Cloned (Comment) | Organism |
---|---|
gene AaSOR, phylogenetic analysis, recombinant expression of wild-type and mutant enzymes in Escherichia coli | Aquifex aeolicus |
phylogenetic analysis, synthetic gene encoding TpSOR, recombinant expression of wild-type and mutant enzymes in Escherichia coli | Thioalkalivibrio paradoxus |
Protein Variants | Comment | Organism |
---|---|---|
C113A | site-directed mutagenesis, almost inactive mutant | Thioalkalivibrio paradoxus |
C116A | site-directed mutagenesis, almost inactive mutant | Thioalkalivibrio paradoxus |
C31A | site-directed mutagenesis, inactive mutant | Aquifex aeolicus |
C44A | site-directed mutagenesis, inactive mutant | Thioalkalivibrio paradoxus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glycine betaine | 25% inhibition at 1 M NaCl, below 10% activity at 3 M, inactive at 4 M NaCl | Thioalkalivibrio paradoxus | |
NaCl | about 80% inhibition at 2 M NaCl, almost inactive at 3 M NaCl | Aquifex aeolicus | |
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 | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | low-potential mononuclear non-heme iron bound in the active site | Thioalkalivibrio paradoxus | |
additional information | TpSOR activity depends on osmolyte concentrations and not on salt | Thioalkalivibrio paradoxus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
556000 | - |
gel filtration, recombinant enzyme | Thioalkalivibrio paradoxus |
602000 | - |
gel filtration, recombinant enzyme | Aquifex aeolicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 sulfur + 4 H2O + O2 | Aquifex aeolicus | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
4 sulfur + 4 H2O + O2 | Thioalkalivibrio paradoxus | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
4 sulfur + 4 H2O + O2 | Thioalkalivibrio paradoxus Arh 1 | - |
2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
Thioalkalivibrio paradoxus | - |
- |
- |
Thioalkalivibrio paradoxus Arh 1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli | Aquifex aeolicus |
recombinant wild-type and mutant enzymes from Escherichia coli | Thioalkalivibrio paradoxus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | highest activity of cells at 35-37°C and pH 10.0 | Thioalkalivibrio paradoxus | - |
additional information | highest activity of cells at 85°C and pH 6.8 | Aquifex aeolicus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production | Thioalkalivibrio paradoxus |
0.03 | - |
purified recombinant enzyme, pH 9.0, 80°C, reductase activity | Thioalkalivibrio paradoxus |
308 | 454 | purified recombinant enzyme, pH 9.0, 80°C, thiosulfate- and sulfite-producing oxygenase activity | Thioalkalivibrio paradoxus |
Storage Stability | Organism |
---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 sulfur + 4 H2O + O2 | - |
Aquifex aeolicus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
4 sulfur + 4 H2O + O2 | - |
Thioalkalivibrio paradoxus | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
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+ | - |
? | |
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+ | - |
? | |
4 sulfur + 4 H2O + O2 | - |
Thioalkalivibrio paradoxus Arh 1 | 2 hydrogen sulfide + 2 HSO3- + 2 H+ | - |
? | |
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+ | - |
? | |
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 | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
More | All SORs seem to form highly thermostable 24-subunit hollow spheres | Thioalkalivibrio paradoxus |
tetraicosamer | 24 * 35287, sequence calculation | Thioalkalivibrio paradoxus |
tetraicosamer | 24 * 37674, sequence calculation | Aquifex aeolicus |
Synonyms | Comment | Organism |
---|---|---|
AaSOR | - |
Aquifex aeolicus |
SOR | - |
Aquifex aeolicus |
SOR | - |
Thioalkalivibrio paradoxus |
sulfur oxygenase | - |
Aquifex aeolicus |
sulfur oxygenase | - |
Thioalkalivibrio paradoxus |
sulfur oxygenase reductase | - |
Aquifex aeolicus |
sulfur oxygenase reductase | - |
Thioalkalivibrio paradoxus |
TpSOR | - |
Thioalkalivibrio paradoxus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
recombinant enzyme | Thioalkalivibrio paradoxus |
85 | - |
recombinant enzyme | Aquifex aeolicus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
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 Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
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 |
85 | - |
purified recombinant enzyme, 45% residual activity after 1 h | Aquifex aeolicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Aquifex aeolicus |
9 | - |
recombinant enzyme | Thioalkalivibrio paradoxus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8 | activity range, profile overview, at 50°C | Aquifex aeolicus |
6.5 | 11.5 | activity range, proflie overview, at 50°C | Thioalkalivibrio paradoxus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |