EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   3.6.4.13 | -999 |
- |
more |
kinetic study |
669358 |
| 3.6.4.13 | -999 |
- |
more |
kinetics of wild-type and mutant enzymes, overview |
699909 |
| 3.6.4.13 | -999 |
- |
more |
Michaelis-Menten kinetics |
734802, 756012 |
| 3.6.4.13 | -999 |
- |
more |
Michaelis-Menten kinetics of ATP hydrolysis |
756204 |
| 3.6.4.13 | -999 |
- |
more |
protease activities of NS3-4A variants analyzed, uncleaved NS3/4A polyprotein lacks protease and helicase activities |
698821 |
| 3.6.4.13 | -999 |
- |
more |
RNA-stimulated ATPase activities of NS3-4A variants analyzed, functionally important ATP-bound state of NS3 binds RNA much more tightly in the presence of NS4A, effectively coupling RNA binding to ATPase activity |
699909 |
| 3.6.4.13 | -999 |
- |
more |
stopped flow assays, kinetics analysis and comparison of wild-type and mutant Upf isozymes with ATP, overview |
757849 |
| 3.6.4.13 | 0.000001 |
- |
ATP |
pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant NS3-4A |
699909 |
| 3.6.4.13 | 0.000002 |
- |
ATP |
pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant S1369R/M1708A |
699909 |
| 3.6.4.13 | 0.0001 |
- |
ATP |
pH 6.5, 37°C, RNA-stimulated ATPase activity of wild-type NS3 |
699909 |
