EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.9 | C25T |
site-directed mutagenesis |
714322 |
| 6.1.1.9 | D276A |
valylation activity is similar to that of wild-type enzyme |
662398 |
| 6.1.1.9 | D279A |
editing site mutation, severely affects the binding ability of pre-transfer substrate Thr-AMP |
702702 |
| 6.1.1.9 | D279A |
valylation activity is similar to that of wild-type enzyme, efficiently produces Thr-tRNAVal, drastic decrease in ATP consumption rate, severe deficiency in deacylation activity with Thr-tRNAVal compared to wild-type enzyme |
662398 |
| 6.1.1.9 | D286A |
site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations |
715519 |
| 6.1.1.9 | D750G |
the mutation is associated with a temperature-sensitive phenotype. Although depicting slower growth at 26°C, the mutant strain is unable to grow at 37°C |
726908 |
| 6.1.1.9 | DELTA1-97 |
an N-domain-deleted yeast valyltRNA synthetase mutant (DELTA1-97) form Saccharomyces cerevisiae can be rescued by fusion of the equivalent domain from its human homologue |
693165 |
| 6.1.1.9 | DELTA1-97 |
deletion of N-terminal polypeptide extension of 97 residues, which is absent in bacteria, severely impairs tRNA binding, aminoacylation, and complementation activities of the enzyme. This N-domain-deleted yeast valyl-tRNA synthetase mutant can be rescued by fusion of the equivalent domain from its human homologue |
693165 |
| 6.1.1.9 | DELTA32-71 |
deletion of a lysine rich insert impairs aminoacylation activity of the enzyme in vitro but aminoacylation activity is still significantly higher than in DELTA1-97 mutant. Km: 0.001 mM (L-valyl-tRNAVal), kcast: 0.06/sec (L-valyl-tRNAVal) |
693165 |
| 6.1.1.9 | F264A |
valylation activity is similar to that of wild-type enzyme, about 15% decrease in ATP consumption rate compared to wild-type enzyme, somewhat reduced deacylation activityith Thr-tRNAVal, mutation impairs editing activity of ValRS |
662398 |
