6.1.1.9	additional information	-	additional information	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	additional information	-	additional information	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