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	Fe3+	dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Ba2+, and Mn2+	488310	
2.4.1.10	additional information	not affected by 5 mM of Ba2+, Zn2+, Hg2+, Ni2+, Mn2+, Cu2+, Co2+, Ca2+, Na2MoO4	488314	
2.4.1.10	Fe2+	4fold increase in activity at 5 mM	488329	
2.4.1.10	Co2+	slightly activating	488345	
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+	stimulates activity, Asp500 residues play an important role in Ca2+ binding	658750	
2.4.1.10	Ca2+	Mg2+, Zn2+, Mn2+, Fe2+ have no effect	684765	
2.4.1.10	Mn2+	The transferase activity of levansucrase in the reaction mixture supplemented with Mn2+ is 100% higher than the enzyme activity in medium without metal ions, the hydrolytic activity of the levansucrase is lowered by 80%	689722	
2.4.1.10	additional information	enzyme activities of free and immobilized enzymes are not affected by Ca2+	701567