1.8.2.2: thiosulfate dehydrogenase
This is an abbreviated version!
For detailed information about thiosulfate dehydrogenase, go to the full flat file.
Word Map on EC 1.8.2.2
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1.8.2.2
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sulfur
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sulfite
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thiobacillus
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rhodanese
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sulfur-oxidizing
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chemolithoautotrophic
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ferrooxidans
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vinosum
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allochromatium
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paracoccus
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acidithiobacillus
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thiooxidans
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tn5-mob
- 1.8.2.2
- sulfur
- sulfite
- thiobacillus
- rhodanese
-
sulfur-oxidizing
-
chemolithoautotrophic
- ferrooxidans
- vinosum
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allochromatium
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paracoccus
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acidithiobacillus
- thiooxidans
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tn5-mob
Reaction
2 thiosulfate + = + 2 ferrocytochrome c + 4 H+
Synonyms
AFE_0042, Alvin_0091, AvTsdA, C8J_0815, D0Y83_01395, di-heme TsdA, DIE28_04650, diheme cytochrome c TsdA, enzymes, thiosulfate-oxidizing, MpTsdBA, oxidase, thiosulfate, Tat pathway signal sequence domain protein, tetrathionate reductase, tetrathionate synthase, thiosulfate dehydrogenase, thiosulfate oxidase, thiosulfate-acceptor oxidoreductase, thiosulfate-oxidizing enzyme, TSD, TsdA
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General Information
General Information on EC 1.8.2.2 - thiosulfate dehydrogenase
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evolution
metabolism
physiological function
additional information
the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins
evolution
the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins
evolution
-
the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins
-
evolution
-
the enzyme belongs to the thiosulfate dehydrogenase (TsdA) family. Axial ligation by histidine and cysteine is typical for the active site of TsdA proteins
-
enzyme activity is detected in strains grown on tetrathionate or sulfur, but no activity is detected in ferrous iron-grown cells
metabolism
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the enzyme oxidizes thiosulfate in a bifurcated manner and uses two different pathways. The primary pathway is Sox (Kelly-Friedrich) pathway, which operates under normal physiological condition and oxidizes thiosulfate to sulfate and transfers electron to cytochrome c to cytochrome c oxidase. However, under acidic condition (pH less than 6.0) and low concentration of thiosulfate, this bacterium may use quinone for thiosulfate oxidation by transferring electron through quinone pool to bd oxidase
metabolism
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the enzyme oxidizes thiosulfate in a bifurcated manner and uses two different pathways. The primary pathway is Sox (Kelly-Friedrich) pathway, which operates under normal physiological condition and oxidizes thiosulfate to sulfate and transfers electron to cytochrome c to cytochrome c oxidase. However, under acidic condition (pH less than 6.0) and low concentration of thiosulfate, this bacterium may use quinone for thiosulfate oxidation by transferring electron through quinone pool to bd oxidase
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a gene deletion mutant does not produce any tetrathionate from thiosulfate during growth at pH 7.2 or 6.9
physiological function
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growth of the microaerophilic mucosal pathogen Campylobacter jejuni under oxygen-limited conditions is stimulated by tetrathionate. A tsdA null mutant still slowly reduces, but can not grow on, tetrathionate under oxygen limitation, lacks thiosulfate-dependent respiration and fails to convert thiosulfate to tetrathionate microaerobically. Physiological role for Campylobacter jejuni TsdA is a tetrathionate reductase
physiological function
the enzyme catalyzes the oxidative condensation of two thiosulfate anions, a reaction that is widespread among prokaryotes
physiological function
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
-
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
-
physiological function
-
a gene deletion mutant does not produce any tetrathionate from thiosulfate during growth at pH 7.2 or 6.9
-
physiological function
-
the enzyme catalyzes the oxidative condensation of two thiosulfate anions, a reaction that is widespread among prokaryotes
-
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
-
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
-
physiological function
-
growth of the microaerophilic mucosal pathogen Campylobacter jejuni under oxygen-limited conditions is stimulated by tetrathionate. A tsdA null mutant still slowly reduces, but can not grow on, tetrathionate under oxygen limitation, lacks thiosulfate-dependent respiration and fails to convert thiosulfate to tetrathionate microaerobically. Physiological role for Campylobacter jejuni TsdA is a tetrathionate reductase
-
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states In Allochromatium vinosum TsdA, heme 2 reduction triggers a switch from His/Lys ligation to His/Met, but the rates of interconversion are such that His/Lys ligation is retained during turnover. Thiosulfate oxidation by enzyme AvTsdA provides electrons for photosynthesis
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Cys96 is an essential residue for catalysis
additional information
thiosulfate dehydrogenase is a periplasmic, monomeric 27.2 kDa diheme c-type cytochrome with an activity optimum at pH 4.0
additional information
-
thiosulfate dehydrogenase is a periplasmic, monomeric 27.2 kDa diheme c-type cytochrome with an activity optimum at pH 4.0
additional information
-
thiosulfate dehydrogenase is a periplasmic, monomeric 27.2 kDa diheme c-type cytochrome with an activity optimum at pH 4.0
-