Anomeric specificity of glucose effect on cAMP, fructose 1,6-bisphosphatase, and trehalase in yeast

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Abstract

The addition of β -D-glucose (final concentration, 50 mM) to a cell suspension of Saccharomyces cerevisiae in stationary phase caused a rapid 4-fold increase in the concentration of cAMP, while a 2-fold increase of cAMP was observed by the addition of α -D-glucose. β -D-Glucose was also more effective than α -D-glucose in the inactivation of fructose 1,6-bisphosphatase and the activation of trehalase. These results, taken together with the previous report that α -D-glucose is transported more rapidly than β -D-glucose in Saccharomyces cerevisiae, do not support the view currently proposed by some investigators that cotransport of D-glucose with protons cause the depolarization of the cell membrane, resulting in the activation of adenylate cyclase. The present data, however, provides supporting evidence for the view that cAMP-dependent protein kinase is implicated in the inactivation of fructose 1,6-bisphosphatase and the activation of trehalase.

References (27)

  • J.B. Van der Plaat

    Biochem. Biophys. Res. Commun

    (1974)
  • H. Holzer

    Trends Biochem. Sci

    (1976)
  • A.-G. Lenz et al.

    FEBS Lett

    (1980)
  • Y. Toyoda et al.

    J. Biol. Chem

    (1984)
  • W. Pigman et al.

    Adv. Carbohyd. Chem

    (1968)
  • J. Okuda

    Trends Biochem. Sci

    (1978)
  • M. Bradford

    Anal. Biochem

    (1976)
  • M.J. Mazon et al.

    Eur. J. Biochem

    (1982)
  • H. Holzer
  • J.M. Thevelein

    J. Bacteriol

    (1984)
  • J.M. Thevelein

    Microbiol. Rev

    (1984)
  • J. Francosis et al.

    Eur. J. Biochem

    (1984)
  • P. Tortora et al.

    Eur. J. Biochem

    (1984)
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