Coupled Reactions and Channelling: their Role in the Control of Metabolism

  • Tamás Keleti
Chapter
Part of the NATO ASI Series book series (NSSA, volume 190)

Abstract

Control analysis was developed for describing the regulatory properties of metabolic pathways (Savageau, 1972, 1976; Kacser & Burns, 1973, 1979; Kacser, 1983; Heinrich & Rapoport, 1973, 1974aó, 1983; Heinrich et al, 1977). The more effective the control, the more elastic the metabolic pathway, i.e more able to respond to changes in external conditions. Kacser (1983) has suggested the idea of “molecular democracy” to characterize each enzyme in a metabolic process as an autonomous entity and the control as a sort of linear superposition of the effects of the individual enzymes. The milieu of this “molecular society” is a bulk aqueous solution with non-interacting enzymes and non-compartmentalized metabolites homogeneously dispersed therein. The links in such a metabolic network are the intermediate metabolite pools.

Keywords

Transient Time Biochemical System Triose Phosphate Isomerase Control Coefficient Allosteric Enzyme 
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.

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References

  1. Bartha, F. & Keleti, T. (1979) Oxid. Commun 1, 75 - 84Google Scholar
  2. Batke, J. & Tompa, P. (1986) in Dynamics of Biochemical Systems (Damjanovich, S., Keleti, T. & Trion, L. eds.). Akadémiai Kiadó, Budapest, and Elsevier, Amsterdam. pp. 247 - 266Google Scholar
  3. Backe, J., Asbóth, G., Lakatos, S., Schmitt, B. & Cohen, R. (1980) Eur. J. Biochem 107, 389 - 394Google Scholar
  4. Batke, J., Nazaryan, K. B. & Karapetian, N. H. (1988) Arch. Biochem. Biophys 264, 510 - 518PubMedCrossRefGoogle Scholar
  5. Brocklehurst, K. (1977) Biochem. J 163, 111 - 116PubMedGoogle Scholar
  6. Bücher, T. & Klingenberg, M. (1958) Angew. Chem 70, 552 - 570CrossRefGoogle Scholar
  7. Clegg, J. S. (1984) Am. J. Physiol 246, R133 - R151PubMedGoogle Scholar
  8. Cleland, W. W. (1975) Acc. Chem. Res 8, 145 - 151CrossRefGoogle Scholar
  9. Cleland, W. W. (1977) Adv. Enzymol 45, 273 - 387PubMedGoogle Scholar
  10. Cornish-Bowden, A. (1987) Biochem. Educ. 15, 144 - 146CrossRefGoogle Scholar
  11. Crabtree, B. & Newsholme, E. A. (1985) Curr. Top. Cell. Regul. 25, 21-76Google Scholar
  12. Cseke, E. & Szabolcsi, G. (1983) Acta Biochim. Biophys. Acad. Sci. Hung 18, 151 - 161PubMedGoogle Scholar
  13. Cseke, E., Varadi, A., Szabolcsi, G. & Biszku, E. (1978) FEBS Lett. 96, 15 - 18PubMedCrossRefGoogle Scholar
  14. Damjanovich, S., Keleti, T. & Trón, L. (eds.) (1986) Dynamics of Biochemical Systems, Akadémiai Kiadó, Budapest, and Elsevier, AmsterdamGoogle Scholar
  15. Easterby, J. S. (1973) Biochim. Biophys. Acta 293, 552 - 558PubMedCrossRefGoogle Scholar
  16. Easterby, J. S. (1981) Biochem. J 199, 155 - 161PubMedGoogle Scholar
  17. Easterby, J. S. (1986) in Dynamics of Biochemical Systems (Damjanovich, S., Keleti, T. & Trion, L., eds.), Akadémiai Kiadó, Budapest and Elsevier, Amsterdam, pp. 145 - 158Google Scholar
  18. Fersht, A. (1977) Enzyme Structure and Mechanism. Freeman, San FranciscoGoogle Scholar
  19. Friedrich, P. (1984) Supramolecular Enzyme Organization. Quaternary Structure and Beyond, Pergamon Press, Oxford, and Akadémiai Kiadó, BudapestGoogle Scholar
  20. Friedrich, P., Apró-Kovacs, A. V. & Solti, M. (1977) FEBS Lett. 84, 183 - 186PubMedCrossRefGoogle Scholar
  21. Hanes, C. S. (1932) Biochem. J 26, 1406 - 1421PubMedGoogle Scholar
  22. Heinrich, R. & Rapoport, S. M. (1983) Biochem. Soc. Trans 11, 31 - 35PubMedGoogle Scholar
  23. Heinrich, R. & Rapoport, T. A. (1973) Acta Biol. Med. Germ 31, 479 - 494PubMedGoogle Scholar
  24. Heinrich, R. & Rapoport, T. A. (1974a) Eur. J. Biochem 42, 89 - 95PubMedCrossRefGoogle Scholar
  25. Heinrich, R. & Rapoport, T. A. (1974b) Eur. J. Biochem 42, 97 - 105PubMedCrossRefGoogle Scholar
  26. Heinrich, R., Rapoport, S. M. & Rapoport, T. A. (1977) Progr. Biophys. Molec. Biol. 32, 1-82Google Scholar
  27. Hess, B. & Wurster, B. (1970) FEBS Lett. 9, 73 - 77PubMedCrossRefGoogle Scholar
  28. Hohorst, H., Kreutz, F. H. & Bücher, T. (1959) Biochem. Z 332, 18 - 46PubMedGoogle Scholar
  29. Holzer, H., Schultz, G. & Lynen, F. (1956) Biochem. Z 328, 252 - 263PubMedGoogle Scholar
  30. Kacser, H. (1983) Biochem. Soc. Trans 11, 35 - 60PubMedGoogle Scholar
  31. Kacser, H. & Bums, J. A. (1973) Symp. Soc. Exp. Biol 27, 65 - 104PubMedGoogle Scholar
  32. Kacser, H. & Bums, J. A. (1979) Biochem. Soc. Trans 7, 1149 - 1160PubMedGoogle Scholar
  33. Keleti, T. (1975) in Mechanism of Action and Regulation of Enzymes (Keleti, T., ed.) Akadémiai Kiadó, Budapest, and North-Holland, Amsterdam. pp. 3 - 27Google Scholar
  34. Keleti, T. (1978) in New Trends in the Description of the General Mechanism and Regulation of Enzymes (Damjanovich, S., Elidi, P. & Somogyi, B., eds.) pp. 107 - 130, Akadémiai Kiadó, BudapestGoogle Scholar
  35. Keleti, T. (1981) in Kinetic Data Analysis (Endrényi, L., ed.) Plenum Press, New York, pp. 353 - 374CrossRefGoogle Scholar
  36. Keleti, T. (1984) in Dynamics of Biochemical Systems (Ricard, J. & Cornish-Bowden, A., eds.) pp. 103 - 114, Plenum Press, New YorkGoogle Scholar
  37. Keleti, T. (1986) Basic Enzyme Kinetics, Akadémiai Kiadó, BudapestGoogle Scholar
  38. Keleti, T. (1988) J. Mol. Catal. 47, 271-279Google Scholar
  39. Keleti, T. (1989) Nova Acta Leopoldina in pressGoogle Scholar
  40. Keleti, T. & Ovâdi, J. (1988) Curr. Top. Cell. Regul 29, 1 - 33PubMedGoogle Scholar
  41. Keleti, T. & Vértessy, B. (1986) in Dynamics of Biochemical Systems (Damjanovich, S., Keleti, T. & Trion, L., eds.) pp. 3 - 10, Akadémiai Kiadó, Budapest, and Elsevier, AmsterdamGoogle Scholar
  42. Keleti, T. & Welch, G. R. (1984) Biochem. J. 223, 299 - 303PubMedGoogle Scholar
  43. Keleti, T., Batke, J., Ovâdi, J., Jancsik, V. & Bartha, F. (1977) Adv. Enzyme Regul. 15, 233 - 265CrossRefGoogle Scholar
  44. Keleti, T., Ovâdi, J. & Batke, J. (1989a) Progr. Biophys. Mol. Biol. 53, 105-152Google Scholar
  45. Keleti, T., Berni, R., Vas, M., Mozzarelli, A. & Rossi, G. L. (1989b) Acta Biochim. Biophys. Hung 24, 15 - 23PubMedGoogle Scholar
  46. Knowles, J. R. (1976) FEBS Lett. 62 (Suppl.), E53 - E61PubMedCrossRefGoogle Scholar
  47. Koshland, D. E., Jr., Némethy, G. & Filmer, D. (1966) Biochemistry 5, 365 - 385PubMedCrossRefGoogle Scholar
  48. Krebs, H. A. & Veech, R. L. (1969) Adv. Enzyme Regul 7, 397 - 413PubMedCrossRefGoogle Scholar
  49. Lineweaver, H., Burk, D. (1934) J. Am. Chem. Soc 56, 658 - 666CrossRefGoogle Scholar
  50. Masters, C. J. (1981) CRC Crit. Rev. Biochem 11, 105 - 144PubMedCrossRefGoogle Scholar
  51. Michaelis, L. & Menten, M. L. (1913) Biochem. Z. 49, 333 - 369Google Scholar
  52. Monod, J., Wyman, J. & Changeux, J.-P. (1965) J. Mol. Biol 12, 88 - 118PubMedCrossRefGoogle Scholar
  53. Northrop, D. B. (1983) Anal. Biochem 132, 457 - 461PubMedCrossRefGoogle Scholar
  54. Grosz, F. & Ovâdi, J. (1986a) Eur. J. Biochem 160, 615 - 619CrossRefGoogle Scholar
  55. Grosz, F. & Ovâdi, J. (1986b) in Chromatography ’84 (Kalâsz, H. & Ettre, L., eds.) Elsevier, Amsterdam, and Akadémiai Kiadó, Budapest. pp. 425 - 434Google Scholar
  56. Grosz, F. & Ovâdi, J. (1987) Biochim. Biophys. Acta 915, 53 - 59CrossRefGoogle Scholar
  57. Grosz, F., Nuridsâny, M. & Ovâdi, J. (1986) J. Biochem. Biophys. Meth 13, 325 - 332CrossRefGoogle Scholar
  58. Grosz, F., Christova, T. Y. & Ovâdi, J. (1987) Biochem. Biophys. Res. Commun 147, 1121 - 1128CrossRefGoogle Scholar
  59. Grosz, F., Christova, T. Y. & Ovâdi, J. (1988a) Biochim. Biophys. Acta 95, 293 - 300Google Scholar
  60. Grosz, F., Christova, T. Y. & Ovâdi, J. (1988b) Mol. Pharmacol. 33, 678 - 682Google Scholar
  61. Ovâdi, J. (1986) in Dynamics of Biochemical Systems (Damjanovich, S., Keleti, T. & Trón, L., eds.). Akadémiai Kiadó, Budapest, and Elsevier, Amsterdam, pp. 203 - 216Google Scholar
  62. Ovadi, J. (1988) Trends Biochem. Sci 13, 486 - 490PubMedCrossRefGoogle Scholar
  63. Ovadi, J. (1989) Progr. Drug Res 33, 353 - 395CrossRefGoogle Scholar
  64. Ovâdi, J. & Keleti, T. (1978) Eur. J. Biochem 85, 157 - 161PubMedCrossRefGoogle Scholar
  65. Ovâdi, J., Salerno, C., Keleti, T. & Fasella, P. (1978) Eur. J. Biochem 90, 499 - 503PubMedCrossRefGoogle Scholar
  66. Ovâdi, J., Mohamed Osman, I. R. & Batke, J. (1983) Eur. J. Biochem 133, 433 - 437PubMedCrossRefGoogle Scholar
  67. Ovâdi, J., Mâtrai, Gy., Bartha, F. & Batke, J. (1985) Biochem. J 229, 57 - 62PubMedGoogle Scholar
  68. Ovâdi, J., Aragón, J. J. & Sols, A. (1986) Biochem. Biophys. Res. Commun 135, 852 - 856PubMedCrossRefGoogle Scholar
  69. Ovâdi, J., Tompa, P., Vértessy, B., Grosz, F., Keleti, T. & Welch, G. R. (1989) Biochem. J 257, 187 - 190PubMedGoogle Scholar
  70. Patthy, L. & Vas, M. (1978) Nature 276, 94 - 95PubMedCrossRefGoogle Scholar
  71. Reich, J. G. (1976) in Mathematical Models of Metabolic Regulation (Keleti, T. & Lakatos, S., eds.). Akadémiai Kiadó, Budapest, pp. 159 - 171Google Scholar
  72. Salerno, C. & Ovâdi, J. (1982) FEBS Lett. 138, 270 - 272PubMedCrossRefGoogle Scholar
  73. Salerno, C., Ovâdi, J., Churchich, J. & Fasella, P. (1975) in Mechanism of Action and Regulation of Enzymes (Keleti, T., ed.) Akadémiai Kiadó, Budapest and North-Holland, Amsterdam, pp. 147160Google Scholar
  74. Salerno, C., Ovâdi, J., Keleti, T. & Fasella, P. (1982) Eur. J. Biochem 121, 511 - 517PubMedCrossRefGoogle Scholar
  75. Savageau, M. A. (1972) Curr. Top. Cell. Regul 6, 63 - 130Google Scholar
  76. Savageau, M. A. (1976) Biochemical Systems Analysis: A Study of Function and Design in Molecular Biology, Addison-Wesley, Reading, MassachusettsGoogle Scholar
  77. Solti, M. & Friedrich, P. (1976) Mol. Cell. Biochem 10, 145 - 152PubMedCrossRefGoogle Scholar
  78. Solti, M. & Friedrich, P. (1979) Eur. J. Biochem 95, 551 - 559PubMedCrossRefGoogle Scholar
  79. Solti, M., Bartha, F., Halâsz, N., Tóth, G., Sirokmân, F. & Friedrich, P. (1981) J. Biol. Chem 256, 9260 - 9265PubMedGoogle Scholar
  80. Srere, P. A. (1987) Ann. Rev. Biochem 56, 21 - 56CrossRefGoogle Scholar
  81. Srivastava, D. K. &Bernhard, S. A. (1986) Curr. Top. Cell. Regul 28, 1 - 68PubMedGoogle Scholar
  82. Srivastava, D. K. & Bernhard, S. A. (1987) Ann. Rev. Biophys. Biophys. Chem. 16, 175-204 Szabolcsi, G. & Cseke, E. (1981) Acta Biol. Med. Germ 40, 471 - 477Google Scholar
  83. Tompa, P., Bär, J. & Batke, J. (1986) Eur. J. Biochem 159, 117 - 124PubMedCrossRefGoogle Scholar
  84. Tompa, P., Batke, J., Ovâdi, J., Welch, G. R. & Srere, P. A. (1987) J. Biol. Chem 262, 6089 - 6092PubMedGoogle Scholar
  85. Veech, R. L., Eggleston, L. V. & Krebs, H. A. (1969) Biochem. J 115, 609 - 619PubMedGoogle Scholar
  86. Veech, R. L., Raijman, L. & Krebs, H. A. (1970) Biochem. J 117, 499 - 503PubMedGoogle Scholar
  87. Vértessy, B. & Ovadi, J. (1987) Eur. J. Biochem 164, 655 - 659PubMedCrossRefGoogle Scholar
  88. Welch, G. R. (1977a) Progr. Biophys. Molec. Biol 32, 103 - 191CrossRefGoogle Scholar
  89. Welch, G. R. (19776) J. Theor. Biol. 68, 267-291Google Scholar
  90. Welch, G. R. (ed.) (1985) Organized Multienzyme Systems: Catalytic Properties, Academic Press, New YorkGoogle Scholar
  91. Welch, G. R. & Clegg, J. S. (eds.) (1986) The Organization of Cell Metabolism, Plenum Press, New YorkGoogle Scholar
  92. Welch, G. R. & Keleti, T. (1981) J. Theor. Biol 93, 701 - 735PubMedCrossRefGoogle Scholar
  93. Welch, G. R. & Keleti, T. (1987) Trends Biochem. Sci. 12, 216 - 217CrossRefGoogle Scholar
  94. Welch, G. R., Keleti, T. & Vértessy, B. (1988) J. Theor. Biol 130, 407 - 422PubMedCrossRefGoogle Scholar
  95. Westerhoff, H. V., Groen, A. K. & Wanders, R. J. A. (1984) Biosci. Rep 4, 1 - 22PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Tamás Keleti
    • 1
  1. 1.Institute of Enzymology, Biological Research CenterHungarian Academy of SciencesBudapestHungary

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