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
2.8.1.3
-
RECOMMENDED NAME
GeneOntology No.
thiosulfate-thiol sulfurtransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
mechanism varies with the acceptor substrate employed
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thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
mechanism, substrates add in a random fashion
-
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
mechanism
-
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glutathione metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glutathione-dependent thiosulfate reductase
-
-
-
-
sulfane reductase
-
-
-
-
sulfane sulfurtransferase
-
-
-
-
sulfurtransferase, sulfane
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
111070-24-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
thiosulfate + cyanide
?
show the reaction diagram
-
-
-
-
?
thiosulfate + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
-
-
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
?
benzenethiosulfonate + glutathione
additional information
-
-
rapid equilibrium-ordered mechanism with glutathione as leading substrate
glutathione persulfide as an immediate product
?
L-cysteine + glutathione
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme has two distinct closely situated substrate binding sites, one for compounds with an RSO3-structure and one for the sulfhydryl substrate
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
benzene sulfinate
-
competitive with both substrates
oxidized glutathione
-
product inhibition, competitive with glutathione
sulfate
-
non-competitive inhibition when glutathione is the varied substrate
Sulfide
-
product inhibition, competitive versus both substrates
-
sulfite
-
competitive with respect to dithiothreitol, non-competitive with respect to thiosulfate
sulfite
-
product inhibition, competitive versus both substrates
sulfite
-
competitive inhibition when glutathione is the varied substrate
benzene thiosulfonate
-
competitive with both substrates
additional information
-
alkylation of cysteine residues with iodoacetate or iodoacetamide does not inactivate
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.24
-
Benzenethiosulfonate
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pH 8.1, 37C
3
-
cyanide
-
pH 8.5, 27C
0.89
-
glutathione
-
pH 8.1, 37C, with benzenethiosulfonate as the other substrate
4
-
glutathione
-
pH 8.1, 37C, with thiosulfate as the other substrate
2.9
-
thiosulfate
-
pH 8.1, 37C
3.2
-
thiosulfate
-
pH 8.5, 27C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
118
-
sulfate
-
pH 8.5, 27C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.1
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-
isoelectric focusing using ampholytes pH 4-6 and pH 2-10
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17000
-
-
SDS-PAGE, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
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1 * 17000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extremely labile during all ion-exchange steps
-
freezing and thawing during the later stages of purification destabilize
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
-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 ACCESSION NO.
LITERATURE
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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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