Abstract
The binding to yeast pyruvate base of Mn2+ has been determined from the enhancement of the proton relaxation rate which it causes. There were further changes in this enhancement in the presence of a substrate (phosphoenolpyruvate) and the effector (fructose diphosphate) and, from these changes, information was derived about their binding. Both strong and weak binding sites for Mn2+ on the enzyme were detected. The affinity of the enzyme for phosphoenolpyruvate was increased when the fructose diphosphate · Mn complex was bound to the enzyme. The proton relaxation enhancement results indicated that there were not more than two sites for fructose diphosphate · Mn, and two sites for phosphoenolpyruvate in the presence of the fructose diphosphate · Mn complex, but that there may have been more than two sites for phosphoenolpyruvate in the presence of Mn2+ only.
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