Information on EC 2.8.1.3 - thiosulfate-thiol sulfurtransferase

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

EC NUMBER
COMMENTARY hide
2.8.1.3
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RECOMMENDED NAME
GeneOntology No.
thiosulfate-thiol sulfurtransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
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thiosulfate disproportionation I (thiol-dependent)
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SYSTEMATIC NAME
IUBMB Comments
thiosulfate:thiol sulfurtransferase
The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. L-Cysteine can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
111070-24-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Red Star brand
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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
L-cysteine + glutathione
?
show the reaction diagram
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-
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?
thiosulfate + cyanide
?
show the reaction diagram
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-
-
-
?
thiosulfate + dithiothreitol
?
show the reaction diagram
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-
-
-
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
benzenethiosulfonate + glutathione
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 + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
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-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzene sulfinate
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competitive with both substrates
benzene thiosulfonate
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competitive with both substrates
oxidized glutathione
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product inhibition, competitive with glutathione
sulfate
Sulfide
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product inhibition, competitive versus both substrates
sulfite
additional information
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alkylation of cysteine residues with iodoacetate or iodoacetamide does not inactivate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
Benzenethiosulfonate
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pH 8.1, 37C
3
cyanide
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pH 8.5, 27C
0.89 - 4
glutathione
2.9 - 3.2
thiosulfate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
118
sulfate
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pH 8.5, 27C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
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isoelectric focusing using ampholytes pH 4-6 and pH 2-10
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
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SDS-PAGE, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 17000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extremely labile during all ion-exchange steps
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freezing and thawing during the later stages of purification destabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-35C, concentrated enzyme in solution of 50 mM Tris, pH 8.0, 0.5 mM NaS2O3, 50% glycerol, stable for at least 4 months
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-40C, 50 mM Tris-acetate, pH 8.0, 0.5 mM Na2S2O3, 50% glycerol, stable for at least 9 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme loses catalytic activity in 6 M guanidinium hydrochloride, renaturation after a short period of time by dialysis is rapid and complete. Renaturation after 10 weeks results in only partial restoration of enzyme activity. Full renaturation can be obtained by adding thioglycolate or 2-mercaptoethanol during denaturation. Renaturation rate is temperature dependent
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