) What are oligomerization domains good for? Matrix Biol. 19, 283-288. https://doi.org/10.1016/S0945-053X(00)00075-5
- Floris, G., Giartosio, A. and Rinaldi, A. (1983) Diamine oxidase from Lens esculenta seedlings: purification and properties. Phytochemistry 22, 1871-1874. https://doi.org/10.1016/0031-9422(83)80004-1
- Frebort, I., Toyama, H., Matsushita, K., and Adachi, O. (1995) Half-site reactivity with p-nitrophenylhydrazine and subunit separation of the dimeric copper-containing amine oxidase from Aspergillus niger. Biochem. Mol. Biol. Int. 36, 1207-1216.
-
Harris, T. K. and Davidson, V. L. (1994) Thermal stability of methanol dehydrogenase is altered by the replacement of enzyme-bound
$Ca^{2+}$ with$Sr^{2+}$ . Biochem. J. 303, 141-145. - Hevel, J. M., Mills, S. A. and Klinman, J. P. (1999) Mutation of a strictly conserved, active-site residue alters substrate specificity and cofactor biogenesis in a copper amine oxidase. Biochemistry 38, 3683-3693. https://doi.org/10.1021/bi982199m
- Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur. S., Maltby, D., Burlingame, A. L. and Klinman, J. P. (1990) A new redox cofactor in eukaryotic enzymes, 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 248, 981-987. https://doi.org/10.1126/science.2111581
- Jones, N. (1990) Transcriptional regulation by dimerization: two sides to an incestuous relationship. Cell 61, 9-11. https://doi.org/10.1016/0092-8674(90)90207-U
- Kumar, V., Dooley, D. M., Freeman, H. C., Guss, J. M., Harvey, I., McGuirl, M. A, Wilce, M. C. and Zubak, V. M. (1996) Crystal structure of a eukaryotic (pea seedling) copper- containing amine oxidase at 2.2 A resolution. Structure 4, 943- 955. https://doi.org/10.1016/S0969-2126(96)00101-3
- Levi, V., Rossi, L. P., Castello, P. R. and Gonzales Flecha, F. L. (2000) Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability. FEBS Letter 483.99-103. https://doi.org/10.1016/S0014-5793(00)02093-7
- Li, R., Klinman, J. P. and Mathews, F. S. (1998) Copper amine oxidase from Hansenula polymorpha, the crystal structure determined at 2.4 A resolution reveals the active conformation. Structure 6, 293-307. https://doi.org/10.1016/S0969-2126(98)00033-1
- Lyles, G. A (1995) Substrate-specificity of mammalian tissue- bound semicarbazide-sensitive amine oxidase. Prog. Brain. Res. 106, 293-303. https://doi.org/10.1016/S0079-6123(08)61226-1
- Lyles, G. A. (1996) Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int. J. Biochem. Cell Biol. 28, 259-274. https://doi.org/10.1016/1357-2725(95)00130-1
- Maccarrone, M., Rossi, A., Avigliano, L. and Finazzi Agro, A. (1991) Activity and expression of diamine oxidase in lentil seedlings under different growth conditions. Plant Science 79, 51-55. https://doi.org/10.1016/0168-9452(91)90068-J
- Massey, J. B. and Churchich, J. E. (1979) Nanosecond spectroscopy of dimeric enzyme: plasma amine oxidase. Biophys. Chem. 9, 157-162. https://doi.org/10.1016/0301-4622(79)87010-6
- Medda, R., Padiglia, A., Lorrai, A., Finazzi Agro, A. and Floris, G. (2000) Arginine and ornithine oxidation catalyzed by lentil seedling copper-amine oxidase. J. Protein Chem. 19,51-57. https://doi.org/10.1023/A:1007094909853
- Moosavi-Nejad, S. Z., Rezaei-Tavirani, M., Padiglia, A., Floris, G. and Moosavi-Movahedi, A. A. (2001) Amine oxidase from lentil seedlings: energetic domains and effect of temperature on activity. J. Protein Chem. 20, 405-411. https://doi.org/10.1023/A:1012284821503
- Neet, K. E. and Timm, D. E. (1994) Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci. 3, 2167-2174. https://doi.org/10.1002/pro.5560031202
- Padiglia, A, Medda, R., Bellelli, A., Agostinelli, E., Morpurgo, L., Mondovi, B., Finazzi Agro, A. and Floris, G. (2001) The reductive and oxidative half-reactions and the role of copper ion in plant and mammalian copper-amine oxidases. Eur. J. Inorg. Chem. 35-42.
- Padiglia, A., Medda, R., Pedersen, J. Z., Lorrai, A., Pee, P., Frebor, I. and Floris, G. (1998) Inhibitors of plant copper amine oxidases. J. Enzyme Inhibition 13, 311-325. https://doi.org/10.3109/14756369809021478
- Poltorak, O. M., Chukhray, E. S. and Torshin, I. Y. (1998) Dissociative thermal inactivation, stability and activity of oligomeric enzymes. Biochemistry (Moscow) 63, 303-311.
- Sacchetta, P., Aceto, A, Bucciarelli, T., Dragani, B., Santarone, S., Allocati, N. and Di Ilio, C. (1993) Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Role of the dimeric structure on the flexibility of the active site. Eur. J. Biochem. 215, 741-745. https://doi.org/10.1111/j.1432-1033.1993.tb18087.x
- Sanchez del Pino, M. M. and Fersht, A. R. (1997) Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol- phosphate synthase. Biochemistry 36, 5560-5565. https://doi.org/10.1021/bi963133z
- Segel, I. H. (1995) Enzyme Kinetics, pp. 926-942, John Wiley & Sons, Inc., New York.
- Sriprapundh, D., Vieille, C. and Zeikus, J. G. (2000) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis. Protein Eng. 13, 259-265. https://doi.org/10.1093/protein/13.4.259
- Steif, C., Weber, P., Hinz, H., Flossdorf, J., Cesareni, G. and Kokkinidis, M. (1993) Subunit interactions provide a significant contribution to the stability of the dimeric four-A-Helical- bundle protein ROP. Biochemistry 32, 3867-3876. https://doi.org/10.1021/bi00066a005
- Wells, J. A. (1994) Structural and functional basis for hormone binding and receptor oligomerization. Curr. Opin. Cell Biol. 6, 163-173. https://doi.org/10.1016/0955-0674(94)90132-5
- Wilce, M. C., Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., McIntire, W. S., Ruggiero, C. E., Tanizawa, K. and Yamaguchi, H. (1997) Crystal structures of the copper- containing amine oxidase from Arthrobacter globiformis in the holo and apo forms, implications for the biogenesis of topaquinone. Biochemistry 36, 16116-16133. https://doi.org/10.1021/bi971797i
- Zaitzeva, E. A, Chukrai, E. S. and Poltorak, O. M. (1996) Thermostability of yeast hexokinase and yeast glucose-6- phosphate dehydrogenase. Appl. Biochem. Biotech. 61,67-74. https://doi.org/10.1007/BF02785689
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