Skip to main content
Log in

Glycolysis — new concepts in an old pathway

  • Review
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

A survey of the existing data on the interactions of glycolytic enzymes with the cellular structure in mammalian tissues has substantiated the occurrence of an extensive degree of such associations in all tissues and during all stages of development. Furthermore, a considerable specificity was evident between the individual multiple forms of the enzymes in relation to these associations.

In reviewing these data, a model has been developed which proposes that the glycolytic sequence is best described as consisting of a number of segments in vivo, each segment formed by a cluster of isozymes, many of which can interact with the actin containing filaments of the cytomatrix. The novel features of this segmentation and compartmentation have been described, and evidence has been provided that these phenomena collectively play a key role in meeting the different types of energy requirement in the cytoplasm of divergent cell types, with the wide selection of isozymes in this system offering the potential for increased flexibility and control in this important area of metabolism.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Lehniger AL: Biochemistry. Worth Publishers Inc, New York, 1975, pp 417–441

    Google Scholar 

  2. Clarke FM, Masters CJ: On the reversible adsorption of aldolase to microsomal membrane fraction from rat brain. Int J Biochem 6:133–145, 1975

    Google Scholar 

  3. Kuter MR, Masters CJ, Winzor DJ: Equilibrium partition studies of the interaction between aldolase and myofibrils. Arch Biochem Biophys 225:384–389, 1983

    Google Scholar 

  4. Clarke FM, Masters CJ: Interactions between muscle proteins and glycolytic enzymes. Int J Biochem 7:359–365, 1976

    Google Scholar 

  5. Walsh TP, Clarke FM, Masters CJ: Modification of the kinetic parameters of aldolase on binding to actin containing filaments of muscle. Biochem J 165:165–167, 1977

    Google Scholar 

  6. Sigel P, Pette D: Intracellular localization of glycogenolytic and glycolytic enzymes in white and red rabbit muscle. A gel film for couple enzyme reactions in histochemistry. J Histochem Cytochem 17:225–237, 1969

    Google Scholar 

  7. Masters CJ: The ontogenic characteristics of lactate dehydrogenase isozymes in mammalian preimplantation ova. Mech Aging Dev 7:455–464, 1978

    Google Scholar 

  8. Turner DC, Eppenberger HM: Developmental changes in creatine kinase and aldolase isoenzymes and their possible function in association with contractile elements. Enzyme 15:224–238, 1973

    Google Scholar 

  9. Clegg J: Properties and metabolism of the aqueous cytoplasm and its boundaries. Am J Physiol 246:R133-R151, 1984

    Google Scholar 

  10. Humphrey L, Masters CJ: On the differential release of glycolytic enzymes from cellular structure. Biochem Inter 13:71–78, 1986

    Google Scholar 

  11. Reid S, Masters CJ: On the ontogeny of aldolase isozymes and their interactions with cellular structure. Mech Ageing Devel 30:299–317, 1985

    Google Scholar 

  12. Reid S, Masters CJ: On the developmental properties and tissue interactions of hexokinase. Mech Age Develop 31:197–212, 1985

    Google Scholar 

  13. Reid S, Masters CJ: Ontogenic variations in the interactions of lactate dehydrogenase isozymes with cellular structure. Mec Ageing Develop 31:69–88, 1985

    Google Scholar 

  14. Masters CJ: Interactions between soluble enzymes and subcellular structure. CRC Rev Biochem 11:105–143, 1981

    Google Scholar 

  15. Masters CJ: Interactions between glycolytic enzymes and the cytomatrix. J Cell Biol 99:222–225, 1984

    Google Scholar 

  16. Poglazov BF, Livanova NB: Interactions of actin with the enzymes of carbohydrate metabolism. Advances in Enzyme Regulation 25:297–305, 1985

    Google Scholar 

  17. Arnold H, Pette D: Binding of aldolase and triosephosphate dehydrogenase to F-actin and modification of catalytic properties of aldolase. Eur J Biochem 15:360–366, 1970

    Google Scholar 

  18. Karadsheh NS, Uyeda K: Changes in allosteric properties of phosphofructokinase bound to erythrocyte membranes. J Biol Chem 252:7418–7420, 1977

    Google Scholar 

  19. Clarke FM, Masters CJ: Reversible and selective adsorption of aldolase isonenzymes in rat brain. Arch Biochem Biophys 153:258–265, 1972

    Google Scholar 

  20. Kliman HJ, Steck TL: Association of G3PDH with the human red cell membrane; a kinetic analysis. J Biol Chem 255:6314–6321, 1980

    Google Scholar 

  21. Humphreys L, Reid S, Masters CJ: Evidence for the spatial separation of the binding sites for substrate and for cytoskeletal proteins on the enzyme aldolase. Int J Biochem 18:7–13, 1986

    Google Scholar 

  22. Humphreys L, Reid S, Masters CJ: Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehyde phosphate dehydrogenase and phosphofructokinase. Int J Biochem 18:445–451, 1986

    Google Scholar 

  23. Wilson JE: Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism. Trends Biochem Sci 3:124–126, 1978

    Google Scholar 

  24. Wilson JE: Brain hexokinase, the prototype ambiquitous enzyme. Cur Topics Cell Reguln 16:1–54, 1980

    Google Scholar 

  25. Bradley TJ, Satis P: Evidence of microfilament — associated mitochondrial movement. J Supramolecular Structure 12:165–175, 1979

    Google Scholar 

  26. Pardo JV, Pittenger MF, Craig SW. Subcellular sorting of isoactins: selective association of γ actin with skeletal muscle mitochondria. Cell 32:1093–1103, 1983

    Google Scholar 

  27. Luca MD, Kricka LJ: Commobilized multienzymes: An in vitro model for cellular processes. Arch Biochem Biophys 226:285–291, 1983

    Google Scholar 

  28. Stephan P, Clarke FM, Morton DJ: The indirect binding of triose-phosphate isomerase to myofibrils to form a glycolytic mini-complex. Biochem Biophys Acta 873:127–135, 1986

    Google Scholar 

  29. Sies H: Introductory remarks. In: Sies H (ed) Metabolic Compartmentation. Academic Press Inc, New York, 1982

    Google Scholar 

  30. Fothergill-Gilmore L: The evolution of the glycolytic pathway. Trends Biochem Sci 11:47–51, 1986

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Masters, C.J., Reid, S. & Don, M. Glycolysis — new concepts in an old pathway. Mol Cell Biochem 76, 3–14 (1987). https://doi.org/10.1007/BF00219393

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00219393

Key words

Navigation