EC Number   |
Metals/Ions |
Reference  |
|---|
   3.6.4.B7 | Mg2+ |
ATP hydrolysis is not detected in presence of Mg2+ |
723283 |
| 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 | NH4Cl |
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 | RbCl |
stimulates the ssDNA-dependent ATPase activity. 1.0 M RbCl does not stimulate the ATPase activity of MmRadA in the absence of DNA |
723824 |
| 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+ |
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 |
| 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 | Mg2+ |
Mg2+ als well as K+ ions are absorbed at the ATPase center |
725699 |
