EC Number   |
Metals/Ions |
Reference |
|---|
   5.1.3.30 | Co2+ |
activates 10.8fold at 1 mM, best divalent cation, dependent on |
748501 |
| 5.1.3.30 | Co2+ |
activates most highly at 0.5 mM, 80% of maximal activation at 1-5 mM, best divalent cation, dependent on |
746879 |
| 5.1.3.30 | Co2+ |
best metal cofactor, has no effect on pH stability and slightly imporves temperature |
748412 |
| 5.1.3.30 | Co2+ |
highly activating at 1 mM, essential for the activity of the recombinant enzyme |
748499 |
| 5.1.3.30 | Co2+ |
metalloprotein that exhibits the highest activity in the presence of Co2+ |
726795 |
| 5.1.3.30 | Co2+ |
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+ |
727657 |
| 5.1.3.30 | Co2+ |
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+ |
727652 |
| 5.1.3.30 | Co2+ |
the metal-dependent enzyme requires Co2+ as optimum cofactor. The relative activity is linearly increased when adding Co2+ from 0.005 mM to 0.035 mM. When adding greater concentrations of Co2+, the relative activity tends to be stable. The optimum Co2+ concentration is 0.2 mM for catalytic activity |
727229 |
| 5.1.3.30 | Fe2+ |
26.59% of the activity with Co2+ at 1 mM |
748412 |
| 5.1.3.30 | Fe2+ |
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Fe2+ the enzyme activity is reduced to 49% of that in the presence of Co2+ |
727657 |
