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EC Tree
IUBMB Comments The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
tetrathionate-forming thiosulfate dehydrogenase, thiosulfate oxidoreductase, thiosulfate oxidoreductase tetrathionate-forming, thiosulfate:quinone oxidoreductase, thiosulphate:quinone oxidoreductase, TQO, TSD,
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tetrathionate-forming thiosulfate dehydrogenase
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thiosulfate oxidoreductase
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thiosulfate oxidoreductase tetrathionate-forming
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thiosulfate:quinone oxidoreductase
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thiosulphate:quinone oxidoreductase
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2 thiosulfate + 6-decylubiquinone = tetrathionate + 6-decylubiquinol
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thiosulfate:6-decylubiquinone oxidoreductase
The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor.
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2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
the physiological electron acceptor is most probably a caldariella quinone type quinone
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r
tetrathionate + reduced methylene blue
thiosulfate + oxidized methylene blue
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
thiosulfate + ferricyanide + H+
tetrathionate + ferrocyanide
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when the concentration of thiosulfate is lower than 4 mM, no enzyme activity is detected
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?
additional information
?
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thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
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?, r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
the enzyme couples sulfur compound oxidation with quinone reduction
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?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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?, r
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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r
additional information
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horse heart cytochrome c is not reduced
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?
additional information
?
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horse heart cytochrome c is not reduced
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?
additional information
?
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the enzyme reduces neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor
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?
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2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
the physiological electron acceptor is most probably a caldariella quinone type quinone
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
the enzyme couples sulfur compound oxidation with quinone reduction
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?
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additional information
a mixture of caldariella quinone, Sulfolobus quinone and menaquinone is non-covalently bound to the protein
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additional information
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a mixture of caldariella quinone, Sulfolobus quinone and menaquinone is non-covalently bound to the protein
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additional information
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does not contain heme
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Dithionite
1 mM, complete inhibition
Metabisulfite
1 mM, complete inhibition
N-ethylmaleimide
1 mM, 54% inhibition
reduced titanium citrate
1 mM, 65% inhibition
Sodium sulfate
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60% reduction in enzyme activity is observed in the reaction mixture containing 200 mM sodium sulfate
Triton X-100
1%, complete inhibition
Zn2+
1 mM, 37% inhibition, 5 mM, 82% inhibition
sulfite
0.005 mM, 48% inhibition, 0.05 mM, complete inhibition
sulfite
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almost complete inhibition in the presence of 10 mM sulfite
additional information
no inhibition by sulfate or tetrathionate
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additional information
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no inhibition by sulfate or tetrathionate
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Sodium sulfate
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the purified enzyme requires 150 mM sodium sulfate to generate maximum activity
sulfite
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the addition of sulfite (2 mM) results in the activation of the enzyme at a magnitude of 1.6fold
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0.00587 - 0.0059
6-decylubiquinone
0.00587
6-decylubiquinone
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0.0059
6-decylubiquinone
80°C, pH 6.0
3.4
ferricyanide
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3.4
ferricyanide
80°C, pH 6.0
2.6
thiosulfate
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2.6
thiosulfate
80°C, pH 6.0
8
thiosulfate
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recombinant enzyme, at pH 2.5 and 50°C
15
thiosulfate
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native enzyme, at pH 2.5 and 70°C
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167
thiosulfate
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167
thiosulfate
80°C, pH 6.0
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0.005
sulfite
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0.005
sulfite
pH 6.0, 80°C
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0.05
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unpurified recombinant enzyme, at pH 2.5 and 40°C
0.397
activity with decyl ubiquinone at pH 6, 92°C
3.16
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recombinant enzyme after 63.2fold purification, at pH 2.5 and 40°C
397
with 6-decylubiquinone as electron acceptor
49.9
with ferricyanide as electron acceptor
73.4
activity with ferricyanide at pH 6, 92°C
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2.5
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native and recombinant enzyme
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2 - 3
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the native enzyme shows about 35% activity at pH 2.0 and 20% activity at pH 3.0, the recombinant enzyme shows about 80% activity at pH 2.0 and about 35% activity at pH 3.0
3.5 - 6.8
approx. 55% of maximal activity at pH 3.5, approx. 22% of maximal activity at pH 6.5
4.5 - 5.5
pH 4.5: about 70% of maximal activity, pH 5.5: about 35% of maximal activity
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20 - 92
increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons
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20 - 92
increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons
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UnIProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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18700
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
20400
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
25000
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x * 25000, SDS-PAGE
16000
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE
16000
alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
28000
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE
28000
alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
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tetramer
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE
tetramer
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
tetramer
alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
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glycoprotein
the larger subunit (28000 Da) appears to be glycosylated
phosphoprotein
glycosylation of subunit DoxA, i.e. beta subunit of TQO
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affinity matrix HR 5/5 column chromatography, matrices based on cytochrome c immobilized on crosslinked triazine (2,4,6-tris(aminoethylamine)-1,3,5-triazine), cytochrome c immobilized on Silasorb-amine with carbodiimide activation and cytochrome c immobilized on Sepharose CL-4B
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ammonium sulfate precipitation, CM-650M column chromatography, butyl-650M column chromatography, and TSKgel G3000 gel filtration
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solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose
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expressed in Escherichia coli BL21(DE3) cells
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Muller, F.H.; Bandeiras, T.M.; Urich, T.; Teixeira, M.; Gomes, C.M.; Kletzin, A.
Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase
Mol. Microbiol.
53
1147-1160
2004
Acidianus ambivalens (P97224 AND P97207), Acidianus ambivalens
brenda
Janiczek, O.; Pokorna, B.; Zemanova, J.; Mandl, M.
Use of immobilized cytochrome c as a ligand for affinity chromatography of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans
J. Biotechnol.
117
293-298
2005
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans CCM 4253
brenda
Kikumoto, M.; Nogami, S.; Kanao, T.; Takada, J.; Kamimura, K.
Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans
Appl. Environ. Microbiol.
79
113-120
2013
Acidithiobacillus ferrooxidans
brenda
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Transporter Classification Database (TCDB):
3.D.4.9.1
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