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EC Number
Metals/Ions
Commentary
Reference
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%)
Co2+
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+
Co2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
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%)
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
Mg2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
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
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%)
Mn2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
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%)
Results 1 - 10 of 11 > >>