Literature summary extracted from
Luo, H.; Laksanalamai, P.; Robb, F.T.
An exceptionally stable group II chaperonin from the hyperthermophile Pyrococcus furiosus (2009), Arch. Biochem. Biophys., 486, 12-18.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
5.6.1.7 |
additional information |
protein substrate binding activates ATPase hydrolysis in 3-5 M Gdn-HCl |
Pyrococcus furiosus |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
5.6.1.7 |
expression in Escherichia coli |
Pyrococcus furiosus |
General Stability
EC Number |
General Stability |
Organism |
---|
5.6.1.7 |
protein substrate binding stabilized the hexadecamer of Pf Cpn in 3 M Gdn-HCl guanidine hydrochloride |
Pyrococcus furiosus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
5.6.1.7 |
KCl |
50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M) |
Pyrococcus furiosus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
5.6.1.7 |
Co2+ |
Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ |
Pyrococcus furiosus |
|
5.6.1.7 |
KCl |
50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M) |
Pyrococcus furiosus |
|
5.6.1.7 |
Mg2+ |
ATPase activity of Pf Cpn is dependent on Mg2+ with uniform activity from 1 to 50 mM |
Pyrococcus furiosus |
|
5.6.1.7 |
Mn2+ |
Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ |
Pyrococcus furiosus |
|
5.6.1.7 |
additional information |
recombinant enzyme remains active in high ionic strength |
Pyrococcus furiosus |
|
5.6.1.7 |
NaCl |
50-500 mM, stimulates ATPase activity. The enzyme maintains full ATPase activity up to 2 M |
Pyrococcus furiosus |
|
5.6.1.7 |
NH4Cl |
50-500 mM, stimulate ATPase activity. The enzyme maintains full ATPase activity up to 2 M |
Pyrococcus furiosus |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
5.6.1.7 |
60000 |
- |
16 * 60000, SDS-PAGE |
Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
5.6.1.7 |
ATP + H2O + a folded polypeptide |
Pyrococcus furiosus |
Pf Cpn protects protein from inactivation and aggregation in an ATP dependent manner |
ADP + phosphate + an unfolded polypeptide |
- |
? |
|
Organic Solvent Stability
EC Number |
Organic Solvent |
Comment |
Organism |
---|
5.6.1.7 |
guanidine hydrochloride |
protein substrate binding stabilized the hexadecamer of Pf Cpn in 3 M Gdn-HCl guanidine hydrochloride |
Pyrococcus furiosus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.6.1.7 |
Pyrococcus furiosus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.6.1.7 |
- |
Pyrococcus furiosus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.6.1.7 |
ATP + H2O + a folded polypeptide |
Pf Cpn protects protein from inactivation and aggregation in an ATP dependent manner |
Pyrococcus furiosus |
ADP + phosphate + an unfolded polypeptide |
- |
? |
|
5.6.1.7 |
ATP + H2O + a folded polypeptide |
Pf Cpn binds specifically to denatured lysozyme. ATP addition results in protection of lysozyme from aggregation and inactivation at 100°C. While complexed to heat inactivated lysozyme, Pf Cpn shows enhanced ATPase activity |
Pyrococcus furiosus |
ADP + phosphate + an unfolded polypeptide |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.6.1.7 |
hexadecamer |
16 * 60000, SDS-PAGE |
Pyrococcus furiosus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
5.6.1.7 |
Pf Cpn |
- |
Pyrococcus furiosus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
5.6.1.7 |
90 |
- |
while complexed to heat inactivated lysozyme, Pf Cpn shows increased optimal temperature for ATPase activity from 90°C to 100°C |
Pyrococcus furiosus |
5.6.1.7 |
100 |
- |
while complexed to heat inactivated lysozyme, Pf Cpn shows increased optimal temperature for ATPase activity from 90°C to 100°C |
Pyrococcus furiosus |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
5.6.1.7 |
additional information |
- |
while complexed to heat inactivated lysozyme, Pf Cpn shows enhanced thermostability |
Pyrococcus furiosus |
5.6.1.7 |
100 |
- |
3 h, 20% loss of activity |
Pyrococcus furiosus |
5.6.1.7 |
105 |
- |
t1/2: 141 min |
Pyrococcus furiosus |
5.6.1.7 |
110 |
- |
t1/2: 82 min |
Pyrococcus furiosus |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
5.6.1.7 |
7.2 |
- |
- |
Pyrococcus furiosus |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
5.6.1.7 |
4 |
11 |
pH 4.0: about 65% of maximal activity, pH 11.0: about 60% of maximal activity |
Pyrococcus furiosus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
5.6.1.7 |
physiological function |
the enzyme is involved in the primary protein folding pathway during cellular heat shock |
Pyrococcus furiosus |