Advertisement

Zero-order Ultrasensitivity in Interconvertible Enzyme Systems

  • Albert Goldbeter
  • Daniel E. KoshlandJr.
Chapter
Part of the NATO ASI Series book series (NSSA, volume 190)

Abstract

How to generate thresholds is an important question in cellular metabolism as well as in other fields of biology. Thresholds are essential if large changes in response are to be elicited by relatively small changes in stimulus, i.e. substrate or effector in the case of enzymes (Koshland et al., 1982). An important role is nevertheless retained in metabolic systems by other reactions in the pathway since these will determine whether any abrupt change is propagated beyond the threshold-generating step. Control of flux indeed appears to be distributed over the various steps of a pathway (Kacser & Bums, 1973; Westerhoff et al., 1984). The reversible shutting down of the flux above a suprathreshold stimulation should, however, prove a most efficient way of generating sharp transitions under steady-state conditions.

Keywords

Converter Enzyme Covalent Modification Hill Coefficient Dual Control Threshold Phenomenon 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Cárdenas, M. L. & Cornish-Bowden, A. (1989) Biochem. J. 257, 339–345PubMedGoogle Scholar
  2. Chock, P. B. & Stadtman, E. R. (1977) Proc. Natl. Acad. Sci. USA 74, 2766–2770PubMedCrossRefGoogle Scholar
  3. Cohen, P. (1983) Phil. Trans. Roy. Soc. Lond. B 302, 13–25CrossRefGoogle Scholar
  4. Degn, H. (1968) Nature 217, 1047–1050PubMedCrossRefGoogle Scholar
  5. Eschrich, K., Schellenberger, W. & Hofmann, E. (1980) Arch. Biochem. Biophys. 205, 114–121PubMedCrossRefGoogle Scholar
  6. Goldbeter, A. & Koshland, D. E., Jr. (1981) Proc. Natl. Acad. Sci. USA 78, 6840–6844PubMedCrossRefGoogle Scholar
  7. Goldbeter, A. & Koshland, D. E., Jr. (1982) Quart. Rev. Biophys. 15, 555–591CrossRefGoogle Scholar
  8. Goldbeter, A. & Koshland, D. E., Jr. (1984) J. Biol. Chem. 259, 14441–14447PubMedGoogle Scholar
  9. Goldbeter, A. & Koshland, D. E., Jr. (1987) J. Biol. Chem. 262, 4460–4471PubMedGoogle Scholar
  10. Hunter, T. (1987) Cell 50, 823–829PubMedCrossRefGoogle Scholar
  11. Kacser, H. & Burns, J. A. (1973) Symp. Soc. Exper. Biol. 27, 65–104Google Scholar
  12. Koshland, D. E., Jr., Némethy, G. & Filmer, D. (1966) Biochemistry 5, 365–385 Google Scholar
  13. Koshland, D. E., Jr., Goldbeter, A. & Stock, J. B. (1982) Science 217, 220–225PubMedCrossRefGoogle Scholar
  14. Krebs, E. G. & Beavo, J. A. (1979) Annu. Rev. Biochem. 48, 923–959PubMedCrossRefGoogle Scholar
  15. LaPorte, D. C. & Koshland, D. E., Jr. (1983). Nature 305, 386–290CrossRefGoogle Scholar
  16. Lefkowitz, R. J. & Caron, M. G. (1986) J. Mol. Cell. Cardiol. 18, 885–895PubMedCrossRefGoogle Scholar
  17. Levitan, I. B. (1985) J. Membr. Biol. 87, 177–190PubMedCrossRefGoogle Scholar
  18. Magasanik, B. (1988) Trends Biochem. Sci. 13, 475–479PubMedCrossRefGoogle Scholar
  19. Meinke, M. H., Bishop, J. S. & Edstrom, R. D. (1986) Proc. Natl. Acad. Sci. USA 83, 2865–2868PubMedCrossRefGoogle Scholar
  20. Monod, J., Wyman, J. & Changeux, J.-P. (1965) J. Mol. Biol. 12, 88–118PubMedCrossRefGoogle Scholar
  21. Naparstek, A., Romette, J. L., Kemevez, J. P. & Thomas, D. (1973) Nature 249, 490–491CrossRefGoogle Scholar
  22. Nestler, E. J. & Greengard, P. (1984) Protein Phosphorylation in the Nervous System, Wiley, New YorkGoogle Scholar
  23. Rhee, S. G., Chock, P. B. & Stadtman, E. R. (1989) Adv. Enzymol. 62, 37–92PubMedGoogle Scholar
  24. Shacter, E., Chock, P. B. & Stadtman, E. R. (1984a)J. Biol. Chem. 259, 12252–12259Google Scholar
  25. Shacter, E., Chock, P. B. & Stadtman, E. R. (1984b)J. Biol. Chem. 259, 12260–12264Google Scholar
  26. Stadtman, E. R. & Chock, P. B. (1977) Proc. Natl. Acad. Sci. USA 74, 2761–2765PubMedCrossRefGoogle Scholar
  27. Stadtman, E. R. & Chock, P. B. (1978) Curr. Topics Cell. Reg. 13, 53–95Google Scholar
  28. Taketa, K. & Pogell, B. M. (1965) J. Biol. Chem. 240, 651–652PubMedGoogle Scholar
  29. 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

  • Albert Goldbeter
    • 1
  • Daniel E. KoshlandJr.
    • 2
  1. 1.Faculté des SciencesUniversité Libre de BruxellesBrusselsBelgium
  2. 2.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA

Personalised recommendations