EC Number |
Metals/Ions |
Reference |
---|
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 |