Organization of Glucose Metabolism: A Model of Compartments by Poly-Isozymic Complexes

  • Tito Ureta
  • Jasna Radojković
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 127)


A metabolite being released from the active site of an enzyme may find itself in the predicament of deciding which pathway to choose among several possibilities. For instance, once glucose-6-P has been synthesized several alternative paths are possible, e.g., glycogen synthesis via phosphoglucomutase, glycolysis via phosphoglucose- isomerase, pentose-P pathway via glucose-6-P dehydrogenase, or back again to glucose through glucose-6-phosphatase (Fig. 1). Furthermore, the same situation will happen again at every branch-point along the metabolic maze until a committed step is reached.


Glycogen Synthesis Glycogen Phosphorylase Phosphoglucose Isomerase Glucose Incorporation Glycogen Phosphorylase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Breitenbach-Schmitt, I., Schmitt, H.D., Heinisch, J. and Zimmermann, F.K., 1984, Genetic and physiological evidence for the existence of a second glycolytic pathway in yeast parallel to the phosphofructokinase-aldolase sequence, Mol. Gen. Genet., 195:536.CrossRefGoogle Scholar
  2. Clegg, J.S., 1984a, Properties and metabolism of the aqueous cytoplasm and its boundaries, Am. J. Phvsiol., 246: R133.Google Scholar
  3. Clegg, J.A., 1984b, Metabolic compartmentation and “soluble” metabolic pathways, BioEssays, 1:129.CrossRefGoogle Scholar
  4. Finkelstein, J.D. and Martin, J.J., 1984, Methionine metabolism in mammals. Distribution of homocysteine between competing pathways, J. Biol. Chem., 259:9508.PubMedGoogle Scholar
  5. Hatzfeld, A., Feldmann, G., Guesnon, J., Frayssinet, C. and Schapira, F., 1978, Location of adult and fetal aldolases A, B, and C by immunoperoxidase technique in LF fast-growing rat hepatomas, Cancer Res., 38:16.PubMedGoogle Scholar
  6. Hue, L. and Hers, H.-G., 1969, A réévaluation of the pathway by which glucose is converted into glycogen in a liver homogenate, FEBS Lett.,3:41.PubMedCrossRefGoogle Scholar
  7. Jungermann, K. and Katz, N., 1982, Metabolic heterogeneity of liver parenchyma, in: “Metabolic Compartmentation”, H. Sies, éd., Academic Press, New York.Google Scholar
  8. Katz, J. and McGarry, J.D., 1984, The glucose paradox. Is glucose a substrate for liver metabolism?, J. Clin. Invest., 74:1901.PubMedCrossRefGoogle Scholar
  9. Lowry, C.V., Kimmey, J.S., Felder, S., Chi, M.M.-Y., Kaiser, K.K., Passonneau, P.N., Kirk, K.A. and Lowry, O.H., 1978, Enzyme patterns in single human muscle fibers, J. Biol. Chem., 253:8269.PubMedGoogle Scholar
  10. Lynch, R.M. and Paul, R.J., 1983, Compartmentation of glycolytic and glycogenolytic metabolism in vascular smooth muscle, Science. 222:1344.PubMedCrossRefGoogle Scholar
  11. MacGregor, J.S., Singh, V.N., Davoust, S., Melloni, E., Pontremoli, S. and Horecker, B.L., 1980, Evidence for formation of a rabbit liver aldolase-rabbit liver fructose-1,6-bisphosphatase complex, Proc. Natl. Acad., Sci. U.S.A., 77:3889.CrossRefGoogle Scholar
  12. Markert, C.L., 1975, Biology of isozymes, In: “Isozymes. I. Molecular Structure,” C.L. Markert, ed., Academic Press, New York.Google Scholar
  13. Markert, C.L. and Moller, F., 1959, Multiple forms of enzymes: tissue, ontogenetic, and species specific patterns, Proc. Natl. Acad. Sci. U.S.A., 45:753.PubMedCrossRefGoogle Scholar
  14. Masters, C.J., 1981, Interactions between soluble enzymes and subcellular structure CRC Crit. Rev. Biochem., 11:105.CrossRefGoogle Scholar
  15. Newgard, C.B., Kirsch, L.J., Foster, D.W. and McGarry, K.D., 1983, Studies on the mechanism by which exogenous glucose is converted into liver glycogen in the rat, A direct or an indirect pathway?, J. Biol. Chem., 258:8046.PubMedGoogle Scholar
  16. Newgard, C.B., Moore, S.V., Foster, D.W. and McGarry, K.D., 1984, Efficient hepatic glycogen synthesis in refeeding rats requires continued carbon flow through the gluconeogenic pathway, J. Biol. Chem., 259:6948.Google Scholar
  17. Ottaway, J.H. and Mowbray, J., 1977, The role of compartmentation in the control of glycolysis, Curr. Top. Cell. Reg., 12:107.Google Scholar
  18. Pilkis, S.J., Regen, D.M., Claus, T.H. and Cherrington, A.D., 1985, Role of hepatic glycolysis and gluco neo gene sis in glycogen synthesis, BioEssays, 2:273.CrossRefGoogle Scholar
  19. Radojković, J. and Ureta, T., 1982, Regulation of carbohydrate metabolism in microinjected frog oocytes, Arch. Biol. Med. Exp., 15:395.Google Scholar
  20. Srere, P.A. and Mosbach, K., 1974, Metabolic compartmentation: symbiotic, organellar, multienzymic, and microenvironmental, Annu. Rev. Microbiol.. 28:61.PubMedCrossRefGoogle Scholar
  21. Stebbing, N., 1980, Evolution of compartmentation, metabolic channelling and control of biosynthetic pathways, In: “Cell Compartmentation and Metabolic Channelling”, L. Nover, F. Lynen, and K. Mothes, eds., Elsevier/North-Holland Biomedical Press, Amsterdam.Google Scholar
  22. Ureta, T., 1978, The role of isozymes in metabolism: a model of metabolic pathways as the basis for the biological role of isozymes, Curr. Top. Cell. Reg., 13:233.Google Scholar
  23. Ureta, T., 1985, Organización del metabolismo: localización subcelular de enzimas glicoliticas, Arch. Biol. Med. Exp., 18:9.PubMedGoogle Scholar
  24. Ureta, T. and Radojkovic, J., 1979, Frog oocytes: a model system for ifi vivo studies on the regulation of glucose metabolism, Acta Cient. Venez., 30:396.PubMedGoogle Scholar
  25. Ureta, T. and Radojkovic, J., 1985a, Search for compartments of glucose metabolism in the microinjected frog oocyte, Arch. Biol. Med. Exp., 18, in the press.Google Scholar
  26. Ureta, T. and Radojkovié, J., 1985b, Microinjected frog oocytes: a first- rate test tube for studies on metabolism and its control, BioEssays., 2:221.CrossRefGoogle Scholar
  27. Wallimann, T., Moser, H. and Eppenberger, H.M., 1983, Isoenzyme-specific localization of M-line bound creatine kinase in myogenic cells, J. Muscle Res. Cell. Mot., 4:429.CrossRefGoogle Scholar
  28. Walsh, K. and Koshland, D.E., Jr., 1984, Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt, J. Biol. Chem., 259:9646.PubMedGoogle Scholar
  29. Welch, G.R., 1977, Role of organization of multienzyme systems in cellular metabolism: a general synthesis. Proc. Biophys. Mol, Biol., 32:103.CrossRefGoogle Scholar
  30. Wilson, J.E., 1985, Regulation of mammalian hexokinase activity, In:“Regulation of Carbohydrate Metabolism,” Vol. 1, R. Beitner, ed., CRC Press, Boca Raton, FL.Google Scholar
  31. Wolpert, J.S, and Ernst-Fonberg, M.L., 1975, Dissociation and characterization of enzymes from a multienzyme complex involved in CO2 fixation, Biochemistrv, 14:1103.CrossRefGoogle Scholar
  32. Wombacher, H., 1983, Molecular compartmentation by enzyme cluster formation. A view over current investigations, Mol. Cell. Biochem., 56:155.PubMedCrossRefGoogle Scholar
  33. Yamashita, S., Yamamoto, N. and Yasuda, K., 1979, Immunohistochemical study of lactate dehydrogenase isozymes in rat liver, Acta Histochem. Cytochem., 12:125.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Tito Ureta
    • 1
  • Jasna Radojković
    • 1
  1. 1.Departamento de Biologia Facultad de CienciasUniversidad de ChileSantiagoChile

Personalised recommendations