EC Number   |
Protein Variants |
Reference |
|---|
    6.3.5.7 | more |
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 | more |
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 | 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 | K254E |
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable |
662450 |
| 6.3.5.7 | T101A |
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable |
662450 |
| 6.3.5.7 | T177V |
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 | 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 | S152A |
mutant is glutaminase inactive |
674787 |
