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Literature summary extracted from
- Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins (2012), J. Biochem., 151, 383-390.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | prefoldin | a molecular chaperone that can stabilize tentatively nascent polypeptide chains or non-native forms of mainly cytoskeletal proteins, which are subsequently delivered to group II chaperonin to accomplish their precise folding, effects of Pyrococcus furiosus prefoldin on the refolding reactions of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein differ in the presence or absence of Pyrococcus furiosus chaperonin, PfuCPN. Both prefoldin and chaperonin CPN interact with Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein refolding intermediates. Recombinant expression of prefoldin in Escherichia coli | Pyrococcus furiosus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | recombinant expression of enzyme CPN in Escherichia coli strain BLR(DE3)/pET23a | Pyrococcus furiosus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | prefoldin | inhibits the GFP protein refolding by interacting with intermediates | Pyrococcus furiosus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.6.4.B10 | cytosol | - |
Pyrococcus furiosus | 5829 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.B10 | Co2+ | activates | Pyrococcus furiosus |  |
| 3.6.4.B10 | Mn2+ | activates | Pyrococcus furiosus | |
| 3.6.4.B10 | additional information | no activity with Mg2+ | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | Pyrococcus furiosus | - |
ADP + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.4.B10 | Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.4.B10 | recombinant enzyme CPN from Escherichia coli strain BLR(DE3)/pET23a by heat treatment for 15 min at 90°C, anion exchange chromatography, ultrafiltration, and gel filtration | Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.B10 | ATP + H2O | - |
Pyrococcus furiosus | ADP + phosphate | - |
? | |
| 3.6.4.B10 | additional information | group II chaperonin CPN accomplishes the precise folding of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein in an ATP-dependent manner. Both prefoldin and chaperonin CPN interact with Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein refolding intermediates. Effects on the refolding reaction vary from passive effects such as ATP-dependent binding and release of CPN towards GFP protein and binding which leads to folding arrest, prefoldin towards GFP protein, to active effects such as net increase in thermal stability, CPN towards citrate synthase to an active improvement in refolding yield, prefoldin towards citrate synthase. PfuCPN cannot assist the refolding of Pyrococcus furiosus citrate synthase, but may contribute to maintaining its active form, while prefolding facilitates the refolding of Pyrococcus furiosus citrate synthase | Pyrococcus furiosus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | oligomer | - |
Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | PfCPN | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 60 | - |
assay at | Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.B10 | 7.1 | - |
assay at | Pyrococcus furiosus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.4.B10 | evolution | the enzyme belongs to the group II chaperonins | Pyrococcus furiosus |
| 3.6.4.B10 | physiological function | prefoldin is a molecular chaperone that can stabilize tentatively nascent polypeptide chains or non-native forms of mainly cytoskeletal proteins, which are subsequently delivered to group II chaperonin to accomplish their precise folding, active and passive effects of Pyrococcus furiosus prefoldin on the refolding reactions of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein differ in the presence or absence of Pyrococcus furiosus chaperonin, PfuCPN | Pyrococcus furiosus |
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