EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    6.1.1.11 | -999 |
- |
more |
a temperature-dependent inhibition by conformational change of the enzyme (50°C-70°C) lowers both the catalytic activity and the substrate affinity of the ATP and amino acid sites as indicated by a sharp rise in Km with temperature |
91 |
| 6.1.1.11 | -999 |
- |
more |
addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview |
715636 |
| 6.1.1.11 | -999 |
- |
more |
calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview |
676937 |
| 6.1.1.11 | -999 |
- |
more |
kinetcis |
673593 |
| 6.1.1.11 | -999 |
- |
more |
kinetic changes in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay |
651138 |
| 6.1.1.11 | -999 |
- |
more |
kinetics |
674636, 674720 |
| 6.1.1.11 | -999 |
- |
more |
kinetics for the ATP-diphosphate exchange reaction |
650314 |
| 6.1.1.11 | -999 |
- |
more |
kinetics with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview |
652204 |
| 6.1.1.11 | -999 |
- |
more |
Km values for tRNASer transcripts |
78 |
| 6.1.1.11 | -999 |
- |
more |
Km-values for different tRNASer variants |
662297 |
