Information on EC 1.8.5.2 - thiosulfate dehydrogenase (quinone)

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

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EC NUMBER
COMMENTARY hide
1.8.5.2
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RECOMMENDED NAME
GeneOntology No.
thiosulfate dehydrogenase (quinone)
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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
thiosulfate oxidation II (via tetrathionate)
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non-pathway related
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Sulfur metabolism
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Microbial metabolism in diverse environments
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
9076-88-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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
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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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?
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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
; 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
sulfite
Triton X-100
; 1%, complete inhibition
Zn2+
; 1 mM, 37% inhibition, 5 mM, 82% inhibition
additional information
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00587 - 0.0059
6-decylubiquinone
3.4
ferricyanide
; 80°C, pH 6.0
2.6 - 15
thiosulfate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167
thiosulfate
; 80°C, pH 6.0
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
sulfite
; pH 6.0, 80°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
49.9
with ferricyanide as electron acceptor
73.4
activity with ferricyanide at pH 6, 92°C
397
with 6-decylubiquinone as electron acceptor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
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native and recombinant enzyme
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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
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 92
increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons
50
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recombinant enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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
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
28000
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
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 25000, SDS-PAGE
tetramer
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.5.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)