EC Number   |
Metals/Ions |
Reference |
|---|
   1.1.2.8 | Ca2+ |
ativates, active site-bound |
742793 |
| 1.1.2.8 | Ca2+ |
contains one Ca2+ ion per subunit of native enzyme. Treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2 + and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. Incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. |
701600 |
| 1.1.2.8 | Ca2+ |
rather loosely bound, necessary for pyrroloquinoline quinone binding and for stability of enzyme |
702114 |
| 1.1.2.8 | Ca2+ |
required |
742110 |
| 1.1.2.8 | Ca2+ |
the enzyme is only active in the presence of Ca2+ |
763417 |
| 1.1.2.8 | Ca2+ |
the prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion.In addition, enzyme contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme |
389959 |
| 1.1.2.8 | Iron |
one [2Fe-2S] cluster per enzyme |
725041 |
| 1.1.2.8 | La3+ |
required, active site-bound, 1.3 mol of La3+ per mol of ExaF protomer, indicating a 1:1 ratio of L3+ to protomer of enzyme |
742793 |
| 1.1.2.8 | Mg2+ |
required |
725154 |
| 1.1.2.8 | more |
the enzyme from strain AM1 utilizes La3+ rather than Ca2+ as a cofactor |
742793 |
