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Literature summary extracted from
- Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: a member of a novel protein family related to protein disulfide-isomerase (2004), Eur. J. Biochem., 271, 3437-3448.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | GSSG | required for oxidation activity | Pyrococcus furiosus |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.99.B1 | expression of wild-type and mutant enzymes C35S, C146S and C35S/C146S in Escherichia coli | Pyrococcus furiosus |
| 5.3.4.1 | overexpression of wild-type and mutant enzyme in Escherichia coli strain BL21(DE3) | Pyrococcus furiosus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.8.99.B1 | C146S | not active in the insulin reductase assay, oxidation of the dithiol peptide NRCSQGSCWN is reduced | Pyrococcus furiosus |
| 1.8.99.B1 | C35S | active in the insulin reductase assay, oxidation of the dithiol peptide NRCSQGSCWN is comparable to wild-type enzyme | Pyrococcus furiosus |
| 1.8.99.B1 | C35S/C146S | not active in the insulin reductase assay, no oxidation of the dithiol peptide NRCSQGSCWN | Pyrococcus furiosus |
| 5.3.4.1 | C146S | site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
| 5.3.4.1 | C35A | site-directed mutagenesis, reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
| 5.3.4.1 | C35A/C146S | site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | 8-azido-ATP | for the ATPase activity, binds at the same site as ATP | Pyrococcus furiosus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | Ca2+ | can partially substitute for Mg2+ | Pyrococcus furiosus | |
| 5.3.4.1 | Co2+ | can partially substitute for Mg2+ | Pyrococcus furiosus | |
| 5.3.4.1 | Cu2+ | only 40% as effective as Mg2+ | Pyrococcus furiosus | |
| 5.3.4.1 | Mg2+ | for the ATPase activity, best divalent cation | Pyrococcus furiosus | |
| 5.3.4.1 | Mn2+ | only 30% as effective as Mg2+ | Pyrococcus furiosus | |
| 5.3.4.1 | additional information | enzyme requires divalent cations for ATPase activity, with descending specificity for Mg2+, Co2+, Ca2+, Cu2+, and Mn2+ | Pyrococcus furiosus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.8.99.B1 | 25650 | - |
wild-type enzyme electrospray mass spectroscopy | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.99.B1 | protein-dithiol + oxidized acceptor | Pyrococcus furiosus | intracellular proteins of certain hyperthermophilic archaea are rich in disulfide bonds. Disulfide bonds stabilize many thermostable proteins | protein-disulfide + reduced acceptor | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.99.B1 | Pyrococcus furiosus | Q51760 | - |
- |
| 5.3.4.1 | Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.99.B1 | - |
Pyrococcus furiosus |
| 5.3.4.1 | recombinant wild-type and mutant enzyme from Escherichia coli strain BL21(DE3) by heat precipitation at 80°C, gel filtration, and anion exchange chromatography | Pyrococcus furiosus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | additional information | - |
ATPase activity, Holmgren's turbimetric method for reductive activity measurement utilizing bovine insulin | Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.99.B1 | dithiol peptide NRCSQGSCWN + acceptor | - |
Pyrococcus furiosus | disulfide peptide NRCSQGSCWN + reduced acceptor | - |
? | |
| 1.8.99.B1 | protein-dithiol + oxidized acceptor | intracellular proteins of certain hyperthermophilic archaea are rich in disulfide bonds. Disulfide bonds stabilize many thermostable proteins | Pyrococcus furiosus | protein-disulfide + reduced acceptor | - |
? | |
| 1.8.99.B1 | [insulin]-disulfide + reduced dithiothreitol | - |
Pyrococcus furiosus | [insulin]-dithiol + oxidized dithiothreitol | - |
? | |
| 5.3.4.1 | insulin | disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method | Pyrococcus furiosus | ? | - |
? | |
| 5.3.4.1 | additional information | the enzyme catalyzes dithiol-disulfide exchange reactions with an essential -C-P-Y-C- active site motif with catalytic C35 and C146, enzyme shows oxidative, reductive, and isomerase activities as well as ATPase activity, the latter being related to the enzyme's chaperone function | Pyrococcus furiosus | ? | - |
? | |
| 5.3.4.1 | NRCSQGSCWN | disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG | Pyrococcus furiosus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | dimer | - |
Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.99.B1 | PfPDO | - |
Pyrococcus furiosus |
| 5.3.4.1 | protein disulfide oxidoreductase | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.8.99.B1 | 90 | - |
- |
Pyrococcus furiosus |
| 5.3.4.1 | 30 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
| 5.3.4.1 | 90 | - |
ATPase activity | Pyrococcus furiosus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 45 | 75 | for the oxidation activity | Pyrococcus furiosus |
| 5.3.4.1 | 45 | 90 | for the ATPase activity | Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | additional information | - |
the enzyme is highly thermostable | Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 7 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
| 5.3.4.1 | 10 | - |
ATPase activity | Pyrococcus furiosus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 7 | 10.5 | ATPase activity is maximal at basic pH | Pyrococcus furiosus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | ATP | for the ATPase activity, binding of ATP does not alter the enzyme's conformation, binding structure | Pyrococcus furiosus | |
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