Archiv für Mikrobiologie

, Volume 88, Issue 2, pp 135–145 | Cite as

The effect of metabolic inhibitors on the loss of isocitrate lyase activity from Chlorella

  • Christopher F. Thurston
  • Peter C. L. John
  • Philip J. Syrett


  1. 1.

    Isocitrate lyase disappeared from acetate-adapted cells of Chlorella when cells were incubated in darkness with glucose. Loss of activity was particularly rapid in nitrogen-free medium and was accompanied by disappearance of the enzyme protein.

  2. 2.

    Loss of isocitrate lyase activity was prevented by addition of 2-deoxyglucose, glucosamine, cycloheximide or chloramphenicol.

  3. 3.

    The rate of loss of activity was increased by addition of 2:4-dinitrophenol but this substance prevented the loss of enzyme protein i.e it protected the inactivated enzyme from degradation.

  4. 4.

    In vitro studies on the digestion of isocitrate lyase protein by papain showed that the enzyme protein was protected from digestion by its substrate, isocitrate, but that inhibitors of the enzyme, namely phosphoenol pyruvate, succinate, oxaloacetate and pyruvate, provided no protection.



Glucose Enzyme Pyruvate Succinate Chloramphenicol 
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  1. Bell, R. G.: Stability of induced glucosidase activity in the absence of inducer. Canad. J. Biochem. 47, 677–684 (1969).Google Scholar
  2. Bradley, S. G., Creevy, D.: Induction and inhibition of α-glucosidase synthesis in Candida stellatoidea. J. Bact. 81, 303–310 (1961).Google Scholar
  3. Engelsma, G.: Photoinduction of phenylalanine deaminase in Gherkin seedlings. 1. Effect of blue light. Planta (Berl.) 75, 207–219 (1967).Google Scholar
  4. Feldman, M., Yagil, G.: Does cycloheximide interfere with protein degradation? Biochem. biophys. Res. Commun. 37, 198–203 (1969).Google Scholar
  5. Ferguson, J. J., Boll, M., Holzer, H.: Yeast malate dehydrogenase: enzyme inactivation in catabolite repression. Europ. J. Biochem. 1, 21–25 (1967).Google Scholar
  6. Goldberg, A. L.: A role of amino acyl-tRNA in the regulation of protein breakdown in Escherichia coli. Proc. nat. Acad. Sci. (Wash.) 68, 363–366 (1971).Google Scholar
  7. Grisiola, S.: The catalytic environment and its biological implications. Physiol. Rev. 44, 657–712 (1964).Google Scholar
  8. Halvorson, H. O.: Intracellular protein and nucleic acid turnover in resting yeast cells. Biochim. biophys. Acta (Amst.) 27, 255–266 (1958).Google Scholar
  9. Holzer, H.: Regulation of enzymes by enzyme-catalysed chemical modification. Advanc. Enzymol. 32, 297–326 (1969).Google Scholar
  10. John, P. C. L., Syrett, P. J.: Isocitrate lyase in Chlorella: purification and the mechanism of its disappearance from cells. J. gen. Microbiol. 46, viii-ix (1967a).Google Scholar
  11. John, P. C. L., Syrett, P. J.: The purification and properties of isocitrate lyase from Chlorella. Biochem. J. 105, 409–416 (1967b).Google Scholar
  12. John, P. C. L., Syrett, P. J.: The inhibition by intermediary metabolites of isocitrate lyase from Chlorella pyrenoidosa. Biochem. J. 110, 481–484 (1968a).Google Scholar
  13. John, P. C. L., Syrett, P. J.: The estimation of the quantity of isocitrate lyase protein in acetate adapted cells of Chlorella pyrenoidosa. J. exp. Bot. 19, 733–741 (1968b).Google Scholar
  14. John, P. C. L., Thurston, C. F., Syrett, P. J.: Disappearance of isocitrate lyase enzyme from cells of Chlorella pyrenoidosa. Biochem. J. 119, 913–919 (1970).Google Scholar
  15. Kenney, F. T.: Turnover of rat liver tyrosine transaminase: stabilization after inhibition of protein synthesis. Science 156, 525–528 (1967).Google Scholar
  16. Kornberg, H. L.: Control of biosynthesis from C2-compounds. In: Mécanisme de régulation des activités cellulaires chez les microorganismes. C.N.R.S. (Paris) 124, 193–207 (1963); published 1965.Google Scholar
  17. Martin, R. G.: The first enzyme of histidine biosynthesis: the nature of feedback inhibition by histidine. J. biol. Chem. 238, 257–268 (1963).Google Scholar
  18. Morris, I.: Inhibition of protein synthesis by cycloheximide (actidione) in Chlorella. Nature (Lond.) 211, 1190–1192 (1966a).Google Scholar
  19. Morris, I.: Some effects of chloramphenicol on the metabolism of Chlorella. I. The effect on protein, polysaccharide and nucleic acid synthesis. Arch. Mikrobiol. 54, 160–168 (1966b).Google Scholar
  20. Ornstein, L., Davis, B. J.: Disc electrophoresis. Rochester, N.Y.: Distillation Products industries preprint 1961.Google Scholar
  21. Pine, M. J.: Intracellular protein breakdown in the L1210 ascites leukemia. Cancer Res. 27, 522–525 (1967).Google Scholar
  22. Schimke, R. T.: On the roles of synthesis and degradation in regulation of enzyme levels in mammalian tissues. Curr. Topics Cellular Regulation 1, 77–124 (1969).Google Scholar
  23. Schimke, R. T., Doyle, D.: Control of enzyme levels in animal tissues. Ann. Rev. Biochem. 39, 929–976 (1970).Google Scholar
  24. Spiegelman, S., Reiner, J. M.: The formation and stabilization of an adaptive enzyme in the absence of its substrate. J. gen. Physiol. 31, 175–193 (1947).Google Scholar
  25. Sussman, M., Sussman, R.: Patterns of RNA synthesis and of enzyme accumulation and disappearance during cellular slime mould cytodifferentiation. Symp. Soc. gen. Microbiol. 19, 403–435 (1969).Google Scholar
  26. Syrett, P. J.: Respiration rate and internal adenosine triphosphate concentration in Chlorella vulgaris. Arch. Biochem. 75, 115–124 (1958).Google Scholar
  27. Thurston, C. F.: The mechanism of the disapperance of isocitrate lyase from Chlorella. Ph.D. Thesis, University of London 1970.Google Scholar
  28. Travis, R. L., Jordan, W. R., Huffaker, R. C.: Evidence for an inactivating system of nitrate reductase in Hordeum vulgare L. during darkness that requires protein synthesis. Plant Physiol. 44, 1150–1156 (1969).Google Scholar
  29. Webb, J. L.: Enzyme and metabolic inhibitors. Vol. 2, pp. 381–383, 386–403. London-New York: Academic Press 1966.Google Scholar
  30. Wiame, J. M.: The regulation of arginine metabolism in Saccharomyces cerevisiae: exclusion mechanisms. Curr. Topics Cellular Regulation 4, 1–38 (1971).Google Scholar

Copyright information

© Springer-Verlag 1973

Authors and Affiliations

  • Christopher F. Thurston
    • 1
  • Peter C. L. John
    • 2
  • Philip J. Syrett
    • 3
  1. 1.Department of MicrobiologyQueen Elizabeth CollegeLondon W. 8England
  2. 2.Department of BotanyQueens UniversityBelfast 7N. Ireland
  3. 3.Department of Botany and MicrobiologyUniversity CollegeSwanseaWales, UK

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