3.6.1.17	Ca2+	activated by physiological concentration, maximal activity at 2 mM	657213	
3.6.1.17	Ca2+	no activity in the presence of 1.0 and 5.0 mM Ca2+	695301	
3.6.1.17	Cd2+	no activity in the presence of 1.0 mM Cd2+, weak enzyme activation at 5 mM (4.% compared to 1.5 mM Mn2+)	695301	
3.6.1.17	Co2+	5 mM, 42% of the activity with Mg2+	733450	
3.6.1.17	Co2+	60% of activity	209908	
3.6.1.17	Co2+	about 50% of the activity with Mn2+. In the presence of Mn2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate mainly into AMP and ATP, whereas in the presence of Co2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17	733872	
3.6.1.17	Co2+	divalent cation required, 20% of maximal activity in presence of 1 mM Co2+	654817	
3.6.1.17	Co2+	the enzyme is dependent on divalent cations	687119	
3.6.1.17	Co2+	weak stimulation	209911	
3.6.1.17	Mg2+	-	209909	
3.6.1.17	Mg2+	5 mM MgCl2 included in assay medium	697896	
3.6.1.17	Mg2+	activated by physiological concentration, maximal activity at 2 mM	657213	
3.6.1.17	Mg2+	best activator, maximum activity at 5 mM	733450	
3.6.1.17	Mg2+	divalent cation required, maximal activity in presence of 3-5 mM Mg2+	654817	
3.6.1.17	Mg2+	in the presence of Mn2+ the Km value for diadenosine 5',5''-P1,P4-tetraphosphate is roughly two orders of magnitude tighter than in the presence of Mg2+	733346	
3.6.1.17	Mg2+	maximum activity at 3 mM	209908	
3.6.1.17	Mg2+	no activity in the presence of 1 mM Mg2+, 9.1% relative activity at 5 mM Mg2+ compared to 1.5 mM Mn2+	695301	
3.6.1.17	Mg2+	required	209893, 209898, 209901, 209911	
3.6.1.17	Mg2+	required, maximum activity at 1 mM	209897	
3.6.1.17	Mg2+	required, maximum activity at 5 mM	209895	
3.6.1.17	Mg2+	required, optimum concentration 3-10 mM	209906	
3.6.1.17	Mg2+	the enzyme is dependent on divalent cations, preferred cation, best at 3-10 mM	687119	
3.6.1.17	Mn2+	-	209909, 209911	
3.6.1.17	Mn2+	15% of maximum activity	209895	
3.6.1.17	Mn2+	40% of activity	209908	
3.6.1.17	Mn2+	5 mM, 11% of the activity with Mg2+	733450	
3.6.1.17	Mn2+	able to substitute for Mg2+, 70% of activity at equal metal ion concentration	209893	
3.6.1.17	Mn2+	activated by physiological concentration, maximal activity at 0.1 mM	657213	
3.6.1.17	Mn2+	best activator. In the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17	733872	
3.6.1.17	Mn2+	divalent cation required, 20% of maximal activity in presence of 0.1 mM Mn2+	654817	
3.6.1.17	Mn2+	enzyme preferentially hydrolyses diadenosine 5',5'-P1P4 tetraphosphate in the form of a Mn2+ complex at a concentration of 1.5 mM, 37.7% relative activity at 0.5 mM compared to 1.5 mM Mn2+	695301	
3.6.1.17	Mn2+	in the presence of Mn2+ the Km value for diadenosine 5',5''-P1,P4-tetraphosphate is roughly two orders of magnitude tighter than in the presence of Mg2+	733346	
3.6.1.17	Mn2+	required, maximum activity at 0.5 mM	209897	
3.6.1.17	Mn2+	required, more effective than Mg2+	209898	
3.6.1.17	Mn2+	the enzyme is dependent on divalent cations	687119	
3.6.1.17	additional information	no activation by Ca2+	733450	
3.6.1.17	additional information	no activation by Cu2+, Fe2+, Ni2+ or Ca2+	687119	
3.6.1.17	Zn2+	25% of activity	209893	
3.6.1.17	Zn2+	5 mM, 2% of the activity with Mg2+	733450	
3.6.1.17	Zn2+	50% of activity	209908	
3.6.1.17	Zn2+	divalent cation required, 20% of maximal activity in presence of 0.05 mM Mn2+	654817	
3.6.1.17	Zn2+	enzyme exhibit residual activity in the presence of 1.5 mM Zn2+ ions, 28.4% relative activity at 5 mM Zn2+ compared to 1.5 mM Mn2+	695301	
3.6.1.17	Zn2+	strongest activation	209909	
3.6.1.17	Zn2+	the enzyme is dependent on divalent cations, high activity	687119