Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Identification and Characterization of Thermoplasma acidophilum 2-Keto-3-Deoxy-D-Gluconate Kinase: A New Class of Sugar Kinases

  • Jung, Jin-Hwa (Department of Chemical Engineering and Division of Molecular Life and Sciences, Pohang University of Science and Technology) ;
  • Lee, Sun-Bok (Department of Chemical Engineering and Division of Molecular Life and Sciences, Pohang University of Science and Technology)
  • Published : 2005.12.31
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Abstract

The thermoacidophilic archaeon Thermoplasma acidophilum has long been known to utilize D-glucose via the non-phosphorylated Entner-Doudoroff (nED) pathway. We now report the identification of a gene encoding 2-keto-3-deoxy-D-gluconate (KDG) kinase. The discovery of this gene implies the presence of a glycolysis pathway, other than the nED pathway. It was found that Ta0122 in the T. acidophilum genome corresponded to KDG kinase. This enzyme shares no similarity with known KDG kinases, and belongs to a novel class of sugar kinases. Of the five sugars tested only KDG was utilized as a substrate.

Keywords

References

  1. Verhees, C. H., S. W. Kengen, J. E. Tuininga, G. J. Schut, M. W. Adams, W. M. De Vos, and J. Van Der Oost (2003) The unique features of glycolytic pathways in archaea. Biochem. J. 375: 231-246 https://doi.org/10.1042/BJ20021472
  2. Lamble, H. J., N. I. Heyer, S. D. Bull, D. W. Hough, and M. J. Danson (2003) Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase. J. Biol. Chem. 278: 34066-34072 https://doi.org/10.1074/jbc.M305818200
  3. De Rosa, M., A. Gambacorta, B. Nicolaus, P. Giardina, E. Poerio, and V. Buonocore (1984) Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 224: 407-414 https://doi.org/10.1042/bj2240407
  4. Budgen, N. and M. J. Danson (1986) Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium Thermoplasma acidophilum. FEBS Lett. 196: 207-210 https://doi.org/10.1016/0014-5793(86)80247-2
  5. Smith, L. D., N. Budgen, S, J. Bungard, M. J. Danson, and D. W. Hough (1989) Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem. J. 261: 973-977 https://doi.org/10.1042/bj2610973
  6. Giardina, P., M. G. De Biasi, M. De Rosa, A. Gambacorta, and V. Buonocore (1986) Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 239: 517-522 https://doi.org/10.1042/bj2390517
  7. Kim S. and S. B. Lee (2005) Identification and characterization of Sulfolobus solfataricus D-gluconate dehydratase: A key enzyme in the nonphosphorylated Entner-Doudoroff pathway. Biochem. J. 387: 271-280 https://doi.org/10.1042/BJ20041053
  8. Lamble, H. J., C. C. Milburn, G. L. Taylor, D. W. Hough, and M. J. Danson (2004) Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus. FEBS Lett. 576: 133-136 https://doi.org/10.1016/j.febslet.2004.08.074
  9. Buchanan, C. L., H. Connaris, M. J. Danson, C. D. Reeve, and D. W. Hough (1999) An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for nonphosphorylated substrates. Biochem. J. 343: 563-570 https://doi.org/10.1042/0264-6021:3430563
  10. Noh, M. (2005) Identification and Characterization of Glycerate Kinase from the Thermoacidophilic Archaeon Thermoplasma acidophilum. Master Thesis, Pohang University of Science and Technology, Pohang, Korea
  11. Szymona, M. and M. Doudoroff (1958) Carbohydrate metabolism in Rhodopseudomonas sphreoides. J. Gen. Microbiol. 22: 167-183
  12. Bender, R., J. R. Andreesen, and G. Gottschalk (1971) 2- Keto-3-deoxygluconate, an intermediate in the fermentation of gluconate by clostridia. J. Bacteriol. 107: 570-573
  13. She, Q., R. K. Singh, F. Confalonieri, Y. Zivanovic, G. Allard, M. J. Awayez, C. C. Chan-Weiher, I. G. Clausen, B. A. Curtis, A. De Moors, G. Erauso, C. Fletcher, P. M. Gordon, I. Heikamp-de Jong, A. C. Jeffries, C. J. Kozera, N. Medina, X. Peng, H. P. Thi-Ngoc, P. Redder, M. E. Schenk, C. Theriault, N. Tolstrup, R. L. Charlebois, W. F. Doolittle, M. Duguet, T. Gaasterland, R. A. Garrett, M. A. Ragan, C. W. Sensen, and J. Van der Oost (2001) The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc. Natl. Acad. Sci. USA 98: 7835-7840
  14. Ahmed, H., T. J. Ettema, B. Tjaden, A. C. Geerling, J. Van Der Oost, and B. Siebers (2005) The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation. Biochem. J. 390: 529-540 https://doi.org/10.1042/BJ20041711
  15. Searcy, D. G. (1976) Thermoplasma acidophilum: intracellular pH and potassium concentration. Biochim. Biophys. Acta 451: 278-286 https://doi.org/10.1016/0304-4165(76)90278-6
  16. Conway, T. (1992) The Entner-Doudoroff pathway: history, physiology and molecular biology. FEMS Microbiol. Rev. 103: 1-27 https://doi.org/10.1111/j.1574-6968.1992.tb05822.x
  17. Cynkin, M. A. and G. Ashwell (1960) Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto- 3-deoxy-D-gluconokinase in Escherichia coli. J. Biol. Chem. 235: 1576-1579
  18. Ohshima, N., E. Inagaki, K. Yasuike, K. Takio, and T. H. Tahirov (2004) Structure of Thermus thermophilus 2-keto- 3-deoxygluconate kinase: evidence for recognition of an open chain substrate. J. Mol. Biol. 340: 477-489 https://doi.org/10.1016/j.jmb.2004.04.074
  19. Berger, M., H. Chen, W. Reutter, and S. Hinderlich (2002) Structure and function of N-acetylglucosamine kinase. Identification of two active site cysteines. Eur. J. Biochem. 269: 4212-4218 https://doi.org/10.1046/j.1432-1033.2002.03117.x
  20. Bork, P., C. Sander, and A. Valencia (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. USA 89: 7290-7294
  21. Rost, B., G. Yachdav, and J. Liu (2003) The PredictProtein Server. Nucleic Acids Res. 32: W321-W326 https://doi.org/10.1093/nar/gkh377