EC Number   |
Metals/Ions |
Reference |
|---|
    1.13.11.54 | Fe2+ |
apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule |
662101 |
| 1.13.11.54 | Fe2+ |
bacterially expressed AsARD1 preferentially binds Fe2+ rather than Ni2+ |
663098 |
| 1.13.11.54 | Fe2+ |
dependent on |
764494, 764909 |
| 1.13.11.54 | Fe2+ |
dependent on, acireductone dioxygenase 1 is an active metalloenzyme, Fe2+ is active site bound |
725438 |
| 1.13.11.54 | Fe2+ |
dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route |
725214 |
| 1.13.11.54 | Fe |
enzyme contains 1 atom of Fe |
661058 |
| 1.13.11.54 | Fe2+ |
Fe2+ can be replaced by Mg2+, albeit with lower activity |
675408 |
| 1.13.11.54 | Fe2+ |
Fe2+-form of enzyme, less than 1 mol per mol of protein |
743725 |
| 1.13.11.54 | Iron |
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions |
685212 |
| 1.13.11.54 | Fe2+ |
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable |
741923 |
