Abstract
WE have described how fructose-1,6-diphosphate (FDP) is a strong activator of yeast pyruvate kinase1. During more detailed investigations of the steady state kinetics of the enzyme we found that the FDP-activation strongly interferes with the activation of the enzyme by ammonium as well as by potassium ions. The activation of the enzyme by both ions has been previously described for the muscle enzyme2 and for the yeast enzyme3 (refs. 3 and 4 and personal communication from C. H. Suelter).
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References
Hess, B., Haeckel, R., and Brand, K., Biochem. Biophys. Res. Commun., 24, 824 (1966).
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Kachmar, J. F., and Boyer, P. D., J. Biol. Chem., 200, 669 (1953).
Suelter, C. H., Singleton, R., Kayne, F. J., Arrington, S., Glass, J., and Mildvan, A. S., Biochemistry, 5, 131 (1966).
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HESS, B., HAECKEL, R. Interaction between Potassium-, Ammonium- and Fructose-1,6-diphosphate Activation of Yeast Pyruvate Kinase. Nature 214, 848–849 (1967). https://doi.org/10.1038/214848a0
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DOI: https://doi.org/10.1038/214848a0
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