Anomeric specificity of glucose effect on cAMP, fructose 1,6-bisphosphatase, and trehalase in yeast.
The addition of beta-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 alpha-D-glucose. beta -D-Glucose was also more effective than alpha-D-glucose in the inactivation of fructose 1,6-bisphosphatase and the activation of trehalase. These results, taken together with the previous report that alpha-D-glucose is transported more rapidly than beta-D-glucose in Saccharomyces cerevisiae, do not support the view currently proposed by some investigators that cotransport of D-glucose with protons causes 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.
D000242:Cyclic AMP / Q000378:metabolism*; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005947:Glucose / Q000494:pharmacology*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D014198:Trehalase / Q000378:metabolism*
D000242:Cyclic AMP; D006597:Fructose-Bisphosphatase; D014198:Trehalase; D005947:Glucose