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Literature summary for 5.3.4.1 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
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GSSG | required for oxidation activity | Pyrococcus furiosus |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of wild-type and mutant enzyme in Escherichia coli strain BL21(DE3) | Pyrococcus furiosus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C146S | site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
| C35A | site-directed mutagenesis, reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
| C35A/C146S | site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme | Pyrococcus furiosus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 8-azido-ATP | for the ATPase activity, binds at the same site as ATP | Pyrococcus furiosus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | can partially substitute for Mg2+ | Pyrococcus furiosus | |
| Co2+ | can partially substitute for Mg2+ | Pyrococcus furiosus | |
| Cu2+ | only 40% as effective as Mg2+ | Pyrococcus furiosus | |
| Mg2+ | for the ATPase activity, best divalent cation | Pyrococcus furiosus | |
| Mn2+ | only 30% as effective as Mg2+ | Pyrococcus furiosus | |
| additional information | enzyme requires divalent cations for ATPase activity, with descending specificity for Mg2+, Co2+, Ca2+, Cu2+, and Mn2+ | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
ATPase activity, Holmgren's turbimetric method for reductive activity measurement utilizing bovine insulin | Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| insulin | disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method | Pyrococcus furiosus | ? | - |
? | |
| 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 | ? | - |
? | |
| NRCSQGSCWN | disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG | Pyrococcus furiosus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Pyrococcus furiosus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| protein disulfide oxidoreductase | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
| 90 | - |
ATPase activity | Pyrococcus furiosus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 75 | for the oxidation activity | Pyrococcus furiosus |
| 45 | 90 | for the ATPase activity | Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme is highly thermostable | Pyrococcus furiosus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
| 10 | - |
ATPase activity | Pyrococcus furiosus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 10.5 | ATPase activity is maximal at basic pH | Pyrococcus furiosus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | for the ATPase activity, binding of ATP does not alter the enzyme's conformation, binding structure | Pyrococcus furiosus | |
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