EC Number |
Metals/Ions |
Reference |
---|
2.7.1.B20 | Co2+ |
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+ |
697882 |
2.7.1.B20 | Mg2+ |
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+. Maximum activity is attained when the ATP/Mg2+ concentration ratio is 0.5 |
697882 |
2.7.1.B20 | Ni2+ |
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+ |
697882 |
2.7.1.B20 | Mg2+ |
there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal |
726575 |
2.7.1.B20 | Co2+ |
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%) |
727430 |
2.7.1.B20 | Mg2+ |
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%) |
727430 |
2.7.1.B20 | Mn2+ |
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%) |
727430 |
2.7.1.B20 | Ni2+ |
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%) |
727430 |
2.7.1.B20 | Co2+ |
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+ |
728780 |
2.7.1.B20 | Mg2+ |
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+ |
728780 |