Protein Variants | Comment | Organism |
---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
dimer | the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 | Pyrococcus furiosus |
monomer | the mutant enzyme C142S/C188S is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5 | Pyrococcus furiosus |
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 | Comment | Organism |
---|---|---|
pyrrolidone carboxyl peptidase | - |
Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
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 |