Advertisement

Channelling and Channel Efficiency: Theory and Analytical Implications

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

Abstract

Channelling of metabolites in a reaction sequence is accepted as the phenomenon where the reaction product of one enzyme is transferred directly to another enzyme as its substrate via transient enzyme-enzyme interactions (Srivastava & Bernhard, 1986, 1987). According to the Srivastava-Bernhard hypothesis such a “one-encounter-type metabolite transfer” can occur if the heterologous enzyme complex associates and dissociates during every catalytic turnover of enzymes. Alternatively, an intermediate can be also channelled if its liberation from the active site of one enzyme is followed by direct transfer to the active site of the next enzyme in the sequence without diffusing into the bulk solution (Srere, 1987; Welch, 1985, Keleti & Ovádi, 1988, and references therein; see also Chapter 21 by Keleti in this book). Both mechanisms of intermediate transfer may result in physiological advantages to an organism, such as (i) segregation of competing pathways by microcompartmentation of intermediates, (ii) reduction of the time required to reach the steady state, and (iii) enhancement of metabolite flux by providing high local metabolite concentrations. A new description of the channelling effect has been elaborated (Tompa et al., 1987) based on inherent parameters such as channel efficiency and intermediate lifetime. These inherent parameters, together with the analytical implications, will be discussed in this chapter. In addition, some examples will be presented to illustrate how the mechanism of intermediate transfer in interacting enzyme systems can be determined and how dynamic channelling complexes of enzymes can be specifically modulated.

Keywords

Glutamate Dehydrogenase Transient Time Triose Phosphate Isomerase Triose Phosphate Dihydroxyacetone Phosphate 
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. Boscâ, L., Aragón, J.J. and Sols, A. (1983) J. Biol. Chem. 269, 2100–2107Google Scholar
  2. Chock, P.B. and Gutfreund, H (1988) Proc. Natl. Acad. Sci. USA 85, 8870–8874PubMedCrossRefGoogle Scholar
  3. Easterby, J.S. (1981) Biochem. J. 199, 155–161PubMedGoogle Scholar
  4. Easterby, J.S. (1984) Biochem. J. 219, 843–847PubMedGoogle Scholar
  5. Grazi, E. and Trombetta, G. (1980) Eur. J. Biochem. 107, 369–373PubMedCrossRefGoogle Scholar
  6. Hess, B. and Wurster, B. (1970) FEBS Lett. 9 ,73–77Google Scholar
  7. Keleti, T. and Ovâdi, J. (1988) Curr. Top. Cell Reg. 29, 1–33Google Scholar
  8. Keleti, T., Batke, J., Ovâdi, J., Jancsik, V. and Bartha, F. (1977) Adv. Enzyme Regul. 15,233–265Google Scholar
  9. Kvassman, J., Petterson, G. and Ryde-Petterson, U. (1988) Eur. J. Biochem. 172, 427–431PubMedCrossRefGoogle Scholar
  10. Masters, C. (1981) CRC Crit. Rev. Biochem. 11, 105–144PubMedCrossRefGoogle Scholar
  11. Mayr, G.W. (1984) Eur. J. Biochem. 143, 513–520PubMedCrossRefGoogle Scholar
  12. Orosz, F., Christova, T.Y. and Ovâdi, J. (1987) Biochem. Biophys. Res. Comm. 147,1121–1128 Orosz, F., and Ovâdi, J. (1987) Biochim. Biophys. Acta 915,53–59Google Scholar
  13. Orosz, F., Christova, T.Y. and Ovâdi, J. (1988a) Biochim. Biophys Acta 957, 293–300PubMedCrossRefGoogle Scholar
  14. Orosz, F., Christova, T.Y. and Ovâdi, J. (1988b) Molec. Pharm. 33, 678–682PubMedGoogle Scholar
  15. Ovâdi, J. (1986) in Dynamics of Biochemical Systems (Damjanovich, S., Keleti, T. and Trón, L., eds.), pp. 203–216, Akadémiai Kiadó, Budapest, and Elsevier, AmsterdamGoogle Scholar
  16. Ovâdi, J. (1988) Trends Biochem. Sci. 13, 486–490PubMedCrossRefGoogle Scholar
  17. Ovâdi, J. and Keleti, T. (1978) Eur. J. Biochem. 85, 157–161PubMedCrossRefGoogle Scholar
  18. Ovâdi, J., Aragón, J.J. and Sols, A. (1986) Biochem. Biophys. Res. Comm. 135, 852–856PubMedCrossRefGoogle Scholar
  19. Ovâdi, J., Salerno, C., Keleti, T. and Fasella, P (1978) Eur. J. Biochem. 90, 499–503PubMedCrossRefGoogle Scholar
  20. Ovâdi, J., Tompa, P., Vértessy, B., Orosz, F., Keleti, T. and Welch, G.R. (1989) Biochem. J. 257, 187–190PubMedGoogle Scholar
  21. Patthy, L. and Vas, M. (1978) Nature 276, 274–276CrossRefGoogle Scholar
  22. Salerno, C., Ovâdi, J., Keleti, T. and Fasella, P. (1982) Eur. J. Biochem. 121, 511–517PubMedCrossRefGoogle Scholar
  23. Srere, P.A. (1967) Science 158, 936–937PubMedCrossRefGoogle Scholar
  24. Srere, P.A. (1987) Annu. Rev. Biochem. 56, 89–124PubMedCrossRefGoogle Scholar
  25. Srivastava, D.K. and Bernhard, S.A. (1987) Ann. Rev. Biophys. Biophys. Chem. 16, 175–204 Srivastava, D.K. and Bernhard, S.A. (1986) Curr. Top. Cell. Reg. 28, 1–68Google Scholar
  26. Tompa, P., Batke, J. and Ovâdi, J. (1987) FEBS Lett. 214, 244–248PubMedCrossRefGoogle Scholar
  27. Vértessy, B. and Ovâdi, J. (1987) EurJ.Biochem 164, 655–659CrossRefGoogle Scholar
  28. Welch, G.R. (ed.) (1985) Organized Multienzyme Systems: Catalytic Properties, Academic Press, New YorkGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Judit Ovádi
    • 1
  1. 1.Institute of Enzymology, Biological Research CenterHungarian Academy of SciencesBudapestHungary

Personalised recommendations