EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
6.1.1.17 | -999 |
- |
more |
- |
214, 221, 228 |
6.1.1.17 | -999 |
- |
more |
as the KCl concentration is raised from 0 to 100 mM, the Km value for L-glutamate in the reaction with E. coli tRNAGlu is remarkably increased wheras the Km value for glutamate with Thermus thermophilus tRNAGlu is slightly increased |
229 |
6.1.1.17 | -999 |
- |
more |
kinetics |
677107 |
6.1.1.17 | -999 |
- |
more |
kinetics, diverse tRNAGlu mutants |
651055 |
6.1.1.17 | -999 |
- |
more |
Km for diverse modified forms of tRNAAsp and tRNAGlu |
651050 |
6.1.1.17 | -999 |
- |
more |
Km-values of mutant enzymes |
209 |
6.1.1.17 | -999 |
- |
more |
Michaelis-Menten steady-state kinetic model |
745395 |
6.1.1.17 | -999 |
- |
more |
steady-state and transient kinetic analysis |
745552 |
6.1.1.17 | -999 |
- |
more |
steady-state kinetics of isozymes GluRS1 and GluRS2 |
676889 |
6.1.1.17 | 0.0000032 |
- |
tRNAGlu |
in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C |
727963 |