1887

Abstract

SUMMARY: grew in medium containing yeast extract when supplied with glutamate, histidine, glucose, maltose or pyruvate. Measurements of values and specific activities for two enzymes, phosphofructokinase and β-methylaspartase indicated that the glucose and glutamate fermentations were inducible. With glucose, the onset of active glucose metabolism was delayed in preference for energy sources provided by yeast extract. The inhibitory mechanism which was responsible for this delay did not appear to be a typical enzyme repression but rather a catabolite inhibition. No significant changes in the cobalamin content of the organisms accompanied growth with different substrates.

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/content/journal/micro/10.1099/00221287-54-2-277
1968-12-01
2024-12-09
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References

  1. BARKER H. A. 1956; BactBacterial Fermentations.. New York: John Wiley and Sons, Inc.
    [Google Scholar]
  2. BARKER H. A., WEISSBACH H., SMYTH R. D. 1958; A coenzyme containing pseudovitamin B12.. Proc. natn. Acad. Sci. U.S.A. 44:1093
    [Google Scholar]
  3. BARKER H. A., SMYTH R. D., WILSON R. M., WEISSBACH H. 1959; The purification and properties of /β-methylaspartase.. J. bJ. biol. Chem.234–320
    [Google Scholar]
  4. BERGMEYER H., BERNT E. 1963; In MethMethods of Enzymatic Analysis.Ed. by H. Bergmeyer, p. 123.. Verlag Chemie Gmb H.
    [Google Scholar]
  5. BUCHER T., CZOK R., LAMPRECHT W., LATKO E. 1963; In MethMethods of Enzymatic Analysis, Ed.by H. Bergmeyer, p. 253.. Verlag Chemie Gmb H.
    [Google Scholar]
  6. DAVIS B. D., MINGIOLI E. S. 1950; Mutants of Escherichiacoli requiring methionine orvitamin B12.. J. Bact. 60:17
    [Google Scholar]
  7. FOSTER M. A., JONES K. M., WOODS D. D. 1961; In MethMethods of Enzymatic Analysis.Ed. by H. Bergmeyer, p. 123.. Verlag Chemie Gmb H.
    [Google Scholar]
  8. HOMMES F. A. Effect of glucose on the level of glycolytic enzymes in yeast.. ArchArchs Biochem. Biophycs. 1966; 114:231
    [Google Scholar]
  9. LEE C. K., ORDAL Z. J. 1967; Regulatory effect of pyruvate on the glucose metabolism of ClosClostridium thermosaccharolyticum. J. Bact.. 90:1530
    [Google Scholar]
  10. Lowry O. H., PASSONNEAU J. V. 1964; A comparison of the kinetic properties of phospho-fructokinase from bacterial, plant and animal sources.. Arch. exp. Path. Pharmak. 248:185
    [Google Scholar]
  11. Lowry O. H., ROSEBROUGH N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent.. J. bJ. biol. Chem 193:265
    [Google Scholar]
  12. MAGASANIK B. 1961; Catabolite repression.. Cold Spring Harb. Symp. quant. Boil. 26:249
    [Google Scholar]
  13. MORGAN M. J., KORNBERG H. L. 1967; Effect of pyruvate on hexose metabolism by EschEscherichiacoli. Biochem J.. 57:57 p.
    [Google Scholar]
  14. OPIE L. H., NEWSHOLME E. A. 1967; The activities of fructose-1,6-diphosphatase, phospho-fructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle.. Biochem. J. 103:391
    [Google Scholar]
  15. PASSONNEAU J. V., LOWRY O. H. 1964; The role of phosphofructokinase in metabolic regulation.InAdvaAdvances in Enzyme Regulation.ED. by G. Weber. 2:265 London: Macmillan.
    [Google Scholar]
  16. SMITH E. L. 1965; VitaminB12.. London: Methun.
    [Google Scholar]
  17. WEBER G., LEE M. A., STAMM W. B. 1967; Inhibition of pyruvate kinase and glucokinase by acetylCoA and inhibition of glucokinase by phosphoenolpyruvate.. Life Sciences 6:2441
    [Google Scholar]
  18. WOODS D. D., CLIFTON C. E. 1938; Studies in the metabolism of the strict anaerobes (genus Clostridium). VI. Hydrogen production and amino acid utilization by Clostridium tetanomorphum. Biochem. J. 31:1774
    [Google Scholar]
  19. WYNGAARDEN J. B., ASHTON D. M. 1959; The regulation of activity of phosphoribosylpyro- phosphate amidotransferase by purine ribonucleotides; a potential feedback control of purine biosynthesis.. J. bio. Chem. 234:1492
    [Google Scholar]
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