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. 1969 Mar;111(5):609–613. doi: 10.1042/bj1110609

Adenosine phosphates and the control of glycolysis and gluconeogenesis in yeast

C Chapman 1,*, W Bartley 1
PMCID: PMC1187588  PMID: 5783465

Abstract

1. Changes in dry weight, protein, RNA and DNA were measured in yeast during adaptation to glycolytic metabolism. 2. Only RNA increased significantly during the lag phase, but during the exponential phase all these cellular components increased in parallel. 3. The concentrations of ATP, ADP, AMP and glucose 6-phosphate were measured in respiring yeast and during the transition to glycolytic metabolism. 4. In respiring cells the concentration of AMP was at its highest and that of ATP was at its lowest; this relationship was reversed in glycolysing cells. 5. ADP concentration was similar in respiring and glycolysing cells, but glucose 6-phosphate concentration was much higher in the glycolysing cells. 6. A possible reason for mitochondrial repression is suggested. 7. It is concluded that adenosine phosphates do not control the direction of glycolytic flux in yeast and an alternative control of glycolysis and gluconeogenesis by enzyme activation and inactivation is suggested.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ashmore J., Wagle S. R., Uete T. Studies on gluconeogenesis. Adv Enzyme Regul. 1964;2:101–114. doi: 10.1016/s0065-2571(64)80008-x. [DOI] [PubMed] [Google Scholar]
  2. BURTON K. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956 Feb;62(2):315–323. doi: 10.1042/bj0620315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chapman C., Bartley W. The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria. Biochem J. 1968 Apr;107(4):455–465. doi: 10.1042/bj1070455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ferguson J. J., Jr, Boll M., Holzer H. Yeast malate dehydrogenase: enzyme inactivation in catabolite repression. Eur J Biochem. 1967 Mar;1(1):21–25. doi: 10.1007/978-3-662-25813-2_4. [DOI] [PubMed] [Google Scholar]
  5. GANCEDO C., SALAS M. L., GINER A., SOLS A. RECIPROCAL EFFECTS OF CARBON SOURCES ON THE LEVELS OF AN AMP-SENSITIVE FRUCTOSE-1,6-DIPHOSPHATASE AND PHOSPHOFRUCTOKINASE IN YEAST. Biochem Biophys Res Commun. 1965 Jun 18;20:15–20. doi: 10.1016/0006-291x(65)90944-7. [DOI] [PubMed] [Google Scholar]
  6. HUTCHISON W. C., MUNRO H. N. The determination of nucleic acids in biological materials. A review. Analyst. 1961 Dec;86:768–813. doi: 10.1039/an9618600768. [DOI] [PubMed] [Google Scholar]
  7. Hommes F. A. Mechanism of the Crabtree effect in yeast grown with different glucose concentrations. Arch Biochem Biophys. 1966 Feb;113(2):324–330. doi: 10.1016/0003-9861(66)90193-7. [DOI] [PubMed] [Google Scholar]
  8. Jayaraman J., Cotman C., Mahler H. R., Sharp C. W. Biochemical correlates of respiratory deficiency. VII. Glucose repression. Arch Biochem Biophys. 1966 Sep 26;116(1):224–251. doi: 10.1016/0003-9861(66)90029-4. [DOI] [PubMed] [Google Scholar]
  9. KREBS E. G., FISCHER E. H. Molecular properties and transformations of glycogen phosphorylase in animal tissues. Adv Enzymol Relat Subj Biochem. 1962;24:263–290. doi: 10.1002/9780470124888.ch5. [DOI] [PubMed] [Google Scholar]
  10. LINNANE A. W., VITOLS E., NOWLAND P. G. Studies on the origin of yeast mitochondria. J Cell Biol. 1962 May;13:345–350. doi: 10.1083/jcb.13.2.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LOWRY O. H., PASSONNEAU J. V., HASSELBERGER F. X., SCHULZ D. W. EFFECT OF ISCHEMIA ON KNOWN SUBSTRATES AND COFACTORS OF THE GLYCOLYTIC PATHWAY IN BRAIN. J Biol Chem. 1964 Jan;239:18–30. [PubMed] [Google Scholar]
  12. MASTER R. W. POSSIBLE SYNTHESIS OF POLYRIBONUCLEOTIDES OF KNOWN BASE-TRIPLET SEQUENCES. Nature. 1965 Apr 3;206:93–93. doi: 10.1038/206093b0. [DOI] [PubMed] [Google Scholar]
  13. Mendicino J., Prihar H. S., Salama F. M. Role of enzyme-enzyme interactions in the regulation of glycolysis. Inactivation of D-fructos 1,6-diphosphatase by kidney cortex mitochondria. J Biol Chem. 1968 May 25;243(10):2710–2717. [PubMed] [Google Scholar]
  14. NEIDHARDT F. C., FRAENKEL D. G. Metabolic regulation of RNA synthesis in bacteria. Cold Spring Harb Symp Quant Biol. 1961;26:63–74. doi: 10.1101/sqb.1961.026.01.012. [DOI] [PubMed] [Google Scholar]
  15. Newsholme E. A., Gevers W. Control of glycolysis and gluconeogenesis in liver and kidney cortex. Vitam Horm. 1967;25:1–87. doi: 10.1016/s0083-6729(08)60033-3. [DOI] [PubMed] [Google Scholar]
  16. Polakis E. S., Bartley W. Changes in dry weight, protein, deoxyribonucleic acid, ribonucleic acid and reserve and structural carbohydrate during the aerobic growth cycle of yeast. Biochem J. 1966 Mar;98(3):883–887. doi: 10.1042/bj0980883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Polakis E. S., Bartley W. Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources. Biochem J. 1965 Oct;97(1):284–297. doi: 10.1042/bj0970284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Polakis E. S., Bartley W., Meek G. A. Changes in the structure and enzyme activity of Saccharomyces cerevisiae in response to changes in the environment. Biochem J. 1964 Feb;90(2):369–374. doi: 10.1042/bj0900369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. SACKTOR B. Cell structure and the metabolism of insect flight muscle. J Biophys Biochem Cytol. 1955 Jan;1(1):29–46. doi: 10.1083/jcb.1.1.29. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Start C., Newsholme E. A. The effects of starvation and alloxan-diabetes on the contents of citrate and other metabolic intermediates in rat liver. Biochem J. 1968 Apr;107(3):411–415. doi: 10.1042/bj1070411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Uyeda K., Racker E. Regulatory mechanisms in carbohydrate metabolism. 8. The regulatory function of phosphate in glycolysis. J Biol Chem. 1965 Dec;240(12):4689–4693. [PubMed] [Google Scholar]
  22. VINUELA E., SALAS M. L., SOLS A. End-product inhibition of yeast phosphofructokinase by ATP. Biochem Biophys Res Commun. 1963 Jul 18;12:140–145. doi: 10.1016/0006-291x(63)90250-x. [DOI] [PubMed] [Google Scholar]
  23. Viñuela E., Salas M. L., Salas M., Sols A. Two interconvertible forms of yeast phosphofructokinase with different sensitivity to endproduct inhibition. Biochem Biophys Res Commun. 1964 Mar 26;15(3):243–249. doi: 10.1016/0006-291x(64)90154-8. [DOI] [PubMed] [Google Scholar]

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