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Literature summary for 6.1.1.19 extracted from
- The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties (1991), Biochem. Biophys. Res. Commun., 180, 702-708.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60000 | - |
x * 60000, free enzyme | Rattus norvegicus |
| 72000 | - |
x * 72000, component of the multienzyme aminoacyl-tRNA synthetase complex, the 12000 MW NH2-terminal extension makes this form much more hydrophobic than the smaller one, SDS-PAGE | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
enzyme exists as a 72000 MW component of the multienzyme aminoacyl-tRNA synthetase complex or as 60000 MW free enzyme form | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 72000 MW form | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 60000, free enzyme | Rattus norvegicus |
| ? | x * 72000, component of the multienzyme aminoacyl-tRNA synthetase complex, the 12000 MW NH2-terminal extension makes this form much more hydrophobic than the smaller one, SDS-PAGE | Rattus norvegicus |
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