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• W2038616879 abstract "We have studied the kinetics of the allosteric interactions of pyruvate kinase from Trypanosoma brucei. The kinetics for phosphoenolpyruvate depended strongly on the nature of the bivalent metal ions. Pyruvate kinase activated by Mg2+ had the highest catalytic activity, but also the highest S0.5 for phosphoenolpyruvate, while the opposite was true for pyruvate kinase activated by Mn2+. The reaction rates of Mg2+ -pyruvate kinase and Mn2+ -pyruvate kinase were clearly allosteric with respect to phosphoenolpyruvate, while the kinetics with Co2+ -pyruvate kinase were hyperbolic. However, Co2+ -pyruvate kinase was still sensitive to heterotropic activation. Trypanosomal pyruvate kinase is unique in that the best activator was fructose 2,6-bisphosphate. Ribulose 1,5-bisphosphate and 5-phosphorylribose 1-pyrophosphate were also strong heterotropic activators, which were much more effective than fructose 1,6-bisphosphate and glucose 1,6-bisphosphate. In the presence of the heterotropic activators, the sigmoidal kinetics with respect to phosphoenolpyruvate and the bivalent metal ions were modified as were the concentrations of phosphoenolpyruvate and the bivalent metal ions needed to attain the maximal activity. Maximal activities were not significantly changed with Mg2+ and Mn2+ as the activating metal ions. Moreover, with Co2+ and fructose 2,6-bisphosphate or ribulose 1,5-bisphosphate or 5-phosphorylribose 1-pyrophosphate, the maximal activity was significantly reduced. Ribulose 1,5-bisphosphate and 5-phosphorylribose 1-pyrophosphate resembled fructose 2,6-bisphosphate rather than fructose 1,6-bisphosphate and glucose 1,6-bisphosphate in their action in that the K0.5 values for the former 3 compounds increased when Mg2+ was replaced by Co2+, while the K0.5 for fructose 1,6-bisphosphate and glucose 1,6-bisphosphate increased. The effect of pH on the cooperativity of the reaction rate of pyruvate kinase from T. brucei towards phosphoenolpyruvate and fructose 2,6-bisphosphate was unique. At alkaline pH the positive cooperativity in the conversion of phosphoenolpyruvate was abolished while the apparent affinity for phosphoenolpyruvate was not altered and the enzyme was still sensitive to heterotropic activation. Optimal catalysis occurred at pH 6.0. At acidic pH the velocity versus fructose 2,6-bisphosphate concentration curve became sigmoidal and the activation constant increased. Between 15′C and 37′C, temperature did not influence the kinetic properties of Mg2+ -pyruvate kinase with respect to phosphoenolpyruvate." @default.
• W2038616879 created "2016-06-24" @default.
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• W2038616879 date "1992-02-01" @default.
• W2038616879 modified "2023-09-30" @default.
• W2038616879 title "Some kinetic properties of pyruvate kinase from Trypanosoma brucei" @default.
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• W2038616879 doi "https://doi.org/10.1016/0166-6851(92)90220-e" @default.
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