2.4.1.10	Ba2+	107% activity at 5 mM	757042	
2.4.1.10	Ca2+	113% activity at 5 mM	757042	
2.4.1.10	Ca2+	activates both transfructosylation and hydrolytic activities	735800	
2.4.1.10	Ca2+	activates, recombinant enzyme	735834	
2.4.1.10	Ca2+	addition of 0.1 mM Ca2+ in the reaction medium, containing 0.05 mM EDTA, causes a significant increase in the enzyme's activity, achieving about 100% relative activity	756953	
2.4.1.10	Ca2+	Ca2+ play an important structural role. At 45°C the mutant enzymes D500A and D500N are inactive in the absence of Ca2+ ions, with, respectively, 15% and 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzymes display highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C	658750	
2.4.1.10	Ca2+	dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Sr2+, Ba2+, and Mn2+	488310	
2.4.1.10	Ca2+	Mg2+, Zn2+, Mn2+, Fe2+ have no effect	684765	
2.4.1.10	Ca2+	stimulates activity, Asp500 residues play an important role in Ca2+ binding	658750	
2.4.1.10	Co2+	activates strongly, recombinant enzyme	735834