EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    6.1.1.20 | -999 |
- |
more |
- |
342, 348, 350, 352 |
| 6.1.1.20 | -999 |
- |
more |
aminoacylation kinetics with Phe and Tyr |
677104 |
| 6.1.1.20 | -999 |
- |
more |
full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview |
672206 |
| 6.1.1.20 | -999 |
- |
more |
kinetics, binding energies in the active conformation |
653011 |
| 6.1.1.20 | -999 |
- |
more |
Km value for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids |
329 |
| 6.1.1.20 | -999 |
- |
more |
Km-value for tRNA mutants |
321 |
| 6.1.1.20 | -999 |
- |
more |
Km-values for mutant yeast tRNAPhe transcripts |
327, 328 |
| 6.1.1.20 | -999 |
- |
more |
negative cooperativity exists in the binding of all substrates |
313 |
| 6.1.1.20 | 0.000066 |
- |
tRNAPhe |
- |
309 |
| 6.1.1.20 | 0.0001 |
- |
tRNAPhe |
recombinant heterodimer, pH 8.0, 25°C |
653743 |
