EC Number |
Metals/Ions |
Reference |
---|
2.7.7.B16 | Ca2+ |
required |
738189 |
2.7.7.B16 | K+ |
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+ |
720567 |
2.7.7.B16 | Mg2+ |
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+ |
720567 |
2.7.7.B16 | Mg2+ |
optimal concentration: 10 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2 |
720231 |
2.7.7.B16 | Mg2+ |
the enzyme is strictly dependent on divalent cations, activating metal preferably used by Rep245 for its DNA polymerase activity is Mg2+ at concentrations between 5 and 10 mM |
719447 |
2.7.7.B16 | Mn2+ |
activates |
739147 |
2.7.7.B16 | Mn2+ |
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+ |
720567 |
2.7.7.B16 | Mn2+ |
in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain |
726027 |
2.7.7.B16 | Mn2+ |
optimal concentration: 5 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2 |
720231 |
2.7.7.B16 | Mn2+ |
RNA synthesis with the Thermococcus kodakaraensis primase complex is stimulated about 2fold by the presence of Mn2+, whereas the size of RNA chains is marginally affected. DNA synthesis is slightly inhibited by Mn2+ |
720015 |