Information on EC 1.8.2.2 - thiosulfate dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.8.2.2
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RECOMMENDED NAME
GeneOntology No.
thiosulfate dehydrogenase
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
-
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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
-
-
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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
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-
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
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Manually annotated by BRENDA team
16B, marine heterotroph
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
W5
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Manually annotated by BRENDA team
X
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Manually annotated by BRENDA team
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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
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Ferricytochrome
halophilic bacterium
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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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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17% inhibition at 5 mM
2,2'-bipyridyl
azide
Cupferron
heterotrophic bacterium
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strongly inhibits thiosulfate oxidation by A-50 extracts
cyanide
deoxycholate
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-
diethyldicarbonate
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diethyldithiocarbamate
heterotrophic bacterium
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slightly inhibits
dithionate
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18% inhibition at 1 mM, 15% inhibition at 0.1 mM and 0.01 mM
HgCl2
N-ethylmaleimide
Na2SeO3
Na2SeO4
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51% inhibition at 5 mM
p-chloromercuribenzoate
p-hydroxymercuribenzoate
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50% inhibition at 1 mM, 40% inhibition at 0.5 mM and 10% inhibition at 0.1 mM
SO42-
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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
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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
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sulfite
2 mM, 1.6fold stimulation. Inhibitory at higher concentrations, almost complete inhibition at 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 3.3
ferricyanide
0.13
high-potential non-heme iron protein
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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
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604 - 250000
thiosulfate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
302
thiosulfate
Campylobacter jejuni
A8FLS7
pH 4.0, 42°C
475
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
Na2SeO3
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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
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
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partially purified enzyme
11.38
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purified enzyme
316
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partially purified enzyme
1149
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purified enzyme
4925
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purified enzyme
5800
30°C, pH 5.0
30000
30°C, pH 4.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.25
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activity assay
5.2
heterotrophic bacterium
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thiosulfate + ferricyanide
6.5
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broad, with cytochrome c as electron acceptor
7
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for the reduction of cytochrome 553.5
7.2 - 7.6
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cytochrome c as electron acceptor
additional information
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no definite pH-optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.8
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little change in activity between
6.8
no residual activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 48
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about 50% of activity maximum at 22°C and 48°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
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determined by chromatofocussing
6.2
calculated, mature protein
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
halophilic bacterium
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Manually annotated by BRENDA team
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
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2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme
24000
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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
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1 * 27900, SDS-PAGE
30000
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determined by gel filtration
33000
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2 * 33000 + 2 * 27000, SDS-PAGE
90000
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gel filtration
102000
115000
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sucrose density gradient method
120000
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gel filtration
138000
180000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
monomer
tetramer
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4 * 45000, SDS-PAGE
trimer
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3 * 45000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a signal peptide of 37 amino acids
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
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unstable below
394126
4
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unstable below
394125
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
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20% decrease of activity in 2 h and 60% decrease of activity in 7 h
4
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6 h, 10% loss of activity, 50% loss of activity after 5 days
25
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30 min, 7% loss of activity
30
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50% decrease of activity in 2 h
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
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-20°C, crude extract, 50% loss of activity after 2 months
heterotrophic bacterium
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-20°C, little loss of activity after 2 months
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-20°C, the ability of the enzyme to couple with cytochrome c decreases during storage
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-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
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-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
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4°C, purified enzyme, 10% loss of activity after 24 h, completely inactive after 7 days
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4°C, stable, 2 days
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diluted enzyme loses 10-15% of the activity each time it is frozen and thawed
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frozen, 0.05 M phosphate buffer, pH 6.2, stable for at least 90 days
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frozen, stable for at least 3 months
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frozen, stable, indefinitely as measured by ferricyanide reduction
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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
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partial
partial, using ion exchange chromatography, gel filtration and hydrophobic interaction chromatography
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partial, using ion-exchange chromatography and calcium phosphate gel treatment
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partial, using ultracentrifugation, ammonium sulfate fractionation, column chromatography on DEAE-cellulose and gel filtration on Sephacryl S-200
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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
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using ammonium sulfate precipitation, hydrophobic interaction chromatography, anion-exchange chromatography and gel filtration
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using chromatography on Phenyl-Sepharose column and Mono Q column, gel filtration on Superdex 200 and column chromatography on Phenyl Superose
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using chromatography on Phenyl-Sepharose column, CM-cellulose column and hydroxylapatite column
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using heat-treatment, 5-17% ethanol precipitation and CM-cellulose treatment
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using MnCl2 precipitation, treatment with calcium phosphate gel, and successive column chromatography on DEAE-Sephadex and Sephadex G-150
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE