EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.26.5 | Ca2+ |
a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. Structural changes that occur upon binding Ca(II) to the ES complex are determined by time-resolved FRET measurements of the distances between donor/acceptor fluorophores introduced at specific locations on the P protein and pre-tRNA 5' leader. The value of KD,obs has an apparent hyperbolic dependence on the concentration of calcium with an apparent dissociation constant for Ca(II) of 0.04 mM |
715914 |
| 3.1.26.5 | Ca2+ |
activates |
716901 |
| 3.1.26.5 | Ca2+ |
Ca2+ can replace Mg2+ |
692711 |
| 3.1.26.5 | Ca2+ |
metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis |
716901 |
| 3.1.26.5 | Ca2+ |
Mg2+, Ca2+, Sr2+, and, to a lesser extent, Mn2+ can perform the electrostatic shielding function and preserve the structural properties of the two RNA molecules necessary to keep the substrate and enzyme in appropriate conformations |
134422 |
| 3.1.26.5 | Ca2+ |
much less efficiently than Mg2+ or Mn2+ |
678540 |
| 3.1.26.5 | Ca2+ |
presence of the protein cofactor increases and equalized substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA |
710141 |
| 3.1.26.5 | Ca2+ |
presence of the protein cofactor increases and equalizes substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA |
710141 |
| 3.1.26.5 | Ca2+ |
stabilizes RNase P folding and substrate binding with little activation of catalytic activity. Affinity of RNase P for A(-4) pre-tRNA increases 4fold as the Ca2+ concentration increases from 2 mM to 5 mM. Affinity for the G(-4) substrate increases 65fold over the same range |
709538 |
| 3.1.26.5 | Ca2+ |
suppresses enzyme activity, but supports RNA folding and substrate binding, used for binding assays |
656698 |
