EC Number   |
Metals/Ions |
Reference  |
|---|
   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 | more |
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 | more |
enzyme activities of free and immobilized enzymes are not affected by Ca2+ |
701567 |
