EC Number   |
Metals/Ions |
Reference |
|---|
    3.2.2.5 | Co2+ |
AA-NADase has one strong and two weak Co2+ binding sites |
709823 |
| 3.2.2.5 | Co2+ |
the enzyme has one strong and two weak Co2+ binding sites |
709823 |
| 3.2.2.5 | Cu2+ |
- |
137059 |
| 3.2.2.5 | Cu2+ |
although Cu2+ ions are important for catalyzing the hydrolysis of NAD, they are also able to inhibit its NADase activity in a concentration-dependent manner, Cu2+ ions in low-affinity binding sites inhibit its NADase activity. AA-NADase has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Cu2+ ions function as a switch for its NADase activity. |
709823 |
| 3.2.2.5 | Cu2+ |
among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains |
707758 |
| 3.2.2.5 | Cu2+ |
among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains. The binding of Cu2þ ions to AA-NADase is reversible, overview |
707587 |
| 3.2.2.5 | Cu2+ |
the enzyme contains Cu2+ ions that are essential for its multicatalytic activity. The enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Both NADase and ADPase activities of the enzyme do not have an absolute requirement for Cu2+ and may be replaced by Zn2+ > Mn2+ > Cu2+/Co2+ > Ni2+ |
709823 |
| 3.2.2.5 | Mn2+ |
AA-NADase has one Mn2+ binding site |
709823 |
| 3.2.2.5 | Mn2+ |
the enzyme has one Mn2+ binding site |
709823 |
| 3.2.2.5 | more |
no absolute requirement for metal ions, metal ion binding affinities in descending order: Cu2+ , Ni2+, Mn2+, Co2+, and Zn2+. Enzyme-metal ion interaction analysis by equilibrium dialysis, isothermal titration calorimetry, fluorescence, circular dichroism, dynamic light scattering and HPLC, overview |
709823 |
