The effect of changing concentrations of glycolytic intermediates on the binding of phosphofructokinase, aldolase and pyruvate kinase to cellular particulate matter was investigated. Concentrations of glycolytic intermediates were altered by adding 2mM iodoacetic acid (IAA) to an incubation medium containing tissues isolated from the channelled whelk Busycon canaliculatum. Iodoacetic acid inhibited glyceraldehyde 3-phosphate dehydrogenase activity causing a 100-400 fold increase in the concentration of fructose 1,6-bisphosphate as well as 3-20 fold increases in glucose 6-phosphate, fructose 6-phosphate, and dihydroxyacetone phosphate levels depending on the experimental protocol. Cellular pH values were not statistically different in the presence of IAA. Measurement of enzyme binding to particulate matter showed that the binding of phosphofructokinase, aldolase and pyruvate kinase was unaffected by iodoacetic acid under any experimental conditon. These results show that changes in the tissue concentrations of enzyme substrates and products do not regulate enzyme binding to particulate matter in the cell. (Mol Cell Biochem 122: 1-7, 1993)

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Keywords enzyme binding, enzyme regulation, glycolytic enzyme complex, inhibition of glycolysis, metabolism
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Journal Molecular and Cellular Biochemistry
Brooks, S.P.J. (Stephen P.J.), & Storey, K. (1993). Control of glycolytic enzyme binding: effect of changing enzyme substrate concentrations on in vivo enzyme distributions. Molecular and Cellular Biochemistry, 122(1), 1–7. doi:10.1007/BF00925731