1887

Abstract

SUMMARY: During growth of on acetate, isocitrate dehydrogenase (ICDH) is partially inactivated by phosphorylation and is thus rendered rate-limiting in the Krebs cycle so that the intracellular concentration of isocitrate rises which, in turn, permits an increased flux of carbon through the anaplerotic sequence of the glyoxylate bypass. A large number of metabolites stimulate ICDH phosphatase and inhibit ICDH kinase in the wild-type ( ML 308) and thus regulate the utilization of isocitrate by the two competing enzymes, ICDH and isocitrate lyase. Addition of pyruvate to acetate grown cultures triggers a rapid dephosphorylation and threefold activation of ICDH, both in the wild-type (ML308) and in mutants lacking pyruvate dehydrogenase (ML308/Pdh), PEP synthase (ML308/Pps) or both enzymes (ML308/Pdh Pps). Pyruvate stimulates the growth on acetate of those strains with an active PEP synthase but inhibits the growth of those strains that lack this enzyme. When pyruvate is exhausted, ICDH is again inactivated and the growth rate reverts to that characteristic of growth on acetate. Because pyruvate stimulates dephosphorylation of ICDH in strains with differing capabilities for pyruvate metabolism, it seems likely that pyruvate itself is a sufficient signal to activate the dephosphorylation mechanism, but this does not discount the importance of other signals under other circumstances.

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/content/journal/micro/10.1099/00221287-132-3-797
1986-03-01
2021-05-13
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References

  1. Ashworth J. M., Kornberg H. L. 1963; Fine control of the glyoxylate cycle by allosteric inhibition of isocitrate lyase. Biochimica et biophysica acta 73:519–522
    [Google Scholar]
  2. Ashworth J. M., Kornberg H. L. 1964; The role of isocitrate lyase in Escherichia coli. Biochimica et biophysica acta 89:383–384
    [Google Scholar]
  3. Bennett P. M., Holms W. H. 1975; Reversible inactivation of the isocitrate dehydrogenase of Escherichia coli ML308 during growth on acetate. Journal of General Microbiology 87:37–51
    [Google Scholar]
  4. Bergmeyer H. U., Möllering H. 1974; Acetate determination with preceding indicator reaction. Edited by H. U. Bergmeyer. New York & London: Academic Press. In Methods of Enzymatic Analysis, 2nd edn vol. 3:1520–1527
    [Google Scholar]
  5. Borthwick A. C., Holms W. H., Nimmo H. G. 1984a; Isolation of active and inactive forms of isocitrate dehydrogenase from Escherichia coli ML308. European Journal of Biochemistry 141:393–400
    [Google Scholar]
  6. Borthwick A. C., Holms W. H., Nimmo H. G. 1984b; The phosphorylation of Escherichia coli isocitrate dehydrogenase in intact cells. Biochemical Journal 222:797–804
    [Google Scholar]
  7. Brown T. D. K., Jones-Mortimer M. C., Kornberg H. L. 1977; The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. Journal of General Microbiology 102:327–336
    [Google Scholar]
  8. Bücher T., Czok R., Lamprecht W., Latzko E. 1963; Pyruvate. Edited by H. U. Bergmeyer. London & New York: Academic Press. In Methods of Enzymatic Analysis, pp.253–259
    [Google Scholar]
  9. Cohn M., Monod J. 1951; Purification et properties de la β-galactosidase (lactase) d'Escherichia coli. Biochimica et biophysica acta 7:153–174
    [Google Scholar]
  10. El-Mansi E. M. T., Nimmo H. G., Holms W. H. 1985; The role of isocitrate in control of the phosphorylation of isocitrate dehydrogenase in Escherichia coli ML308. FEBS Letters 183:251–255
    [Google Scholar]
  11. Friedemann T. E., Haugen G. E. 1943; Pyruvic acid. II. The determination of keto-acids in blood and urine. Journal of Biological Chemistry 147:415–442
    [Google Scholar]
  12. Garnak M., Reeves H. C. 1979a; Phosphorylation of isocitrate dehydrogenase of Escherichia coli. Science 203:1111–1112
    [Google Scholar]
  13. Garnak M., Reeves H. C. 1979b; Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli. Journal of Biological Chemistry 254:7915–7920
    [Google Scholar]
  14. Gounaris A. D., Hager L. P. 1961; A resolution of the Escherichia coli pyruvate dehydrogenase complex. Journal of Biological Chemistry 236:1013–1018
    [Google Scholar]
  15. Hamilton I. D., Holms W. H. 1970; Measurement of respiration of micro-organisms during batch culture. Laboratory Practice 19:797–798
    [Google Scholar]
  16. Harvey N. L., Fewson C. A., Holms W. H. 1968; Apparatus for batch culture of micro-organisms. Laboratory Practice 17:1134–1136
    [Google Scholar]
  17. Holms W. H., Bennett P. M. 1971; Regulation of isocitrate dehydrogenase activity in Escherichia coli on adaptation to acetate. Journal of General Microbiology 65:57–68
    [Google Scholar]
  18. Holms W. H., Robertson A. G. 1974; Control of derepressed β-galactosidase synthesis in Escherichia coli. Archives of Microbiology 96:21–35
    [Google Scholar]
  19. Hsie A. W., Rickenberg H. V. 1966; A mutant of Escherichia coli deficient in phosphoenolpyruvate carboxykinase activity. Biochemical and Biophysical Research Communications 25:676–683
    [Google Scholar]
  20. Kornberg H. L. 1966; The role and control of the glyoxylate cycle in Escherichia coli. Biochemical Journal 99:1–11
    [Google Scholar]
  21. Ingledew W. J., Poole R. K. 1984; The respiratory chains of Escherichia coli. Microbiological Reviews 48:222–271
    [Google Scholar]
  22. LaPorte D. C., Koshland D. E. Jr. 1982; A protein with kinase and phosphatase activity involved in Krebs cycle regulation. Nature, London 300:458–460
    [Google Scholar]
  23. LaPorte D. C., Koshland D. E. Jr. 1983; Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation. Nature, London 305:286–290
    [Google Scholar]
  24. Matin A., Konings W. N. 1973; Transport of lactate and succinate by membrane vesicles of Escherichia coli, Bacillus subtilis and a Pseudomonas species. European Journal of Biochemistry 34:58–67
    [Google Scholar]
  25. Nimmo G. A., Nimmo H. G. 1984; The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli and the roles of these activities in the control of isocitrate dehydrogenase. European Journal of Biochemistry 141:409–414
    [Google Scholar]
  26. Nimmo G. A., Borthwick A. C., Holms W. H., Nimmo H. G. 1984; Partial purification and properties of isocitrate dehydrogenase kinase/phos-phatase from Escherichia coli ML308. European Journal of Biochemistry 141:401–408
    [Google Scholar]
  27. Sanwal B. D. 1970; Allosteric controls of amphibolic pathways in bacteria. Bacteriological Reviews 34:20–39
    [Google Scholar]
  28. Seakins J. W. T., Smith I., Smith M. J. 1976; Ketoacids. Edited by I. Smith and J. W. T. Seakins. London: Heinemann. In Chromatographic and Electrophoretic Techniques, 4th edn vol. 1 Paper and Thin layer Chromatography, pp.:244–252
    [Google Scholar]
  29. Shaw-Goldstein L. A., Gennis R. B., Walsh C. 1978; Identification, localization and function of the thiamin pyrophosphate and flavin adenine dinucleotide dependent pyruvate oxidase in isolated membrane vesicles of Escherichia coli B. Biochemistry 17:5605–5613
    [Google Scholar]
  30. Walsh K., Koshland D. E. Jr. 1984; Determination of flux through the branch point of two metabolic cycles : the tricarboxylic acid cycle and the glyoxylate shunt. Journal of Biological Chemistry 259:9646–9654
    [Google Scholar]
  31. Woeller F.-H. 1961; Liquid scintillation counting of 14CO2 with phenethylamine. Analytical Biochemistry 2:508–511
    [Google Scholar]
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