Activating Compound | Comment | Organism | Structure |
---|---|---|---|
GSSG | required for oxidation activity | Pyrococcus furiosus |
Cloned (Comment) | Organism |
---|---|
overexpression of wild-type and mutant enzyme in Escherichia coli strain BL21(DE3) | Pyrococcus furiosus |
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 | Comment | Organism | Structure |
---|---|---|---|
8-azido-ATP | for the ATPase activity, binds at the same site as ATP | Pyrococcus furiosus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
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 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 | 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 | Comment | Organism |
---|---|---|
dimer | - |
Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
protein disulfide oxidoreductase | - |
Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
90 | - |
ATPase activity | Pyrococcus furiosus |
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 Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the enzyme is highly thermostable | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at, oxidoreductase and isomerase activity | Pyrococcus furiosus |
10 | - |
ATPase activity | Pyrococcus furiosus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 10.5 | ATPase activity is maximal at basic pH | Pyrococcus furiosus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | for the ATPase activity, binding of ATP does not alter the enzyme's conformation, binding structure | Pyrococcus furiosus |