Information on EC 1.8.5.2 - thiosulfate dehydrogenase (quinone)

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.8.5.2
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RECOMMENDED NAME
GeneOntology No.
thiosulfate dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 thiosulfate + 6-decylubiquinone = tetrathionate + 6-decylubiquinol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Sulfur metabolism
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thiosulfate oxidation II (via tetrathionate)
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non-pathway related
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-88-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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P97224 AND P97207
UnIProt
Manually annotated by BRENDA team
strain CCM 4253
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
show the reaction diagram
P97224 AND P97207
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
show the reaction diagram
P97224 AND P97207
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
show the reaction diagram
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
show the reaction diagram
thiosulfate + ferricyanide + H+
tetrathionate + ferrocyanide
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
show the reaction diagram
P97224 AND P97207
the physiological electron acceptor is most probably a caldariella quinone type quinone
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
show the reaction diagram
P97224 AND P97207
the enzyme couples sulfur compound oxidation with quinone reduction
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
P97224 AND P97207
; 1 mM, complete inhibition
Metabisulfite
P97224 AND P97207
; 1 mM, complete inhibition
N-ethylmaleimide
P97224 AND P97207
1 mM, 54% inhibition
reduced titanium citrate
P97224 AND P97207
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
sulfite
Triton X-100
P97224 AND P97207
; 1%, complete inhibition
Zn2+
P97224 AND P97207
; 1 mM, 37% inhibition, 5 mM, 82% inhibition
additional information
P97224 AND P97207
no inhibition by sulfate or tetrathionate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00587 - 0.0059
6-decylubiquinone
3.4
ferricyanide
P97224 AND P97207
; 80C, pH 6.0
2.6 - 15
thiosulfate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167
thiosulfate
Acidianus ambivalens
P97224 AND P97207
; 80C, pH 6.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
sulfite
P97224 AND P97207
; pH 6.0, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
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unpurified recombinant enzyme, at pH 2.5 and 40C
0.397
P97224 AND P97207
activity with decyl ubiquinone at pH 6, 92C
3.16
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recombinant enzyme after 63.2fold purification, at pH 2.5 and 40C
49.9
P97224 AND P97207
with ferricyanide as electron acceptor
73.4
P97224 AND P97207
activity with ferricyanide at pH 6, 92C
397
P97224 AND P97207
with 6-decylubiquinone as electron acceptor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
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native and recombinant enzyme
4.5 - 5
P97224 AND P97207
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5
P97224 AND P97207
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
P97224 AND P97207
approx. 55% of maximal activity at pH 3.5, approx. 22% of maximal activity at pH 6.5
4.5 - 5.5
P97224 AND P97207
pH 4.5: about 70% of maximal activity, pH 5.5: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 92
P97224 AND P97207
increasing activity is observed in the range between 20 and 92C, a maximum is not observed because of technical reasons
50
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recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 92
P97224 AND P97207
increasing activity is observed in the range between 20 and 92C, a maximum is not observed because of technical reasons
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
P97224 AND P97207
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
P97224 AND P97207
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; 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
18700
P97224 AND P97207
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
20400
P97224 AND P97207
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
25000
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x * 25000, SDS-PAGE
28000
P97224 AND P97207
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; 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
102000
P97224 AND P97207
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 25000, SDS-PAGE
tetramer
P97224 AND P97207
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence; 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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
P97224 AND P97207
the larger subunit (28000 Da) appears to be glycosylated
phosphoprotein
P97224 AND P97207
glycosylation of subunit DoxA, i.e. beta subunit of TQO
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose
P97224 AND P97207
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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