EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    6.1.1.19 | -999 |
- |
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide |
Km values for different tRNAArg variants |
653866 |
| 6.1.1.19 | -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 |
| 6.1.1.19 | -999 |
- |
more |
effect on the Km of several variations of the tRNAArg sequence |
651112 |
| 6.1.1.19 | -999 |
- |
more |
Km values for aminoacylation of various amino acids with tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2) |
260 |
| 6.1.1.19 | -999 |
- |
more |
Km values for ATP and L-arginine for 26 mutants |
653868 |
| 6.1.1.19 | -999 |
- |
more |
Km values for ATP and L-arginine for several mutants and revertants |
652831 |
| 6.1.1.19 | -999 |
- |
more |
Km values for the wild type and mutant enzymes using tRNAArg with different nucleotides at position 20 |
653659 |
| 6.1.1.19 | -999 |
- |
more |
Km values for tRNAArg, arginine, and ATP in the presence of hemin are not altered, but kcat values dramatically decrease compared with those in the absence of hemin, kinetic analysis, overview |
715565 |
| 6.1.1.19 | 0.00005 |
- |
tRNAArg |
37°C, pH 7.5, arginylation, full-length enzyme |
662416 |
| 6.1.1.19 | 0.00005 |
0.0006 |
tRNAArg |
pH 7.4 |
278 |
