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Literature summary extracted from
- The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyroccoccus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding (1998), Biochemistry, 37, 17537-17544.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.19.3 | C142S/C188S | the mutant enzyme is used in unfolding and refolding experiments to exclude the complexity in reaction due to oxidation of SH groups | Pyrococcus furiosus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.19.3 | wild-type and mutant enzyme C142S/C188S, the anomalous high stability of the hyperthermophilic enzyme originates from the unusually slow rate of unfolding reaction during treatment with guanidine-hydrochloride | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.3 | Bacillus amyloliquefaciens | - |
- |
- |
| 3.4.19.3 | Pyrococcus furiosus | - |
- |
- |
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