Implications of Metabolic Compartmentation in Prokaryotic Cells

  • V. Moses
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 127)


Contemplation of the sheer complexity of cellular metabolism, coupled with the realization that in bacterial cells it all takes place in a minute volume exhibiting a minimum of cellular architectural detail, soon begins to prompt questions about the nature of intracellular organization in prokaryotic cells. The very absence of membrane-bounded organelles suggests that, aside from reactions localized in or about the cell membrane, organizational structure is likely to be based on direct macromolecular interactions. These would yield macro structures which in some cases might also act in a more-or-less compartmentalized fashion, leading to the separate channelling of whole series of sequential reactions. There is some variation in the way in which the terms “compartment” and “channel” are used. In the present contribution a “channel” is defined as a structure or a facet of organization which acts as a constraint to free chemical diffusion. A “compartment” is a sequestered volume; it may be similar to a channel. Any defined aspect of biochemical organization may represent a compartment so long as it remains chemically inactive. For example, a ligand bound to an enzyme is in a compartment until it undergoes a reaction.


Glycolytic Enzyme Tricarboxylic Acid Cycle Triosephosphate Isomerase Proline Biosynthesis Proline Synthesis 
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. Atkinson, D.E., 1969, Curr, Top Cell. Regul., 1:29.Google Scholar
  2. Barnes, S. and Weitzman, P.D.J., 1985, This volume.Google Scholar
  3. Bearden, L. and Moses, V., 1972, Biochim. Biophys. Acta., 279:513.PubMedCrossRefGoogle Scholar
  4. Gamper, H. and Moses, V., 1974, Biochim. Biophys. Acta, 354:75.PubMedCrossRefGoogle Scholar
  5. Garrib, A., 1983, Ph.D. Thesis, University of London: “The enzymes of proline biosynthesis in Escherichia coli and Proteus mirabillis”.Google Scholar
  6. Gorringe, D.M. and Moses, V., 1980, Int. J. Biol. Macromol., 2:161.CrossRefGoogle Scholar
  7. Hayzer, D.J. and Moses, V., 1978, Biochem. J., 173:219.PubMedGoogle Scholar
  8. Katchalsky, A. and Paecht, M., 1954, J. Amer. Chem. Soc., 76:6042.CrossRefGoogle Scholar
  9. Kingdon, C.F.M., 1983, Ph.D. Thesis, University of London: “The status of glycolytic organization in Escherichia coli”.Google Scholar
  10. Ling, G.N. and Cope, F.W., 1969, Science. 163:1335.PubMedCrossRefGoogle Scholar
  11. Macnab, R., Moses, V. and Mowbray, J., 1973, Eur. J. Biochem., 34:15.PubMedCrossRefGoogle Scholar
  12. Manney, T.R., 1970, J. Bacteriol.. 102:483.PubMedGoogle Scholar
  13. McBrien, D.C.H. and Moses, V., 1968, J. Gen. Microbiol., 51:159.PubMedGoogle Scholar
  14. Moses, V. and Lonberg-Holm, K.K., 1968, J. Theor. Biol., 10:336.CrossRefGoogle Scholar
  15. Mowbray, J. and Moses, V., 1976, Eur. J. Biochem.. 66:25.PubMedCrossRefGoogle Scholar
  16. Pflugfelder, M., Adams, B., and Kirschner, K., 1985, Abstracts of the 24th Harden Conference, 19.Google Scholar
  17. Sols, A. and Marco, R., 1970, Curr, Top Cell. Regul., 2:227.Google Scholar
  18. Strecker, H.J., 1960. J. Biol. Chem., 235:2045.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • V. Moses
    • 1
  1. 1.School of Biological SciencesQueen Mary College (University of London)LondonUK

Personalised recommendations