EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.13.4 | Fe2+ |
can substitute for Mg2+, Mn2+, optimal at 0.01 mM, two binding sites |
652348 |
| 3.1.13.4 | K+ |
K+ is essential to PARN activity and acts as an allosteric activator of PARN with multiple binding sites. K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation |
749789 |
| 3.1.13.4 | K+ |
required |
714476, 714876 |
| 3.1.13.4 | K+ |
required, optimal around 100 mM |
652023 |
| 3.1.13.4 | K+ |
required, optimal at about 100 mM |
653131 |
| 3.1.13.4 | K+ |
the binding of K+ to the entire RNA-recognition motif domain, which plays a central role in the allosteric communications of PARN regulation, leads to an increase of substrate-binding affinity but a decrease in the cooperativity of the substrate-binding site, while the binding of the cap analogue decreases both the catalytic efficiency and the substrate-binding affinity |
690777 |
| 3.1.13.4 | K3PO4 |
absolute required in absence of spermidine |
134096 |
| 3.1.13.4 | Mg2+ |
2 mM, activates reaction, can modulated the substrate length requirement |
669291 |
| 3.1.13.4 | Mg2+ |
active site consists of two metal ions (MgA and MgB), residue D50 takes a central position by contacting both metal ions. MgA is also coordinated by E52 and D240, while D171 contacts MgB. Seven water molecules, three associated with MgA and four with MgB, complete the dual octahedral coordination spheres of the two ions |
682172 |
| 3.1.13.4 | Mg2+ |
can be replaced by Mn2+ |
134089 |
