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Literature summary extracted from
- Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (2006), FEBS J., 273, 5407-5420.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.1.B4 | expression in Escherichia coli | Saccharolobus solfataricus |
| 1.8.99.B1 | expression in Escherichia coli | Saccharolobus solfataricus |
| 5.3.4.1 | expression in Escherichia coli | Saccharolobus solfataricus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.B4 | 0.0003 | - |
[protein disulfide oxidoreductase]-disulfide | pH 7.0, 60°C | Saccharolobus solfataricus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.8.99.B1 | 26032 | - |
x * 26032, calculated from sequence | Saccharolobus solfataricus |
| 1.8.99.B1 | 27100 | - |
gel filtration, electrospray mass spectrometry | Saccharolobus solfataricus |
| 5.3.4.1 | 26032 | - |
x * 26032, calculated from sequence | Saccharolobus solfataricus |
| 5.3.4.1 | 27100 | - |
gel filtration, electrospray mass spectrometry | Saccharolobus solfataricus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | Saccharolobus solfataricus | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? |  |
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | Saccharolobus solfataricus P2 | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.B4 | Saccharolobus solfataricus | Q97W27 | - |
- |
| 1.8.1.B4 | Saccharolobus solfataricus P2 | Q97W27 | - |
- |
| 1.8.99.B1 | Saccharolobus solfataricus | Q980T5 | - |
- |
| 1.8.99.B1 | Saccharolobus solfataricus P2 | Q980T5 | - |
- |
| 5.3.4.1 | Saccharolobus solfataricus | Q980T5 | - |
- |
| 5.3.4.1 | Saccharolobus solfataricus P2 | Q980T5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.B4 | - |
Saccharolobus solfataricus |
| 1.8.99.B1 | - |
Saccharolobus solfataricus |
| 5.3.4.1 | - |
Saccharolobus solfataricus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus | Saccharolobus solfataricus | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? | |
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232) | Saccharolobus solfataricus | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? | |
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus | Saccharolobus solfataricus P2 | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? | |
| 1.8.1.B4 | [protein disulfide oxidoreductase]-disulfide + NADPH + H+ | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232) | Saccharolobus solfataricus P2 | [protein disulfide oxidoreductase]-dithiol + NADP+ | - |
? | |
| 1.8.99.B1 | [insulin]-disulfide + reduced dithiothreitol | - |
Saccharolobus solfataricus | [insulin]-dithiol + oxidized dithiothreitol | - |
? | |
| 1.8.99.B1 | [insulin]-disulfide + reduced dithiothreitol | - |
Saccharolobus solfataricus P2 | [insulin]-dithiol + oxidized dithiothreitol | - |
? | |
| 5.3.4.1 | scrambled RNAse A | the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity | Saccharolobus solfataricus | ? | - |
? | |
| 5.3.4.1 | scrambled RNAse A | the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity | Saccharolobus solfataricus P2 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.99.B1 | ? | x * 26032, calculated from sequence | Saccharolobus solfataricus |
| 5.3.4.1 | ? | x * 26032, calculated from sequence | Saccharolobus solfataricus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.B4 | SSO2416 | locus name | Saccharolobus solfataricus |
| 1.8.1.B4 | SsTR | - |
Saccharolobus solfataricus |
| 1.8.99.B1 | protein disulfide oxidoreductase | - |
Saccharolobus solfataricus |
| 1.8.99.B1 | SSO0192 | locus name | Saccharolobus solfataricus |
| 1.8.99.B1 | SsPDO | - |
Saccharolobus solfataricus |
| 5.3.4.1 | protein disulfide oxidoreductase | - |
Saccharolobus solfataricus |
| 5.3.4.1 | SSO0192 | locus name | Saccharolobus solfataricus |
| 5.3.4.1 | SsPDO | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.B4 | 60 | - |
assay at | Saccharolobus solfataricus |
| 1.8.99.B1 | 30 | - |
assay at | Saccharolobus solfataricus |
| 5.3.4.1 | 30 | - |
assay at | Saccharolobus solfataricus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.B4 | 7 | - |
assay at | Saccharolobus solfataricus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.B4 | FAD | the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors | Saccharolobus solfataricus | |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.8.99.B1 | Saccharolobus solfataricus | calculated from sequence | - |
4.7 |
| 5.3.4.1 | Saccharolobus solfataricus | calculated from sequence | - |
4.7 |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.8.99.B1 | Saccharolobus solfataricus | when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment | up |
| 5.3.4.1 | Saccharolobus solfataricus | when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment | up |
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