EC Number   |
Metals/Ions |
Reference |
|---|
   1.13.11.53 | Co2+ |
apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule |
662101 |
| 1.13.11.53 | Co2+ |
Co2+-form of enzyme, about 1 mol per mol of protein |
743725 |
| 1.13.11.53 | Co2+ |
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable |
741923 |
| 1.13.11.53 | Co2+ |
quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics |
742270 |
| 1.13.11.53 | Fe2+ |
the Fe2+ bound protein catalyzes the reaction of EC 1.13.11.54 |
741923 |
| 1.13.11.53 | Iron |
the enzyme contains a non-heme, iron-binding site critical for its activity |
764226 |
| 1.13.11.53 | Mg2+ |
required |
662091 |
| 1.13.11.53 | Mn2+ |
Mn2+-form of enzyme, less than 1 mol per mol of protein |
743725 |
| 1.13.11.53 | Mn2+ |
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable |
741923 |
| 1.13.11.53 | more |
the identity of bound metal ion does not affect the oligomeric state of ARD |
741923 |
