1.13.11.55: sulfur oxygenase/reductase
This is an abbreviated version!
For detailed information about sulfur oxygenase/reductase, go to the full flat file.
Word Map on EC 1.13.11.55
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1.13.11.55
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ambivalens
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thiosulfate
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acidianus
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thermoacidophilic
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hollow
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non-heme
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disproportionation
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acidithiobacillus
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acidophil
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sulfobacillus
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tetrathionate
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tokodaii
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heterodisulfide
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bioleaching
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degradation
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low-potential
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caldus
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pharmacology
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industry
- 1.13.11.55
- ambivalens
- thiosulfate
- acidianus
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thermoacidophilic
-
hollow
-
non-heme
-
disproportionation
- acidithiobacillus
-
acidophil
- sulfobacillus
- tetrathionate
- tokodaii
-
heterodisulfide
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bioleaching
- degradation
-
low-potential
- caldus
- pharmacology
- industry
Reaction
4 sulfur + 4 H2O + = 2 hydrogen sulfide + 2 sulfite
Synonyms
AaSOR, SAMN00768000_1627, SAMN00768000_1798, SOR, SOR protein, SOR-AT, sulfur oxygenase, sulfur oxygenase reductase, sulfuroxygenasereductase, sulphur oxygenase reductase, TpSOR, TPY_0405
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General Information
General Information on EC 1.13.11.55 - sulfur oxygenase/reductase
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evolution
metabolism
physiological function
additional information
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the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
evolution
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the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
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sulfur oxygenase reductase is the initial enzyme of the sulfur oxidation pathway in the thermoacidophilic Archaeon Acidianus ambivalens catalyzing an oxygen-dependent sulfur disproportionation to H2S, sulfite and thiosulfate
metabolism
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proposed sulfur metabolism pathways of Sulfobacillus acidophilus strain TPY involving the enzyme, overview
metabolism
the enzyme is involved in the sulfur oxidation metabolism of Acidithiobacillus thiooxidans strain A01, sulfur oxidation model, overview
metabolism
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the enzyme is involved in the sulfur oxidation metabolism of Acidithiobacillus thiooxidans strain A01, sulfur oxidation model, overview
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metabolism
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proposed sulfur metabolism pathways of Sulfobacillus acidophilus strain TPY involving the enzyme, overview
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catalyzes the initial step in the dissimilatory sulfur oxidation pathway
physiological function
initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
physiological function
initial enzyme in the sulfur-oxidation pathway
physiological function
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the enzyme oxidizes the cytoplasmic elemental sulfur, but cannot couple the sulfur oxidation with the electron transfer chain or substrate-level phosphorylation
physiological function
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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
physiological function
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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
physiological function
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initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
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physiological function
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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
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physiological function
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initial enzyme in the sulfur-oxidation pathway
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physiological function
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the enzyme oxidizes the cytoplasmic elemental sulfur, but cannot couple the sulfur oxidation with the electron transfer chain or substrate-level phosphorylation
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modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
additional information
the spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. The expansion of the pores in the outer shell leads to an increased enzyme activity while the integrity of the active site pore seems to be important. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine. Modeling of the SOR and its pores, overview. Opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
additional information
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the spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. The expansion of the pores in the outer shell leads to an increased enzyme activity while the integrity of the active site pore seems to be important. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine. Modeling of the SOR and its pores, overview. Opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
additional information
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three-dimensional modeling of the enzyme, overview
additional information
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modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
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additional information
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three-dimensional modeling of the enzyme, overview
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