| + |
TARS1 | down-regulates quantity 
chemical modification
|
threonine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270502 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
threonine | up-regulates quantity 
|
AminoAcids |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264761 |
|
|
|
|
| pmid |
sentence |
| 29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
| Publications: |
1 |
| + |
threonine | up-regulates quantity
precursor of
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270508 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
threonine