2.4.2.29	D264N	is inactive and incapable of forming the covalent intermediate, while maintaining the ability to bind noncovalently to RNA	702263	
2.4.2.29	D89A	less than 1% of the activity of the histidine-tagged wild-type enzyme	644933	
2.4.2.29	D89C	less than 1% of the activity of the histidine-tagged wild-type enzyme	644933	
2.4.2.29	D89E	about 50% of the activity of the histidine-tagged wild-type enzyme	644933	
2.4.2.29	D89N	less than 1% of the activity of the histidine-tagged wild-type enzyme	644933	
2.4.2.29	E235Q	the mutation has no significant influence on kcat, but Km for preQ1 is drastically increased, while Km for preQ0 seems to be decreased	688390	
2.4.2.29	K52M	reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident	705164	
2.4.2.29	S90A	activity of the mutant enzyme is to low to determine Vmax and Km-value	644934	
2.4.2.29	S90C	30fold increase in Km-value for tRNATyr and 4fold increase in Km-value for guanine	644934	
2.4.2.29	S90F	mutant enzyme has no detectable solubility and reduced solubility	644934