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Interaction between Potassium-, Ammonium- and Fructose-1,6-diphosphate Activation of Yeast Pyruvate Kinase

Nature volume 214, pages 848–849 (1967)Cite this article

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

  1. Hess, B., Haeckel, R., and Brand, K., Biochem. Biophys. Res. Commun., 24, 824 (1966).

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  2. Boyer, P. D., Lardy, H. A., and Philipp, P. H., J. Biol. Chem., 146, 673 (1942).

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  6. Suelter, C. H., Singleton, R., Kayne, F. J., Arrington, S., Glass, J., and Mildvan, A. S., Biochemistry, 5, 131 (1966).

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Authors and Affiliations

  1. Max-Planck-Institut für Ernährungsphysiologie, 46, Dortmund

    BENNO HESS & RAINER HAECKEL

Authors
  1. BENNO HESS
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  2. RAINER HAECKEL
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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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