EC Number   |
Metals/Ions |
Reference |
|---|
   2.7.7.7 | Ca2+ |
bound to the active site, structure, overview |
690974 |
| 2.7.7.7 | Ca2+ |
Ca2+ (but not Ba2+, Co2+, Cu2+, Ni2+, or Zn2+) is a cofactor for Dpo4-catalyzed polymerization with both native and 8-oxoG-containing DNA templates. Both dNTP and ddNTP are substrates of the polymerase in the presence of either Mg2+ or Ca2+. No pyrophosphorolysis occurs in the presence of Ca2+ |
718842 |
| 2.7.7.7 | Ca2+ |
causes a concentration-dependent shift in the translocation equilibrium, predominantly by decreasing the forward translocation rate. Decreases the dNTP dissociation rate relative to Mg2+ and increases the dNTP association rate |
761458 |
| 2.7.7.7 | Ca2+ |
competes with Mg2+ for metal ion binding site(s) |
760574 |
| 2.7.7.7 | Co2+ |
activates |
761877 |
| 2.7.7.7 | Co2+ |
can effectively replace Mg2+. When Mg2+ is replaced with Co2+, the efficiency of incorporation of dTMP opposite dA increases by 5-fold |
760574 |
| 2.7.7.7 | Co2+ |
can partially replace Mg2+ in activation, optimal concentration: 2.5 mM |
643637 |
| 2.7.7.7 | DTT |
- |
690974, 690989 |
| 2.7.7.7 | Fe2+ |
required, in [4Fe-4S] clusters, that are bound to the CysB motif in all yeast B family DNA polymerases, assembly of the essential Fe-S cluster is strictly dependent on the function of mitochondrial Nfs1 and cytosolic Nbp35. The C-terminal domain of the catalytic subunit binds the Fe-S cluster in the CysB motif requiring all Cys residues of motif Cysb |
723249 |
| 2.7.7.7 | K+ |
- |
643594 |
