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Vacuoles of the Saccharomyces cerevisiae yeast possess a polyphosphatase activity which differs from other known vacuolar phosphohydrolase activities by pH-optimum, sensitivity towards inhibitors and distribution between the tonoplast and vacuolar sap. The polyphosphatase activity is inhibited by EDTA, molybdate, ortho-vanadate and fluoride. Nearly 77% of this activity is located in the vacuolar sap, while 25%--in the tonoplast fraction. Both the soluble and membrane-bound polyphosphatase activities are maximal at pH 6.8-7.2. Bivalent metal cations stimulate this activity in the following order: Zn2+ > Mg2+ > Co2+ > Mn2+. Other ions (Fe2+, Cu2+, Ca2+) inhibit this activity at all concentrations tested. The polyphosphatase activity of both the vacuolar sap and the tonoplast increases 2.4-and 2-fold, respectively, with an increase in the degree of substrate polymerization--from n = 3 to n = 208.
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