1887

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Volume 128, Issue 1

Control of Pyruvate Kinase Activity during Glycolysis and Gluconeogenesis in Free

Abstract

The concentrations of glycolytic intermediates and ATP and the activities of certain glycolytic and gluconeogenic enzymes were determined in cultures grown on a fully defined medium with glucose, glycerol or lactate as energy source. On all three energy sources, enzyme activities were similar and pyruvate kinase was considerably more active than the gluconeogenic enzyme pyruvate, orthophosphate dikinase, indicating the need for regulation of pyruvate kinase activity. The intracellular concentration of glucose 6-phosphate, a specific activator of pyruvate kinase in this organism, changed markedly according to both the nature and the concentration of the growth substrate: the concentration (7–10 m) during growth with excess glucose or glycerol was higher than that (1–2 m) during growth with lactate or at growth-limiting concentrations of glycerol or glucose. Other glycolytic intermediates, apart from pyruvate, were present at concentrations below 2 m. Glucose 6-phosphate overcame inhibition of pyruvate kinase activity by ATP and inorganic phosphate. With 1 m-ATP and more than 10 m inorganic phosphate, a change in glucose 6-phosphate concentration from 1–2 m to 7–10 m was sufficient to switch pyruvate kinase from a strongly inhibited to a fully active state. The results provide a plausible mechanism for the regulation of glycolysis and gluconeogenesis in .

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© Society for General Microbiology, 1982
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1982-01-01
2024-12-07
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References

  1. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dyebinding. Analytical Biochemistry 72:248–254
     [Google Scholar]
  2. Cook A. M., Urban E., Schlegel H. G. 1976; Measuring the concentrations of metabolites in bacteria. Analytical Biochemistry 72:191–201
     [Google Scholar]
  3. Endrenyi L., Fajszi C., Kwong F. H. F. 1975; Evaluation of Hill slopes and Hill coefficients when the saturation binding or velocity is not known. European Journal of Biochemistry 51:317–328
     [Google Scholar]
  4. Harold F. M., Spitz E. 1975; Accumulation of arsenate, phosphate and aspartate by Streptococcus faecalis. Journal of Bacteriology 122:266–277
     [Google Scholar]
  5. Lambert M., Neish A. C. 1950; Rapid method for estimation of glycerol in fermentation solutions. Canadian Journal of Research 28B:83–89
     [Google Scholar]
  6. Lowry O. H., Carter J., Ward J. B., Glaser L. 1971; The effect of carbon and nitrogen sources on the level of metabolic intermediates in Escherichia coli. . Journal of Biological Chemistry 246:6511–6521
     [Google Scholar]
  7. Mizushima S., Kitahara K. 1964; Quantitative studies on glycolytic enzymes in Lactobacillus plantarum. II. Intracellular concentrations of glycolytic intermediates in glucose-metabolizing washed cells. Journal of Bacteriology 87:1429–1435
     [Google Scholar]
  8. O’Brien W. E., Bowien S., Wood H. G. 1975; Isolation and characterisation of a pyrophosphate-dependent phosphofructokinase from Propioni-bacterium shermanii. . Journal of Biological Chemistry 250:8690–8695
     [Google Scholar]
  9. Rolleston F. S., Newsholme E. A. 1967; Control of glycolysis in cerebral cortex slices. Biochemical Journal 104:524–533
     [Google Scholar]
  10. Siegel W. H., Donohue T., Bernlohr R. W. 1977; Determination of pools of tricarboxylic acid cycle and related acids in bacteria. Applied and Environmental Microbiology 34:512–517
     [Google Scholar]
  11. Siu P. M. L., Wood H. G. 1962; Phospho-enolpyruvic carboxytransphosphorylase, a CO2 fixation enzyme from propionic acid bacteria. Journal of Biological Chemistry 237:3044–3051
     [Google Scholar]
  12. Slein M. W., Cori G. T., Cori C. F. 1950; A comparative study of hexokinase from yeast and animal tissues. Journal of Biological Chemistry 186:763–780
     [Google Scholar]
  13. Smart J. B., Pritchard G. G. 1979; Regulation of pyruvate kinase from Propionibacterium shermanii. . Archives of Microbiology 122:281–288
     [Google Scholar]
  14. Thomas T. D., Ellwood D. C., Longyear V. M. C. 1979; Change from homo-to heterolactic fermentation by Streptococcus lactis resulting from glucose limitation in anaerobic chemostat cultures. Journal of Bacteriology 138:109–117
     [Google Scholar]
  15. Thompson J. 1978; In vivo regulation of glycolysis and characterisation of sugar: phosphotransferase systems in Streptococcus lactis. . Journal of Bacteriology 136:465–476
     [Google Scholar]
  16. Thompson J., Thomas T. D. 1977; Phosphoenolpyruvate and 2-phosphoglycerate: endogenous energy source(s) for sugar accumulation by starved cells of Streptococcus lactis. . Journal of Bacteriology 130:583–595
     [Google Scholar]
  17. Devries W., Van Wyck-Kapteyn W. M. C., Stouthamer A. H. 1973; Generation of ATP during cytochrome-linked anaerobic electron transport in propionic acid bacteria. Journal of General Microbiology 76:31–41
     [Google Scholar]
  18. Wood H. G., O’Brien W. E., Michaels G. 1977; Properties of carboxytransphosphorylase; pyruvate,phosphate dikinase; pyrophosphate phosphofructokinase and pyrophosphate-acetate kinase and their roles in the metabolism of inorganic pyrophosphate. Advances in Enzymology 45:85–155
     [Google Scholar]
  19. Yamada T., Carlsson J. 1975; Regulation of lactate dehydrogenase and change of fermentation products in streptococci. Journal of Bacteriology 124:55–61
     [Google Scholar]
  20. Yoshizaki F., Imahori K. 1979; Key role of phosphoenolpyruvate in the regulation of glycolysis-gluconeogenesis in Thermus thermophilus HB 8. Agricultural and Biological Chemistry 43:537–545
     [Google Scholar]
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Control of Pyruvate Kinase Activity during Glycolysis and Gluconeogenesis in Propionibacterium shermanii
Microbiology 128, 167 (1982); https://doi.org/10.1099/00221287-128-1-167
/content/journal/micro/10.1099/00221287-128-1-167
/content/journal/micro/10.1099/00221287-128-1-167
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