EC Number |
Metals/Ions |
Reference |
---|
3.6.4.B7 | K+ |
Mg2+ als well as K+ ions are absorbed at the ATPase center. K+ (but not Na+), stimulates the ATP hydrolysis reaction with an apparent dissociation constant of about 40 mM. The strand exchange activity of the wild-type enzyme is also stimulated by potassium with an apparent dissociation constant of 35 mM |
725699 |
3.6.4.B7 | KCl |
stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP |
723824 |
3.6.4.B7 | Mg2+ |
ATP hydrolysis is not detected in presence of Mg2+ |
723283 |
3.6.4.B7 | Mg2+ |
Mg2+ als well as K+ ions are absorbed at the ATPase center |
725699 |
3.6.4.B7 | Mg2+ |
required |
722331, 725102, 733620, 734044, 756571, 756730, 757584, 757833, 757864 |
3.6.4.B7 | Mg2+ |
required for ATPase activity. The enzyme contains a secondary Mg2+ site as well as a canonical P-loop and nucleotide-lined primary Mg2+ site. The secondary Mg2+ site is important for modulating the ATPase activity |
724274 |
3.6.4.B7 | Mg2+ |
required. A magnesium ion is observed in all nucleotide-bound structures. It is positioned in the same location in ATP and AMPPNP structures, co-ordinated by the beta- and gamma-phosphate groups and the hydroxyl group of Thr145. In the ADP structure, the Mg2+ ion is shifted slightly towards the beta-phosphate group, it is also co-ordinated by the beta-phosphate and the hydroxyl group of Thr145, in addition to four water molecules. The residue Glu174 likely activates a water molecule for hydrolysis of ATP. Glu174 forms an indirect interaction with the Mg2+ ion via a bridging water molecule. As magnesium is not present in the crystallisation conditions of RadA, the phosphate-bound form also lacks magnesium, but this appears to have little impact on the binding of the phosphate |
756730 |
3.6.4.B7 | Mg2+ |
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+ |
724905 |
3.6.4.B7 | Mn2+ |
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+ |
724905 |
3.6.4.B7 | NaCl |
20 mM NaCl used in this mixture was found to be optimal for ATP hydrolysis |
725237 |