6.3.5.7	D178E	glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable	662450	
6.3.5.7	D178N	glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable	662450	
6.3.5.7	E125D	mutation in subunit B, molecular dynamics simulations	-, 745612	
6.3.5.7	E125Q	mutation in subunit B, molecular dynamics simulations	-, 745612	
6.3.5.7	K236E/E328A	mutant used for crystallization, secondary structure contents and enzymatic activities similar to wild-type	743955	
6.3.5.7	K254E	glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable	662450	
6.3.5.7	K88R	mutation in subunit B, molecular dynamics simulations	-, 745612	
6.3.5.7	additional information	activity of the engineered enzyme variants indicates that the acceptor stem loop is the principle discrimination element because insertion of this loop alone enhances the specificity of the archaeal enzyme toward tRNAGln2	728668	
6.3.5.7	additional information	construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA	-, 745552	
6.3.5.7	S128T	mutant protein retains significant glutaminase activity and transamidase activity in the presence of Gln	674787	
6.3.5.7	S152A	mutant is glutaminase inactive	674787	
6.3.5.7	S152T	mutant is glutaminase inactive	674787	
6.3.5.7	T101A	glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable	662450	
6.3.5.7	T101S	hydrolyzes about 10% of glutamine compared to wild-type enzyme. Compared to wild-type enzyme, the mutant enzyme converts approximately half as much mischarged tRNA substrate to product	662450	
6.3.5.7	T175V	mutation in subunit B, molecular dynamics simulations	-, 745612	
6.3.5.7	T177S	mutant enzyme hydrolyzes the same amount of glutamine as the wild-type enzyme. As the wild-type enzyme, the mutant enzyme transforms most of Glu-tRNAGln to Gln-tRNAGln	662450	
6.3.5.7	T177V	glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable	662450