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
+
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
ECTree
1.8.2.2 thiosulfate dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.8.2.2 - thiosulfate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C123G
residue probably acts as sixth distal axial ligand of a heme iron, mutant is inactive
K208G
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction
K208N
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction
M209G
site-directed mutagenesis, the mutant is catalytically active in thiosulfate oxidation as well as in tetrathionate reduction
C123G
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residue probably acts as sixth distal axial ligand of a heme iron, mutant is inactive
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N254K
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the enzyme shows 10fold reduced oxidation activity of thiosulfate but has a comparable maximum rate of tetrathionate reduction compared to the wild type enzyme
additional information
additional information
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains. Redox activity of AvTsdA adsorbed on a mesoporous nanocrystalline SnO2 electrode
additional information
-
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains. Redox activity of AvTsdA adsorbed on a mesoporous nanocrystalline SnO2 electrode
additional information
-
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains. Redox activity of AvTsdA adsorbed on a mesoporous nanocrystalline SnO2 electrode
-
additional information
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains
additional information
-
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains
additional information
-
construction of a fusion enzyme of Allochromatium vinosum TsdA and Marichromatium purpuratum TsdBA that reacts efficiently in vitro with high potential iron-sulfur protein from Allochromatium vinosum. High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains
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