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Literature summary for 6.1.1.6 extracted from
- High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation (1982), Biochem. Biophys. Res. Commun., 106, 44-47.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + lysine + tRNALys | - |
Rattus norvegicus | AMP + L-lysyl-tRNALys + diphosphate | - |
? |  |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
24 S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°C, 37°C and 43°C | Rattus norvegicus |
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