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Literature summary extracted from
- Kinetically robust monomeric protein from a hyperthermophile (2004), Biochemistry, 43, 13859-13866 .
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.4 | Thermococcus kodakarensis | O74035 | - |
- |
| 3.1.26.4 | Thermococcus kodakarensis ATCC BAA-918 | O74035 | - |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | the denaturation by guanidinium chloride is completely reversible at 50°C, the unfolding and refolding reactions of the enzyme attain a two-state equilibrium in 2 weeks | Thermococcus kodakarensis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | Tk-Tk-RNase HII | - |
Thermococcus kodakarensis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | 87.2 | - |
the denaturation temperature at a scan rate of 5°C/h is 87.2°C. The heat-induced unfolding of the enzyme does not attain equilibrium because of the slow unfolding | Thermococcus kodakarensis |
| 3.1.26.4 | 89.2 | - |
the denaturation temperature at a scan rate of 90°C/h is 89.2°C. The heat-induced unfolding of the enzyme does not attain equilibrium because of the slow unfolding | Thermococcus kodakarensis |
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Release 2023.1 (January 2023)
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