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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 5
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Original Articles

Purification and Characterization of Fumarase from Corynebacterium glutamicum

Tomoko GENDABiological Institute, Faculty of Education, Yamaguchi University
,
Shoji WATABEBasic Laboratory Science, Faculty of Health Sciences, Yamaguchi University School of Medicine
&
Hachiro OZAKIBiological Institute, Faculty of Education, Yamaguchi University
Pages 1102-1109 | Received 02 Aug 2005, Accepted 10 Dec 2005, Published online: 22 May 2014

  • 1) Bock, R. M., and Alberty, R. A., Studies of the enzyme fumarase. I. Kinetics and equilibrium. J. Am. Chem. Soc., 75, 1921–1925 (1953).
  • 2) Massey, V., and Alberty, R. A., Ionization constants of fumarase. Biochim. Biophys. Acta, 13, 354–359 (1954).
  • 3) Alberty, R. A., Massey, V., Frieden, C., and Fuhlbrigge, A. R., Studies of the enzyme fumarase. III. The dependence of the kinetic constants at 25 °C upon the concentration and pH of phosphate buffers. J. Am. Chem. Soc., 76, 2485–2493 (1954).
  • 4) Kanarek, L., and Hill, R. L., The preparation and characterization of fumarase from swine heart muscle. J. Biol. Chem., 239, 4202–4206 (1964).
  • 5) Robinson, G. W., Bradshaw, R. A., Kanarek, L., and Hill, R. L., The thiol groups of fumarase. J. Biol. Chem., 242, 2709–2718 (1967).
  • 6) Teipel, J. W., Hass, G. M., and Hill, R. L., The substrate specificity of fumarase. J. Biol. Chem., 243, 5684–5694 (1968).
  • 7) Kobayashi, K., Yamanishi, T., and Tuboi, S., Physicochemical, catalytic, and immunochemical properties of fumarases crystallized separately from mitochondrial and cytosolic fractions of rat liver. J. Biochem., 89, 1923–1931 (1981).
  • 8) Kobayashi, K., and Tuboi, S., End group analysis of the cytosolic and mitochondrial fumarases from rat liver. J. Biochem., 94, 707–713 (1983).
  • 9) Woods, S. A., Schwartzbach, S. D., and Guest, J. R., Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta, 954, 14–26 (1988).
  • 10) Yumoto, N., and Tokushige, M., Characterization of multiple fumarase proteins in Escherichia coli. Biochem. Biophys. Res. Commun., 153, 1236–1243 (1988).
  • 11) Ueda, Y., Yumoto, N., Tokushige, M., Fukui, K., and Ohya-Nishiguchi, H., Purification and characterization of two types of fumarase from Escherichia coli. J. Biochem., 109, 728–733 (1991).
  • 12) Weaver, T. M., Levitt, D. G., and Banaszak, L. J., Purification and crystallization of fumarase C from Escherichia coli. J. Mol. Biol., 231, 141–144 (1993).
  • 13) Shiio, I., Ozaki, H., and Ujigawa, K., Regulation of citrate synthase in Brevibacterium flavum, a glutamate-producing bacterium. J. Biochem., 82, 395–405 (1977).
  • 14) Shiio, I., and Ozaki, H., Concerted inhibition of isocitrate dehydrogenase by glyoxylate plus oxalacetate. J. Biochem., 64, 45–53 (1968).
  • 15) Ozaki, H., and Shiio, I., Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. I. Inhibition of isocitrate lyase and isocitrate dehydrogenase by organic acids related to the TCA and glyoxylate cycles. J. Biochem., 64, 355–363 (1968).
  • 16) Shiio, I., and Ujigawa-Takeda, K., Presence and regulation of α-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium, Brevibacterium flavum. Agric. Biol. Chem., 44, 1897–1904 (1980).
  • 17) Genda, T., Nakamatsu, T., and Ozaki, H., Purification and characterization of malate dehydrogenase from Corynebacterium glutamicum. J. Biosci. Bioeng., 95, 562–566 (2003).
  • 18) Molenaar, D., van der Rest, M. E., and Petrovic, S., Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum. Eur. J. Biochem., 254, 395–403 (1998).
  • 19) Molenaar, D., van der Rest, M. E., Drysch, A., and Yucel, R., Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Corynebacterium glutamicum. J. Bacteriol., 182, 6884–6891 (2000).
  • 20) Beeckmans, S., and Driessche, E. V., Pig heart fumarase contains two distinct substrate-binding sites differing in affinity. J. Biol. Chem., 273, 31661–31669 (1998).
  • 21) Weaver, T., and Banaszak, L., Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry, 35, 13955–13965 (1996).
  • 22) Weaver, T., Lees, M., Zaitsev, V., Zaitseva, I., Duke, E., Lindley, P., McSweeny, S., Svensson, A., Keruchenko, J., Keruchenko, I., Gladilin, K., and Banaszak, L., Crystal structures of native and recombinant yeast fumarase. J. Mol. Biol., 280, 431–442 (1998).
  • 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) Keruchenko, J. S., Keruchenko, I. D., Gladilin, K. L., Zaitsev, V. N., and Chirgadze, N. Y., Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae. Biochim. Biophys. Acta, 1122, 85–92 (1992).
  • 25) Moir, A., Feavers, I. M., and Guest, J. R., Characterization of the fumarase gene of Bacillus subtilis 168 cloned and expressed in Escherichia coli K 12. J. Gen. Microbiol., 130, 3009–3017 (1984).
  • 26) Puchegger, S., Redl, B., and Stöffler, G., Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus. J. Gen. Microbiol., 136, 1537–1541 (1990).
  • 27) Mizobata, T., Fujioka, T., Yamasaki, F., Hidaka, M., Nagai, J., and Kawata, Y., Purification and characterization of a thermostable class II fumarase from Thermus thermophilus. Arch. Biochem. Biophys., 355, 49–55 (1998).
  • 28) Hill, R. L., and Teipel, J. W., Fumarase and crotonase. In “The Enzymes” 3rd ed., ed. Boyer, P. D., Academic Press, New York, pp. 539–571 (1971).
  • 29) Hassett, D. J., Howell, M. L., Sokol, P. A., Vasil, M. L., and Dean, G. E., Fumarase C activity is elevated in response to iron deprivation and in mucoid, alginate-producing Pseudomonas aeruginosa: cloning and characterization of fumC and purification of native FumC. J. Bacteriol., 179, 1442–1451 (1997).
  • 30) Teipel, J. W., and Hill, R. L., The subunit interactions of fumarase. J. Biol. Chem., 246, 4859–4865 (1971).
  • 31) Nakamura, S., and Ogata, H., Specificity of fumarate hydratase. I. Formation of oxalacetate from unnatural (−)-tartrate by fumarate hydratase. J. Biol. Chem., 243, 528–532 (1968).
  • 32) Alberty, R. A., Fumarase. In “The Enzymes” 2nd ed., eds. Boyer, P. D., Lardy, H., and Myrbuck, K., Academic Press, New York, pp. 531–544 (1961).
  • 33) Dixon, M., Webb, E. C., Thorne, C. J. R., and Tipton, K. F., Equilibrium constant in terms of V and K m: the Haldane relationship. In “Enzymes” 3rd ed., eds. Dixon, M., and Webb, E. C., Longman Group, London, pp. 67–70 (1979).
  • 34) Penner, P. E., and Cohen, L. H., Effects of adenosine triphosphate and magnesium ions on the fumarase reaction. J. Biol. Chem., 244, 1070–1075 (1969).
  • 35) Dixon, M., Webb, E. C., Thorne, C. J. R., and Tipton, K. F., Enzyme inhibition and activation. In “Enzymes” 3rd ed., eds. Dixon, M., and Webb, E. C., Longman Group, London, pp. 332–353 (1979).
  • 36) Beeckmans, S., and Kanarek, L., A new purification procedure for fumarase based of affinity chromatography: isolation and characterization of pig-liver fumarase. Eur. J. Biochem., 78, 437–444 (1977).
  • 37) Wigler, P. W., and Alberty, R. A., The pH dependence of the competitive inhibition of fumarase. J. Am. Chem. Soc., 82, 5482–5488 (1960).
  • 38) Rose, I. A., Restructuring the active site of fumarase for the fumarate to malate reaction. Biochemistry, 36, 12346–12354 (1997).
  • 39) Massey, V., Studies on fumarase. 4. The effects of inhibitors on fumarase activity. Biochem. J., 55, 172–177 (1953).
  • 40) Rose, I. A., Warms, J. V. B., and Kuo, D. J., Proton transfer in catalysis by fumarase. Biochemistry, 31, 9993–9999 (1992).
  • 41) Rose, I. A., and Weaver, T. M., The role of the allosteric B site in the fumarase reaction. Proc. Natl. Acad. Sci. USA, 101, 3393–3397 (2004).
  • 42) Rose, I. A., How fumarase recycles after the malate→fumarate reaction: insights into the reaction mechanism. Biochemistry, 37, 17651–17658 (1998).

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