Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | strongly stimulates activity of wild-type enzyme and mutant enzyme C188S and shifts the pH-optimum to higher temperatures by about 10°C | Pyrococcus furiosus |
Protein Variants | Comment | Organism |
---|---|---|
C142S/C188S | mutant enzyme loses its activity completely | Pyrococcus furiosus |
C188S | activity is reduced by one-fourth relative to the activity of the wild-type enzyme | Pyrococcus furiosus |
General Stability | Organism |
---|---|
subunit interactions play an important role in stabilizing the enzyme in addition to the intrinsic enhanced stability of its monomer | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
the heat denaturation of wild-type enzyme and mutant enzymes C188S and C142S/C188S is highly reversible in the dimeric forms, but completely irreversible in the tetrameric form | Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-pyroglutamyl-p-nitroanilide + H2O | - |
Pyrococcus furiosus | L-pyroglutaminic acid + p-nitroaniline | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5 | Pyrococcus furiosus |
monomer | the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5 | Pyrococcus furiosus |
tetramer | the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5 | Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
PCP | - |
Pyrococcus furiosus |
pyrrolidone carboxyl peptidase | - |
Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | 85 | wild-type enzyme in absence of dithiothreitol | Pyrococcus furiosus |
90 | - |
wild-type enzyme in presence of dithiothreitol | Pyrococcus furiosus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 100 | 60°C: about 40% of maximal activity, 100°C: about 90% of maximal activity, wild-type enzyme, in presence of dithiothreitol | Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the heat denaturation of wild-type enzyme and mutant enzymes C188S and C142S/C188S is highly reversible in the dimeric forms, but completely irreversible in the tetrameric form | Pyrococcus furiosus |