EC Number   |
Metals/Ions |
Reference |
|---|
    4.2.1.3 | Fe2+ |
required, binding structure in the [Fe-S] cluster, mechanism of activation of the enzyme by Fe2+, overview |
696168 |
| 4.2.1.3 | Fe2+ |
required, both isoenzymes have an [4Fe-4S] iron-sulfur cluster bound with cysteine residues Cys437, Cys503, and Cys506, under the action of reductants, the active enzyme form is produced with a complex cation of the [3Fe3S]2+ type, structure, and mechanism of activation of the enzyme by Fe2+, overview |
696168 |
| 4.2.1.3 | Fe2+ |
required, the enzyme contains iron-sulfur clusters. Chelating mitochondrial free iron in various cell systems causes loss of aconitase activity |
696992 |
| 4.2.1.3 | Fe2+ |
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview |
696029 |
| 4.2.1.3 | Iron |
a significant proportion of the enzyme is in the inactive [3Fe-4S]1+ or apoenzyme forms. AcnB contains a much higher proportion of inactive enzyme than AcnA |
649675 |
| 4.2.1.3 | Iron |
activity is posttranslationally regulated by iron |
652441 |
| 4.2.1.3 | Iron |
contains 2 gatoms of non-heme iron per mol of enzyme |
33795, 33803, 33805 |
| 4.2.1.3 | Iron |
contains 2.1 mol of iron per mol of enzyme |
33794 |
| 4.2.1.3 | Iron |
contains a [4Fe-4D] cluster |
666327 |
| 4.2.1.3 | Iron |
crystallographic evidence for a three-iron center |
33798 |
