Assocaiations between glycolytic enzymes and subscellular structures have been interpreted as presenting a novel mechanism of glycolytic control; reversible enzymes binding to subcellular structural components is believed to regulate enzymes activity in vivo through the formation of a multi-enzyme complex. However, three lines of evidence suggest that eyzyme binding to cellular structures is not involved in the control of glycolsis, (i) Calculations of the distribution of glycolytic enzymes under the physiological cellular conditions of higher ionic strenght and higher enzyme concentrations indicate that a large multi-enzyme complex would not exist, (ii) In many eases, binding to subcellular structures is accompanied by changes in enzyme kinetic parameters brought about by allosteric modification, but these changes often inhibit enzyme activity, (iii) In the case where formation of binary enzyme/enzyme complexes activates enzymes, the overall increase in flux through the enzyme reaction is negible.

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FEBS Letters
Department of Biology

Brooks, S.P.J., & Storey, K. (1991). Where is the glycolytic complex? A critical evaluation of present data from muscle tissue. FEBS Letters (Vol. 278, pp. 135–138). doi:10.1016/0014-5793(91)80101-8