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Literature summary for 6.1.1.1 extracted from
- Comparative structural dynamics of Tyrosyl-tRNA synthetase complexed with different substrates explored by molecular dynamics (2008), Eur. Biophys. J., 38, 25-35.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | A6QHR2 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr | molecular dynamics simulations of TyrRS in its free form and complexed with Tyr, ATP, tyrosyl adenylate and inhibitor respectively are carried out to investigate the ligand-linked conformational stability changes associated with its catalytic cycle. Unliganded TyrRS samples a more relaxed conformational space than substrate-bound TyrRS. There are three high flexibility regions encompassing residues 114-118, 128-133, and 226-238 respectively. The region which includes the KFGKS motif shows the highest difference in fluctuations | Staphylococcus aureus |
aSynonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tyrosyl-tRNA synthetase | - |
Staphylococcus aureus |
| TyrRS | - |
Staphylococcus aureus |
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