EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   3.1.26.5 | -999 |
- |
more |
- |
134419, 666501 |
| 3.1.26.5 | -999 |
- |
more |
both pre-steady state and steady state kinetics |
656352 |
| 3.1.26.5 | -999 |
- |
more |
dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release |
730326 |
| 3.1.26.5 | -999 |
- |
more |
dissociation of the tRNA product from the catalytic RNA usually limits the rate of the RNA-alone reaction under multiple-turnover conditions, single-turnover conditions allow to analyze steps preceding product release, pseudo-first-order rate constants of cleavage are calculated by nonlinear regression analysis |
730326 |
| 3.1.26.5 | -999 |
- |
more |
kinetics |
654201, 656698, 656825, 657342, 730931 |
| 3.1.26.5 | -999 |
- |
more |
kinetics and kinetic mechanism of reaction and enzyme stablization with metal ions, overview |
715914 |
| 3.1.26.5 | -999 |
- |
more |
kinetics of deletion mutants |
714543 |
| 3.1.26.5 | -999 |
- |
more |
kinetics of wild-type and mutant enzymes, affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp substrate, overview. Apparent pKa and pH-independent single-turnover rate constants for wild-type enzyme and mutants R60A and R62A in Mg(II) |
716901 |
| 3.1.26.5 | -999 |
- |
more |
kinetics, the rate constant for the scissile bond cleavage is pH-dependent |
654201 |
| 3.1.26.5 | -999 |
- |
more |
KM-values for pre-tRNATyr, mutant enzymes |
666911 |
