Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae.

Homogeneous soluble exopolyphosphatase (EC 3.6.1.11) from yeast Saccharomyces cerevisiae, (scPPX1) behaves as an adenosine 5'-tetraphosphate phosphohydrolase (EC 3.6.1.14). The hydrolysis of adenosine 5'-tetraphosphate (p4A) to ATP and orthophosphate absolutely depends on one of the following cations: Co2+>Mn2+>Mg2+>Ni2+. Optimum pH is around 4.75 and the Km for p4A estimated at that pH in 50 mM sodium acetate and at 5 mM CoCl2 is 80+/-10 microM. Adenosine 5'-pentaphosphate (p5A) is degraded under these conditions 18-fold more slowly than p4A. Assuming that the mass of scPPX1 is 45 kDa, the calculated kcat values for p4A and for p5A are 723 and 40 s-1, respectively. Two other nucleoside 5'-tetraphosphates (p4N), guanosine tetraphosphate (p4G) and inosine tetraphosphate (p4I), were hydrolyzed to Pi and either GTP or ITP, respectively, at the same rate as that observed for the hydrolysis of p4A. Ammonium molybdate, sodium o-vanadate and zinc chloride inhibit the hydrolysis of p4A (I50 values are 0.08, 0.3 and 0.4 mM, respectively). This newly recognized 'acidic' adenosine tetraphosphatase activity from yeast is compared with two 'pH 8' adenosine tetraphosphatases described earlier in rabbit and yellow lupin.