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EC Number
Metals/Ions
Commentary
Reference
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
Co2+
Co2+-form of enzyme, about 1 mol per mol of protein
Co2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
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
Fe2+
the Fe2+ bound protein catalyzes the reaction of EC 1.13.11.54
Mg2+
required
Mn2+
Mn2+-form of enzyme, less than 1 mol per mol of protein
Mn2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
more
the identity of bound metal ion does not affect the oligomeric state of ARD
Results 1 - 10 of 25 > >>