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The ATPase activity of whole cells of anaerobically grown Saccharomyces carlsbergensis was low, but EDTA or glucose revealed ATPase activity. The ATPase was activated by Mg++ and Ca++; excess Ca++ was inhibitory. The optimum pH was 8·0 and optimum temperature about 40° C. The enzyme liberated less than two moles of phosphate from one mole of ATP and other nucleoside triphosphates and released phosphate slowly from ADP; nucleoside monophosphates were not hydrolysed. The enzyme was inhibited by atebrin, sodium azide and ADP, but was unaffected by ouabain, sodium fluoride or 2,4-dinitrophenol.
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Ohwaki et al. (1971) studied this question.
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