EC Number   |
Metals/Ions  |
Reference |
|---|
    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 |
| 1.13.11.54 | Fe2+ |
required |
764775 |
| 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 | Mn2+ |
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53 |
741923 |
| 1.13.11.54 | more |
the identity of bound metal ion does not affect the oligomeric state of ARD |
741923 |
| 1.13.11.54 | Ni2+ |
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53 |
741923 |
