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Literature summary extracted from
- Slow irreversible unfolding of Pyrococcus furiosus triosephosphate isomerase: Separation and quantitation of conformers through a novel electrophoretic approach (2005), Anal. Biochem., 347, 49-59.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 5.3.1.1 | global unfolding effected by heat and denaturants such as urea or guanidine hydrochloride is irreversible | Pyrococcus furiosus |
| 5.3.1.1 | native form of enzyme is stable to unfolding by SDS | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.1 | Pyrococcus furiosus | - |
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Release 2023.1 (January 2023)
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