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Literature summary for 6.1.1.19 extracted from
- Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase (1989), Mol. Cell. Biochem., 86, 125-133.
General Stability
| General Stability | Organism |
|---|---|
| complexed arginyl-tRNA synthetase is more stable than the free enzyme | Oryctolagus cuniculus |
| reduced glutathione effectively protects the enzyme from thermal inactivation | Oryctolagus cuniculus |
| tRNA reduces thermal inactivation | Oryctolagus cuniculus |
| zinc or Triton X-100 increases thermal inactivation | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
enzyme exists as a high MW component of the multienzyme aminoacyl-tRNA synthetase complex and a low MW free enzyme | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Oryctolagus cuniculus | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
tRNA reduces thermal inactivation, reduced glutathione effectively protects the enzyme from thermal inactivation, zinc or Triton X-100 increases thermal inactivation | Oryctolagus cuniculus |
| 37 | - |
20 min, 25% loss of activity of high MW form, 50% loss of activity of low MW form | Oryctolagus cuniculus |
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