Any feedback?
Literature summary extracted from
- A sulfur oxygenase from the haloalkaliphilic bacterium Thioalkalivibrio paradoxus with atypically low reductase Activity (2017), J. Bacteriol., 199, e00675 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.55 | gene AaSOR, phylogenetic analysis, recombinant expression of wild-type and mutant enzymes in Escherichia coli | Aquifex aeolicus |
| 1.13.11.55 | phylogenetic analysis, synthetic gene encoding TpSOR, recombinant expression of wild-type and mutant enzymes in Escherichia coli | Thioalkalivibrio paradoxus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.55 | C113A | site-directed mutagenesis, almost inactive mutant | Thioalkalivibrio paradoxus |
| 1.13.11.55 | C116A | site-directed mutagenesis, almost inactive mutant | Thioalkalivibrio paradoxus |
| 1.13.11.55 | C31A | site-directed mutagenesis, inactive mutant | Aquifex aeolicus |
| 1.13.11.55 | C44A | site-directed mutagenesis, inactive mutant | Thioalkalivibrio paradoxus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.55 | glycine betaine | 25% inhibition at 1 M NaCl, below 10% activity at 3 M, inactive at 4 M NaCl | Thioalkalivibrio paradoxus |  |
| 1.13.11.55 | NaCl | about 80% inhibition at 2 M NaCl, almost inactive at 3 M NaCl | Aquifex aeolicus | |
| 1.13.11.55 | NaCl | 25% inhibition at 1 M NaCl, below 10% activity at 3 M, residual activities of 0.2% of the maximum at 5 M NaCl | Thioalkalivibrio paradoxus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.55 | Fe2+ | low-potential mononuclear non-heme iron bound in the active site | Thioalkalivibrio paradoxus | |
| 1.13.11.55 | additional information | TpSOR activity depends on osmolyte concentrations and not on salt | Thioalkalivibrio paradoxus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 556000 | - |
gel filtration, recombinant enzyme | Thioalkalivibrio paradoxus |
| 1.13.11.55 | 602000 | - |
gel filtration, recombinant enzyme | Aquifex aeolicus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | Aquifex aeolicus | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | Thioalkalivibrio paradoxus | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | Thioalkalivibrio paradoxus Arh 1 | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.55 | Aquifex aeolicus | - |
- |
- |
| 1.13.11.55 | Thioalkalivibrio paradoxus | - |
- |
- |
| 1.13.11.55 | Thioalkalivibrio paradoxus Arh 1 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.55 | recombinant wild-type and mutant enzymes from Escherichia coli | Aquifex aeolicus |
| 1.13.11.55 | recombinant wild-type and mutant enzymes from Escherichia coli | Thioalkalivibrio paradoxus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.13.11.55 | additional information | highest activity of cells at 35-37°C and pH 10.0 | Thioalkalivibrio paradoxus | - |
| 1.13.11.55 | additional information | highest activity of cells at 85°C and pH 6.8 | Aquifex aeolicus | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | additional information | - |
recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production | Thioalkalivibrio paradoxus |
| 1.13.11.55 | 0.03 | - |
purified recombinant enzyme, pH 9.0, 80°C, reductase activity | Thioalkalivibrio paradoxus |
| 1.13.11.55 | 308 | 454 | purified recombinant enzyme, pH 9.0, 80°C, thiosulfate- and sulfite-producing oxygenase activity | Thioalkalivibrio paradoxus |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.13.11.55 | 4°C, purified recombinant enzyme, up to 2 weeks without significant loss of activity, inactivation of the enzyme after 12 weeks, the inactive enzyme shows complete unfolding of the protein | Thioalkalivibrio paradoxus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | - |
Aquifex aeolicus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | - |
Thioalkalivibrio paradoxus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method | Aquifex aeolicus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method | Thioalkalivibrio paradoxus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | - |
Thioalkalivibrio paradoxus Arh 1 | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | 4 sulfur + 4 H2O + O2 | discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method | Thioalkalivibrio paradoxus Arh 1 | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
| 1.13.11.55 | additional information | at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%) | Thioalkalivibrio paradoxus | ? | - |
? | |
| 1.13.11.55 | additional information | at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%) | Thioalkalivibrio paradoxus Arh 1 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.13.11.55 | More | All SORs seem to form highly thermostable 24-subunit hollow spheres | Thioalkalivibrio paradoxus |
| 1.13.11.55 | tetraicosamer | 24 * 35287, sequence calculation | Thioalkalivibrio paradoxus |
| 1.13.11.55 | tetraicosamer | 24 * 37674, sequence calculation | Aquifex aeolicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.55 | AaSOR | - |
Aquifex aeolicus |
| 1.13.11.55 | SOR | - |
Aquifex aeolicus |
| 1.13.11.55 | SOR | - |
Thioalkalivibrio paradoxus |
| 1.13.11.55 | sulfur oxygenase | - |
Aquifex aeolicus |
| 1.13.11.55 | sulfur oxygenase | - |
Thioalkalivibrio paradoxus |
| 1.13.11.55 | sulfur oxygenase reductase | - |
Aquifex aeolicus |
| 1.13.11.55 | sulfur oxygenase reductase | - |
Thioalkalivibrio paradoxus |
| 1.13.11.55 | TpSOR | - |
Thioalkalivibrio paradoxus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 80 | - |
recombinant enzyme | Thioalkalivibrio paradoxus |
| 1.13.11.55 | 85 | - |
recombinant enzyme | Aquifex aeolicus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 40 | 95 | activity range, profile overview. 13.4% of maximal activity at 40°C, maximal activity at 80°C, at pH 9.0 | Thioalkalivibrio paradoxus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 80 | - |
purified recombinant enzyme, a total of 55% of the TpSOR activity is lost after 25 min, and 99% is lost after 60 min | Thioalkalivibrio paradoxus |
| 1.13.11.55 | 85 | - |
purified recombinant enzyme, 45% residual activity after 1 h | Aquifex aeolicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 7.2 | - |
assay at | Aquifex aeolicus |
| 1.13.11.55 | 9 | - |
recombinant enzyme | Thioalkalivibrio paradoxus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.55 | 5.5 | 8 | activity range, profile overview, at 50°C | Aquifex aeolicus |
| 1.13.11.55 | 6.5 | 11.5 | activity range, proflie overview, at 50°C | Thioalkalivibrio paradoxus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.55 | physiological function | the enzyme is involved in the dissimilatory oxidation of sulfur compounds, schematic overview. Sulfur oxygenase reductases (SORs) catalyze a dioxygen-dependent disproportionation reaction of elemental sulfur (S0, consisting mostly of cyclo-octasulfur) with sulfite, thiosulfate, and sulfide as detectable products | Aquifex aeolicus |
| 1.13.11.55 | physiological function | the enzyme is involved in the dissimilatory oxidation of sulfur compounds, schematic overview. Sulfur oxygenase reductases (SORs) catalyze a dioxygen-dependent disproportionation reaction of elemental sulfur (S0, consisting mostly of cyclo-octasulfur) with sulfite, thiosulfate, and sulfide as detectable products. Recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production | Thioalkalivibrio paradoxus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
