Literature summary extracted from
Ogasahara, K.; Khechinashvili, N.N.; Nakamura, M.; Yoshimoto, T.; Yutani, K.
Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic archaeon, Pyrococcus furiosus (2001), Eur. J. Biochem., 268, 3233-3242.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.4.19.3 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.19.3 |
C142S/C188S |
mutant enzyme loses its activity completely |
Pyrococcus furiosus |
3.4.19.3 |
C188S |
activity is reduced by one-fourth relative to the activity of the wild-type enzyme |
Pyrococcus furiosus |
General Stability
EC Number |
General Stability |
Organism |
---|
3.4.19.3 |
subunit interactions play an important role in stabilizing the enzyme in addition to the intrinsic enhanced stability of its monomer |
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 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)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.19.3 |
L-pyroglutamyl-p-nitroanilide + H2O |
- |
Pyrococcus furiosus |
L-pyroglutaminic acid + p-nitroaniline |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.19.3 |
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 |
3.4.19.3 |
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 |
3.4.19.3 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.19.3 |
PCP |
- |
Pyrococcus furiosus |
3.4.19.3 |
pyrrolidone carboxyl peptidase |
- |
Pyrococcus furiosus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.4.19.3 |
80 |
85 |
wild-type enzyme in absence of dithiothreitol |
Pyrococcus furiosus |
3.4.19.3 |
90 |
- |
wild-type enzyme in presence of dithiothreitol |
Pyrococcus furiosus |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
3.4.19.3 |
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]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
3.4.19.3 |
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 |