Abstract
Oxalate dianion exerts a dual effect on allosteric liver and erythrocyte pyruvate kinases. In the absence of fructose 1,6 bisphosphate and at phosphoenolpyruvate concentrations lower than K 0.5s, oxalate apparently behaves as an allosteric activator. In the presence of fructose 1,6 bisphosphate and at higher phosphoenolpyruvate concentrations, oxalate is a powerful competitive inhibitor with respect to phosphoenolpyruvate. Such properties are consistent with the allosteric model of Monod-Wyman-Changeux for a substrate analogue. Inhibition constants of oxalate towards pyruvate kinase are in the same order of magnitude as blood oxalate concentration.
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