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
-
thermoacidophilic
-
hollow
-
non-heme
-
disproportionation
- acidithiobacillus
-
acidophil
- sulfobacillus
- tetrathionate
- tokodaii
-
heterodisulfide
-
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
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.55 - sulfur oxygenase/reductase
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Fe
iron content: 0.45 mol per mol subunit for recombinant wild-type enzyme, below 0.1 mol per mol subunit for mutant enzyme H86A, below 0.02 mol per mol subunit for mutant enzyme H90A, below 0.01 mol per mol subunit for mutant enzyme E114A, 0.02 mol per mol subunit for mutant enzyme E114D, 0.47 mol per mol subunit for mutant enzyme C31A, 0.42 mol per mol subunit for mutant enzyme C31S, 0.22 mol per mol subunit for mutant enzyme C101A, below 0.03 mol per mol subunit for mutant enzyme C101S, 0.19 mol per mol subunit for mutant enzyme C104A, 0.3 mol per mol subunit for mutant enzyme C104S, 0.56 mol per mol subunit for mutant enzyme C101A/C104A, 0.4 mol per mol subunit for mutant enzyme C101S/C104S
Fe2+
Iron
Zn2+
additional information
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TpSOR activity depends on osmolyte concentrations and not on salt
Fe2+
non-heme iron. 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
Fe2+
essential for activity, recombinant SOR had a molar ratio of 1.86:1 (iron to subunit of SOR), excesses of ferric and ferrous ions have inhibitory effect on SOR activity
Fe2+
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low-potential mononuclear non-heme iron bound in the active site
low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitutes the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction
Iron
the enzyme contains a low-potential mononuclear non-heme iron centre, which has a reduction potential of -268 mV at pH 6.5, one iron atom per subunit
Iron
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at the catalytic center, iron is ligated to His86, His90, Glu114, and two water molecules