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Results 1 - 10 of 28 > >>
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Reference
-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
-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
0.06
-
L-valyl-tRNAVal
DELTA32-71 mutant
0.064
-
L-valine
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.074
-
L-valine
at pH and °C
0.2
-
L-valyl-tRNAVal
-
0.28
-
ATP
pH 7.5, 37°C, mutant D286A, in presence of tRNA
0.34
-
ATP
pH 7.5, 37°C, mutant K277P, in presence of tRNA
0.36
-
tRNAVal
C-terminally truncated mutant enzyme, pH 7.7, 65°C
0.48
-
ATP
pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA
Results 1 - 10 of 28 > >>