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IUBMB Comments The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1 , cytochrome-c 3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5 , dissimilatory sulfite reductase.
The enzyme appears in viruses and cellular organisms
Synonyms MARPU_02550 , PsrA, thiosulfate reductase, TsdA, more
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thiosulfate reductase
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MARPU_02550
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TsdA
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sulfite + hydrogen sulfide + 2 ferricytochrome c3 = thiosulfate + 2 ferrocytochrome c3
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MetaCyc
thiosulfate disproportionation II (cytochrome)
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sulfite,hydrogen sulfide:ferricytochrome-c3 oxidoreductase (thiosulfate-forming)
The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5, dissimilatory sulfite reductase.
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thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
Megalodesulfovibrio gigas
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Substrates: - Products: -
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thiosulfate + reduced benzyl viologen
sulfite + hydrogen sulfide + oxidized benzyl viologen
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Substrates: - Products: about 50% of the rate with methyl viologen
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
additional information
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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Substrates: - Products: -
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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Substrates: - Products: -
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
Megalodesulfovibrio gigas
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Substrates: - Products: -
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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Substrates: - Products: -
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additional information
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Substrates: with inner- and outer-labeled 35S-thiosulfate, the enzyme reduces only the outer sulfur atom to hydrogen sulfide. No substrates: sulfate, sulfite, tetrathionate, dithionate. No electron donors: reduced nicotinamide adenine dinucleotide, reduced nicotinamide adenine dinucleotide phosphate, reduced glutathione, or cysteine Products: -
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additional information
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Substrates: the enzyme catalyzes the reductive dismutation of thiosulfate to sulfide and sulfite. The outer sulfur atom of thiosulfate is reduced to sulfide and the inner sulfur atom is released as sulfite Products: -
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additional information
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Megalodesulfovibrio gigas
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Substrates: enzyme catalyzes the stoichiometric production of hydrogen sulfide and sulfite from thiosulfate. The most efficient coupling is obtained with a system containing cytochromes c3. The enzyme exhibits tetrathionate reductase activity. It does not show sulfite reductase activity Products: -
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thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
Megalodesulfovibrio gigas
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Substrates: - Products: -
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cytochrome c
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presence of a cytochrome that may be an intermediary hydrogen carrier involved in reducing systems for sulfate and other sulfur compounds
cytochrome c3
Megalodesulfovibrio gigas
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4-chloromercuribenzoate
Megalodesulfovibrio gigas
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0.02 mM, 100% inhibition. Inhibition can be partially or completely reversed by cysteine
4-hydroxymercuribenzoate
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activity can be restored by cysteine
Ag+
Megalodesulfovibrio gigas
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0.01 mM, 90% inhibition
Hg2+
Megalodesulfovibrio gigas
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0.01 mM, 100% inhibition
iodoacetate
Megalodesulfovibrio gigas
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0.5 mM, 70% inhibition
o-Iodosobenzoate
Megalodesulfovibrio gigas
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0.05 mM, 52% inhibition
N-ethylmaleimide
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N-ethylmaleimide
Megalodesulfovibrio gigas
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0.5 mM, 55% inhibition
sulfite
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sulfite
Megalodesulfovibrio gigas
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3 mM, 45% inhibition
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0.5
thiosulfate
Megalodesulfovibrio gigas
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37°C, pH 7.6
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41
Megalodesulfovibrio gigas
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37°C, pH 7.6
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7.4 - 8
Megalodesulfovibrio gigas
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-
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8.8
Megalodesulfovibrio gigas
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8% of maximum activity
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brenda
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brenda
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UniProt
brenda
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UniProt
brenda
Megalodesulfovibrio gigas
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brenda
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brenda
sulfate-reducing bacteria
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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A0A3U7JSZ7_SALET
758
0
82783
TrEMBL
-
A0A0D6FIB2_SALTM
758
0
82800
TrEMBL
-
A0A8G0U1C8_SHEPU
760
0
83226
TrEMBL
-
A0A8F2UVJ9_SALET
758
0
82799
TrEMBL
-
A0A5H9E5A6_SALET
758
0
82800
TrEMBL
-
A0A3V8XNX3_SALMO
758
0
82812
TrEMBL
-
A0A1R2ZV02_SALEN
758
0
82800
TrEMBL
-
A0A3T3INT7_SALDU
758
0
82800
TrEMBL
-
A0A8E6KLT5_SALET
758
0
82800
TrEMBL
-
A0A8E9YQR7_SALET
758
0
82798
TrEMBL
-
A0A8E7QNP8_SALET
758
0
82798
TrEMBL
-
A0A0R9PAL2_SALNE
758
0
82698
TrEMBL
-
Q8Z5K4_SALTI
758
0
82758
TrEMBL
-
A0A603N5N2_SALET
758
0
82812
TrEMBL
-
A0A8E6S1R4_SALER
758
0
82740
TrEMBL
-
A0A8E6SHP5_SALER
758
0
82797
TrEMBL
-
A0A8E5U910_9ENTR
758
0
82800
TrEMBL
-
A0A3V9X0M8_SALNE
758
0
82800
TrEMBL
-
A0A8E6UZU3_SALER
758
0
82798
TrEMBL
-
A0A379SK78_SALER
758
0
82699
TrEMBL
-
A0A4Y6N3J0_SALET
758
0
82698
TrEMBL
-
A0A5B8R3X3_9GAMM
760
0
83286
TrEMBL
-
A0A8F7UMF0_SALER
758
0
82728
TrEMBL
-
A0A8E6MZ01_SALNE
758
0
82800
TrEMBL
-
A0A8F6SBR4_SALET
758
0
82812
TrEMBL
-
A0A8E7CR62_SALPU
758
0
82834
TrEMBL
-
A0A550ABY1_9GAMM
Shewanella eurypsychrophilus
760
0
83052
TrEMBL
-
A0A3T3EK24_SALMU
758
0
82800
TrEMBL
-
A0A702JA86_SALET
758
0
82855
TrEMBL
-
A0A8F6S2W2_SALET
758
0
82811
TrEMBL
-
A0A6Y2KPN4_SALDZ
758
0
82625
TrEMBL
-
A0A3V5UTW2_SALET
758
0
82830
TrEMBL
-
A0A3Z0MCV2_SALET
758
0
82812
TrEMBL
-
A0A8E6RUU2_SALET
758
0
82840
TrEMBL
-
A0A5I1XLL9_SALET
758
0
82829
TrEMBL
-
A0A8G0X0X8_SHEPU
760
0
83060
TrEMBL
-
A0A3V2KPB6_SALTM
758
0
82818
TrEMBL
-
A0A8E7V514_SALDU
758
0
82830
TrEMBL
-
A0A8E6MKY9_SALER
758
0
82735
TrEMBL
-
A0A8F7Y9U6_SALER
758
0
82728
TrEMBL
-
A0A5J1IDI6_SALET
758
0
82829
TrEMBL
-
A0A2D1VKL2_SALET
758
0
82800
TrEMBL
-
A0A8E5JP55_SALEN
758
0
82800
TrEMBL
-
A0A8F5N4T3_SALDZ
758
0
82709
TrEMBL
-
A0A3Z3FQR1_SALER
758
0
82705
TrEMBL
-
A0A658B2Q4_SALET
758
0
82794
TrEMBL
-
A0A8E6U964_SALET
758
0
82740
TrEMBL
-
A0A8F9Z0Q8_SALET
758
0
82812
TrEMBL
-
A0A8E6NL56_SALET
758
0
82782
TrEMBL
-
A0A3Z6DPQ8_SALET
758
0
82800
TrEMBL
-
A0A8E9YIF8_SALDZ
758
0
82794
TrEMBL
-
A0A8E5U142_9ENTR
758
0
82800
TrEMBL
-
A0A8E9Z7P2_SALER
758
0
82768
TrEMBL
-
A0A8E6JLZ2_SALTM
758
0
82800
TrEMBL
-
A0A8E7VPU1_SALRU
758
0
82811
TrEMBL
-
W0DW89_MARPU
541
0
56656
TrEMBL
-
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16300
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sedimentation equilibrium centrifugation
220000
Megalodesulfovibrio gigas
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gel filtration
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monomer
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1 * 15500, amino acid analysis
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additional information
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presence of two half-cystine residues per mole of enzyme
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three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3
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enzyme loses activtiy upon freezing and thawing
Megalodesulfovibrio gigas
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-20°C, 33% loss of activity within 2 weeks
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-20°C, lyophilized preparation, stable for at least 1 month
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unstable during purification
Megalodesulfovibrio gigas
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Hatchikian, E.
Purification and properties of thiosulfate reductase from Desulfovibrio gigas
Arch. Microbiol.
105
249-256
1975
Megalodesulfovibrio gigas
brenda
Haschke, R.; Campbell, L.
Thiosulfate reductase of Desulfovibrio vulgaris
J. Bacteriol.
106
603-607
1971
Desulfovibrio vulgaris
brenda
Nakatsukasa, W.; Akagi, J.
Thiosulfate reductase isolated from Desulfotomaculum nigrificans
J. Bacteriol.
98
429-433
1969
Desulfotomaculum nigrificans
brenda
Ishimoto, M.; Koyama, J.
Biochemical studies on sulfate-reducing bacteria: VI. separation of hydrogenase and thiosulfate reductase and partial purification of cytochrome and green pigment
J. Biochem.
44
233-242
1957
uncultured bacterium
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brenda
Kurth, J.M.; Brito, J.A.; Reuter, J.; Flegler, A.; Koch, T.; Franke, T.; Klein, E.M.; Rowe, S.F.; Butt, J.N.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase
J. Biol. Chem.
291
24804-24818
2016
Marichromatium purpuratum (W0DW89), Marichromatium purpuratum 984 (W0DW89)
brenda
Yu, Q.; Sun, W.; Gao, H.
Thiosulfate oxidation in sulfur-reducing Shewanella oneidensis and its unexpected influences on the cytochrome c content
Environ. Microbiol.
23
7056-7072
2021
Shewanella oneidensis
brenda
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