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 | 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 | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Oryctolagus cuniculus | - |
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 |