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Literature summary for 5.6.1.7 extracted from
- An exceptionally stable group II chaperonin from the hyperthermophile Pyrococcus furiosus (2009), Arch. Biochem. Biophys., 486, 12-18.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | protein substrate binding activates ATPase hydrolysis in 3-5 M Gdn-HCl | Pyrococcus furiosus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pyrococcus furiosus |
General Stability
| General Stability | Organism |
|---|---|
| protein substrate binding stabilized the hexadecamer of Pf Cpn in 3 M Gdn-HCl guanidine hydrochloride | Pyrococcus furiosus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| KCl | 50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M) | Pyrococcus furiosus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ | Pyrococcus furiosus | |
| KCl | 50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M) | Pyrococcus furiosus | |
| Mg2+ | ATPase activity of Pf Cpn is dependent on Mg2+ with uniform activity from 1 to 50 mM | Pyrococcus furiosus | |
| Mn2+ | Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ | Pyrococcus furiosus | |
| additional information | recombinant enzyme remains active in high ionic strength | Pyrococcus furiosus | |
| NaCl | 50-500 mM, stimulates ATPase activity. The enzyme maintains full ATPase activity up to 2 M | Pyrococcus furiosus | |
| NH4Cl | 50-500 mM, stimulate ATPase activity. The enzyme maintains full ATPase activity up to 2 M | Pyrococcus furiosus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60000 | - |
16 * 60000, SDS-PAGE | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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
| Organic Solvent | Comment | Organism |
|---|---|---|
| guanidine hydrochloride | protein substrate binding stabilized the hexadecamer of Pf Cpn in 3 M Gdn-HCl guanidine hydrochloride | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| hexadecamer | 16 * 60000, SDS-PAGE | Pyrococcus furiosus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pf Cpn | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
while complexed to heat inactivated lysozyme, Pf Cpn shows increased optimal temperature for ATPase activity from 90°C to 100°C | Pyrococcus furiosus |
| 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]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
while complexed to heat inactivated lysozyme, Pf Cpn shows enhanced thermostability | Pyrococcus furiosus |
| 100 | - |
3 h, 20% loss of activity | Pyrococcus furiosus |
| 105 | - |
t1/2: 141 min | Pyrococcus furiosus |
| 110 | - |
t1/2: 82 min | Pyrococcus furiosus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
- |
Pyrococcus furiosus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 11 | pH 4.0: about 65% of maximal activity, pH 11.0: about 60% of maximal activity | Pyrococcus furiosus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is involved in the primary protein folding pathway during cellular heat shock | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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