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Literature summary extracted from
- The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus (2002), J. Mol. Biol., 316, 991-1003.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.19.3 | C142S/C188S | small thermodynamic stability of the mutant enzyme C142S/C188S at low pH. The mutant enzyme is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5. The heat-denaturation of the mutant enzyme is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.3 | Pyrococcus furiosus | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.4.19.3 | the heat-denaturation of the mutant enzyme C142S/C188S is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics | Pyrococcus furiosus |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.19.3 | dimer | the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 | Pyrococcus furiosus |
| 3.4.19.3 | monomer | the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 | Pyrococcus furiosus |
| 3.4.19.3 | tetramer | the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 | Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.3 | pyrrolidone carboxyl peptidase | - |
Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.19.3 | 47 | - |
thermodynamics of heat denaturation of the monomeric enzyme form of mutant enzyme C142S/C188S at pH 2.3. The mechanism of refolding is a two-state process. The equilibrium establishes with a relaxation time of 5080 s at Tm = 46.5°C | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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