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Literature summary for 3.4.19.3 extracted from
- Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic archaeon, Pyrococcus furiosus (2001), Eur. J. Biochem., 268, 3233-3242.
Activating Compound
| 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
| 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
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Renatured (Commentary)
| 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 and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-pyroglutamyl-p-nitroanilide + H2O | - |
Pyrococcus furiosus | L-pyroglutaminic acid + p-nitroaniline | - |
? | |
Subunits
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| PCP | - |
Pyrococcus furiosus |
| pyrrolidone carboxyl peptidase | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| 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 Range [°C]
| 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 [°C]
| 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 |
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Release 2023.1 (January 2023)
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