title: In vivo glucose activation of the yeast plasma membrane ATPase.
abstract: 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.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D005632:Fructose / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates / Q000494:pharmacology; D019807:Iodoacetic Acid; D008358:Mannose / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D007461:Iodoacetates; D005632:Fructose; D000251:Adenosine Triphosphatases; D005947:Glucose; D008358:Mannose; D019807:Iodoacetic Acid