Information on EC 1.8.2.2 - thiosulfate dehydrogenase

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

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EC NUMBER
COMMENTARY hide
1.8.2.2
-
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RECOMMENDED NAME
GeneOntology No.
thiosulfate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thiosulfate:ferricytochrome-c oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY hide
9076-88-4
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
bifunctional tetrathionate reductase/thiosulfate dehydrogenase
A8FLS7
UniProt
Manually annotated by BRENDA team
bifunctional tetrathionate reductase/thiosulfate dehydrogenase
A8FLS7
UniProt
Manually annotated by BRENDA team
halophilic bacterium
extremely halophilic, neutrophilic archaeon
-
-
Manually annotated by BRENDA team
heterotrophic bacterium
two bacteria designated A-50 and C-3, isolated from percolation units containing garden soil and elemental sulfur, the enzyme system in C-3 is constitutive, but in A-50 it is induced by thiosulfate or tetrathionate
-
-
Manually annotated by BRENDA team
16B, marine heterotroph
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
W5
-
-
Manually annotated by BRENDA team
X
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
enzyme activity is detected in strains grown on tetrathionate or sulfur, but no activity is detected in ferrous iron-grown cells
physiological function
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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 + 2 ferricyanide
tetrathionate + 2 ferrocyanide
show the reaction diagram
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
show the reaction diagram
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
show the reaction diagram
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
show the reaction diagram
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
show the reaction diagram
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
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
show the reaction diagram
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
-
-
Ferricytochrome
halophilic bacterium
-
-
heme c
additional information
no cofactor: heme
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
enzyme contains 2 mol of non-heme iron
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
17% inhibition at 5 mM
2,2'-bipyridyl
azide
Cupferron
heterotrophic bacterium
-
strongly inhibits thiosulfate oxidation by A-50 extracts
cyanide
deoxycholate
-
-
diethyldicarbonate
-
-
diethyldithiocarbamate
heterotrophic bacterium
-
slightly inhibits
dithionate
-
18% inhibition at 1 mM, 15% inhibition at 0.1 mM and 0.01 mM
HgCl2
N-ethylmaleimide
Na2SeO3
Na2SeO4
-
51% inhibition at 5 mM
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
50% inhibition at 1 mM, 40% inhibition at 0.5 mM and 10% inhibition at 0.1 mM
SO42-
-
33% inhibition at 1 mM, 15% inhibition at 0.1 mM, 7% inhibition at 0.01 mM
sulfate
200 mM, about 60% reduction in activity
sulfite
2 mM, 1.6fold stimulation. Inhibitory at higher concentrations, almost complete inhibition at 10 mM
Thiocyanate
-
slightly inhibits
additional information
-
reagents selective for arginine, cysteine and tryptophane have no effect on enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cl-
halophilic bacterium
-
-
sulfite
2 mM, 1.6fold stimulation. Inhibitory at higher concentrations, almost complete inhibition at 10 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 3.3
ferricyanide
0.13
high-potential non-heme iron protein
-
-
-
0.004 - 15
thiosulfate
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17000
ferricyanide
Allochromatium vinosum
-
-
604 - 250000
thiosulfate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
302
thiosulfate
Campylobacter jejuni
A8FLS7
pH 4.0, 42°C
475
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
Na2SeO3
-
it is possible that selenite blocks access to the thiosulfate dehydrogenase or has an inhibiting effect on the respiratory chain itself
0.3
SO32-
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sulfite resembles the sulfonate part of thiosulfate and might, therefore, block the active site of the enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.16
pH 2.5, 40°C, recombinant protein
6.5
native protein, pH 2.5, 50°C
9.13
-
partially purified enzyme
11.38
-
purified enzyme
316
-
partially purified enzyme
1149
-
purified enzyme
4925
-
purified enzyme
5800
30°C, pH 5.0
30000
30°C, pH 4.0
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.25
-
activity assay
5.2
heterotrophic bacterium
-
thiosulfate + ferricyanide
6.5
-
broad, with cytochrome c as electron acceptor
7
-
for the reduction of cytochrome 553.5
7.2 - 7.6
-
cytochrome c as electron acceptor
additional information
-
no definite pH-optimum
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.8
-
little change in activity between
6.8
no residual activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
activity assay
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 48
-
about 50% of activity maximum at 22°C and 48°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
determined by chromatofocussing
6.2
calculated, mature protein
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
halophilic bacterium
-
-
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme
24000
-
2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme
25000
x * 25000, SDS-PAGE, x * 25796, calculated, mature protein
25796
x * 25000, SDS-PAGE, x * 25796, calculated, mature protein
25798
25800, SDS-PAGE, x * 25798, calculated
25800
25800, SDS-PAGE, x * 25798, calculated
27900
-
1 * 27900, SDS-PAGE
30000
-
determined by gel filtration
33000
-
2 * 33000 + 2 * 27000, SDS-PAGE
90000
-
gel filtration
102000
115000
-
sucrose density gradient method
120000
-
gel filtration
138000
180000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
monomer
tetramer
-
4 * 45000, SDS-PAGE
trimer
-
3 * 45000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a signal peptide of 37 amino acids
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
-
unstable below
394126
4
-
unstable below
394125
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
20% decrease of activity in 2 h and 60% decrease of activity in 7 h
4
-
6 h, 10% loss of activity, 50% loss of activity after 5 days
25
-
30 min, 7% loss of activity
30
-
50% decrease of activity in 2 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lability of enzyme during purification and storage at -20°C
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 36% loss of activity after 9 days
-
-20°C, crude extract, 50% loss of activity after 2 months
heterotrophic bacterium
-
-20°C, little loss of activity after 2 months
-
-20°C, the ability of the enzyme to couple with cytochrome c decreases during storage
-
-20°C, the activity of cell-free extracts is stable for several days in the presence of 20% v/v glycerol, without glycerol most of the activity is lost after 2 days
-
-20°C, the activity of whole cells is stable for 3 months
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-25°C, 0.02 M phosphate, 40% loss of activity after 2 months
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20-30% loss of activity after freezing at -20°C and thawing
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4°C, 10% loss of activity after 6 h and 50% loss of activity after 5 days
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4°C, 50% loss of activity after 3 days, 75% loss of activity after 14 days
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4°C, cell-free extracts lose most of the activity after 2 days even in the presence of glycerol
-
4°C, purified enzyme, 10% loss of activity after 24 h, completely inactive after 7 days
-
4°C, stable, 2 days
-
diluted enzyme loses 10-15% of the activity each time it is frozen and thawed
-
frozen, 0.05 M phosphate buffer, pH 6.2, stable for at least 90 days
-
frozen, stable for at least 3 months
-
frozen, stable, indefinitely as measured by ferricyanide reduction
-
the activity in cell-free extracts is lost very rapidly after freezing and thawing
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography with immobilized cytochrome c
-
partial
partial, using ion exchange chromatography, gel filtration and hydrophobic interaction chromatography
-
partial, using ion-exchange chromatography and calcium phosphate gel treatment
-
partial, using ultracentrifugation, ammonium sulfate fractionation, column chromatography on DEAE-cellulose and gel filtration on Sephacryl S-200
-
partial, using ultracentrifugation, ultrafiltration, column chromatography on DEAE-Sephadex A-25 and gel filtration on Sephadex S-200
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using a Phenyl-Sepharose, a DEAE Sephacel and a Macroprep ceramic hydroxyapatite type I, and a Mono Q column
-
using ammonium sulfate precipitation, hydrophobic interaction chromatography, anion-exchange chromatography and gel filtration
-
using chromatography on Phenyl-Sepharose column and Mono Q column, gel filtration on Superdex 200 and column chromatography on Phenyl Superose
-
using chromatography on Phenyl-Sepharose column, CM-cellulose column and hydroxylapatite column
-
using heat-treatment, 5-17% ethanol precipitation and CM-cellulose treatment
-
using MnCl2 precipitation, treatment with calcium phosphate gel, and successive column chromatography on DEAE-Sephadex and Sephadex G-150
-
using sonication, column chromatography on DEAE-cellulose, pH-adjustment to 4.5 and calcium phosphate gel treatment
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.2.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)