2.4.1.10 Ba2+ 107% activity at 5 mM 757042 2.4.1.10 Ni2+ 109% activity at 5 mM 757042 2.4.1.10 Ca2+ 113% activity at 5 mM 757042 2.4.1.10 Mg2+ 115% activity at 5 mM 757042 2.4.1.10 K+ 118% activity at 5 mM 757042 2.4.1.10 Mn2+ 128% activity at 5 mM 757042 2.4.1.10 Sn2+ 143% activity at 5 mM 757042 2.4.1.10 MnCl2 22% activation of the immobilized enzyme at 0.1 mM, 30% activation at 0.1 mM of the free enzyme 702972 2.4.1.10 Fe2+ 4fold increase in activity at 5 mM 488329 2.4.1.10 Ca2+ activates both transfructosylation and hydrolytic activities 735800 2.4.1.10 Mg2+ activates both transfructosylation and hydrolytic activities 735800 2.4.1.10 Rb+ activates slightly, recombinant enzyme 735834 2.4.1.10 Co2+ activates strongly, recombinant enzyme 735834 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 Fe3+ dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Ba2+, and Mn2+ 488310 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 additional information enzyme activities of free and immobilized enzymes are not affected by Ca2+ 701567 2.4.1.10 Ca2+ Mg2+, Zn2+, Mn2+, Fe2+ have no effect 684765 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 additional information not influenced by Rb+, Na+, Co2+ and Li+ 757042 2.4.1.10 Co2+ slightly activating 488345 2.4.1.10 Ca2+ stimulates activity, Asp500 residues play an important role in Ca2+ binding 658750 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