EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.30.2 | Ca2+ |
activates at pH 8.0 |
730587 |
| 3.1.30.2 | Ca2+ |
activates at pH 8.0, preferred divalent cation |
730587 |
| 3.1.30.2 | Ca2+ |
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+ |
750660 |
| 3.1.30.2 | Mg2+ |
- |
654944, 657122, 699775 |
| 3.1.30.2 | Mg2+ |
activates |
135020 |
| 3.1.30.2 | Mg2+ |
coordinates 5 water molecules that participate in the enzyme-controlled reaction |
657343 |
| 3.1.30.2 | Mg2+ |
in the presence of 0.58 mM Mg2+, the digestive activity of the enzyme is approximately fourfold increased as compared with the activity in the absence of Mg2+ taken as 100%. Further fivefold increase in Mg2+ concentration causes near 1.5fold enhancement in the enzyme activity. Subsequent two- and fourfold increases in Mg2+ concentration have only a minor impact on the enzyme activity within the experimental error range. 6.0-11.6 mM of Mg2+ corresponding to 20-40 Mg2+ per 1 phosphate in RNA is optimal for the hydrolysis of RNA. Optimal Mg2+ amount is linked with the changing secondary structure of RNA substrates within A-helix. Addition of Mg2+ affects both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that is supported by strong increase in the Kcat values and change in the Km values |
750015 |
| 3.1.30.2 | Mg2+ |
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+ |
750660 |
| 3.1.30.2 | Mg2+ |
increases hydrolysis rate of EDTA-dialyzed RNA, no effect on hydrolysis of undialyzed RNA, inhibition at high concentrations |
135006 |
| 3.1.30.2 | Mg2+ |
molecular dynamic simulations, interaction with enzyme monomer-DNA complex via 6 ligands, which are changing during the reaction simulation, e.g. Asn119 loses its coordination while Glu127 becomes a ligand, overview |
666881 |
