EC Number   |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s]  |
Substrate |
Reference |
|---|
    6.1.1.9 | -999 |
- |
more |
kcat for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the kcat for aminoacylation by 19fold |
653871 |
| 6.1.1.9 | -999 |
- |
more |
rate of hydrolysis of Thr-tRNAVal and Val-tRNAVal by wild-type and mutant enzyme, incorporation of amino acids valine and threonine into the enzyme |
650122 |
| 6.1.1.9 | 0.06 |
- |
L-valyl-tRNAVal |
DELTA32-71 mutant |
693165 |
| 6.1.1.9 | 0.064 |
- |
L-valine |
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C |
650122 |
| 6.1.1.9 | 0.074 |
- |
L-valine |
at pH and °C |
727894 |
| 6.1.1.9 | 0.2 |
- |
L-valyl-tRNAVal |
- |
693165 |
| 6.1.1.9 | 0.28 |
- |
ATP |
pH 7.5, 37°C, mutant D286A, in presence of tRNA |
715519 |
| 6.1.1.9 | 0.34 |
- |
ATP |
pH 7.5, 37°C, mutant K277P, in presence of tRNA |
715519 |
| 6.1.1.9 | 0.36 |
- |
tRNAVal |
C-terminally truncated mutant enzyme, pH 7.7, 65°C |
653871 |
| 6.1.1.9 | 0.48 |
- |
ATP |
pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA |
715519 |
