In vivo glucose activation of the yeast plasma membrane ATPase

FEBS Lett. 1983 May 30;156(1):11-4. doi: 10.1016/0014-5793(83)80237-3.


The addition of glucose to yeast cells activates proton efflux mediated by the plasma membrane ATPase. Accordingly, the ATPase activity of purified plasma membranes is increased up to 10-fold. The activated ATPase has a more alkaline pH optimum, better affinity for ATP and greater sensitivity to vanadate than the non-activated enzyme. All these changes are reversed by washing the cells free of glucose. This suggests two states of the ATPase which are interconverted by a covalent modification. As glucose does not affect the phosphorylation of plasma membrane polypeptides, other type of covalent modification may be involved.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Cell Membrane / enzymology
  • Enzyme Activation / drug effects
  • Fructose / pharmacology
  • Glucose / pharmacology*
  • Hydrogen-Ion Concentration
  • Iodoacetates / pharmacology
  • Iodoacetic Acid
  • Mannose / pharmacology
  • Saccharomyces cerevisiae / enzymology*


  • Iodoacetates
  • Fructose
  • Adenosine Triphosphatases
  • Glucose
  • Mannose
  • Iodoacetic Acid