Macromolecular interactions in enzyme regulation

T. Keleti, J. Batke, J. Ovádi, V. Jancsik, F. Bartha

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The differences observed by several authors in the NaDH-binding ability of the subunits of glyceraldehyde-3-phosphate dehydrogenase are caused by the dissociation of the enzyme. A specific model has been elaborated for the interpretation of the phenomenon; the earlier interpretation in terms of ligand-induced negative cooperatively seems to be erroneous. In the regulation of the reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase in the glycolytic pathway the association-dissociation dynamics of the enzyme play the decisive role. In the higher aggregational forms of the enzyme the relative concentration of "functioning active centres" progressively decrease and this may furnish the basis for a novel type of regulatory mechanism. Aldolase forms a complex with glyceraldehyde-3-phosphate dehydrogenase (presumably with the dimeric form) thereby enhancing the activity of the latter. This finding calls the attention to the importance of enzyme-enzyme interactions in the intracellular metabolic regulation. The modelling of enzyme-other macromolecule interactions was performed by studying the behavior of aldolase and glyceraldehyde-3-phosphate dehydrogenase in the solution of synthetic polymers. The change of kinetic parameters suggests that the interaction induces conformational alterations in the enzymes. The kinetic consequences of structural changes depend not only on the enzyme, but also on the structure of the polymer.

Original languageEnglish
Pages (from-to)233-265
Number of pages33
JournalAdvances in Enzyme Regulation
Issue numberC
Publication statusPublished - 1977


ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Genetics
  • Cancer Research

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