Abstract
The specific activity of inorganic pyrophosphatase (EC 3.6.1.1) fromSchizophyllum commune correlated with the growth pattern so that actively dividing cells contained the highest enzyme activities. Continuous illumination which induce a certain series of morphogenetic events in the colony, exhibited no specific effects on the enzyme activity. There was no detectable activity in the absence of divalent cations. Mg2+ was required for maximum activity; Mn2+ and Co2+ supported 7.3 and 6.7 % of the activity observed with Mg2+, respectively. The results of kinetic experiments suggest that P2O7 4− is a strong inhibitor, whereas Mg1P2O7 2− and Mg2P2O7 are substrates, the latter being leas reactive than the former. The enzyme was inhibited by ATP, which competes with P2O7 4− for the chelation of Mg2+. Furthermore, 2,4,6-trinitrobenzenesulphonic acid and thiol inhibitors, N-ethylmaleimide and 4-hydroxymercuribenzoate, inhibited the enzyme, suggesting that lysine and cvsteine play essential roles in the enzyme activity.
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