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Literature summary for 1.8.99.B1 extracted from
- Sulfolobus solfataricus thiol redox puzzle characterization of an atypical protein disulfide oxidoreductase (2014), Extremophiles, 18, 219-228 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Sso1120, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21-Codon Plus (DE3)RIL | Saccharolobus solfataricus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant enzyme, hanging-drop vapor-diffusion method, mixing of 0.001 ml of 5.5 mg/ml protein solution with 0.001 ml of reservoir solution containing 13% PEG 20000, and 0.1 M MES buffer, pH 6.0, method optimization, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular modelling | Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q97Z21 | - |
- |
| Saccharolobus solfataricus P2 | Q97Z21 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21-Codon Plus (DE3)RIL by ultracentrifugation, heat treatment at 70°C for 20 min, metal chelating affinity chromatography, dialysis, anion exchange chromatography, and again dialysis | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| insulin disulfide + reduced thioredoxin | with NADPH and FAD | Saccharolobus solfataricus | insulin dithiol + oxidized thioredoxin | - |
? |  |
| insulin disulfide + reduced thioredoxin | with NADPH and FAD | Saccharolobus solfataricus P2 | insulin dithiol + oxidized thioredoxin | - |
? | |
| additional information | 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) reduction method is used. The enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase | Saccharolobus solfataricus | ? | - |
? | |
| additional information | 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) reduction method is used. The enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase | Saccharolobus solfataricus P2 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | primary structure analysis revealed presence of two Trx units, like in the other PDOs, but only one potential redox site, fitting the sequence of a CXXC motif. Two additional cysteine residues, Cys24 and Cys45, are also present compared to other PDOs | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glutaredoxin related protein | UniProt | Saccharolobus solfataricus |
| PDO | - |
Saccharolobus solfataricus |
| Sso1120 | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 30 | assay at | Saccharolobus solfataricus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 90 | stable up to 85°C, enzyme melting point, circular dichroism spectroscopy thermal denaturation study | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Saccharolobus solfataricus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Saccharolobus solfataricus | |
| NADPH | - |
Saccharolobus solfataricus | |
| thioredoxin | - |
Saccharolobus solfataricus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the thioredoxin (Trx) superfamily. Its crystal structure shows differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium, PDO structure comparisons | Saccharolobus solfataricus |
| additional information | Sso1120 active site region structure, overview | Saccharolobus solfataricus |
| physiological function | PDOs are proteins involved in disulfide bond formation | Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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