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EC Tree
IUBMB Comments The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide. L-Cysteine can also act as acceptor.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sulfane sulfurtransferase, sulfane reductase,
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glutathione-dependent thiosulfate reductase
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sulfane reductase
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sulfane sulfurtransferase
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sulfurtransferase, sulfane
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thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
mechanism
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thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
mechanism varies with the acceptor substrate employed
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thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
mechanism, substrates add in a random fashion
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thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
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sulfur atom transfer
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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.
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L-cysteine + glutathione
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?
thiosulfate + cyanide
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?
thiosulfate + cyanide
sulfite + thiocyanate
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?
thiosulfate + dithiothreitol
?
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?
thiosulfate + glutathione
? + glutathione disulfide
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?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
thiosulfate + thioredoxin
?
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?
benzenethiosulfonate + glutathione
additional information
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thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
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?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
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the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
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thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
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the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
?
thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
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the primary product is glutathione hydrodisulfide, which reacts with glutathione to give oxidized glutathione and sulfide
?
benzenethiosulfonate + glutathione
additional information
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rapid equilibrium-ordered mechanism with glutathione as leading substrate
glutathione persulfide as an immediate product
?
additional information
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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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thiosulfate + glutathione
sulfite + glutathione disulfide + sulfide
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?
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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
Sulfide
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product inhibition, competitive versus both substrates
additional information
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alkylation of cysteine residues with iodoacetate or iodoacetamide does not inactivate
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sulfate
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sulfate
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non-competitive inhibition when glutathione is the varied substrate
sulfite
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competitive with respect to dithiothreitol, non-competitive with respect to thiosulfate
sulfite
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product inhibition, competitive versus both substrates
sulfite
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competitive inhibition when glutathione is the varied substrate
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0.24
Benzenethiosulfonate
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pH 8.1, 37°C
0.89
glutathione
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pH 8.1, 37°C, with benzenethiosulfonate as the other substrate
4
glutathione
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pH 8.1, 37°C, with thiosulfate as the other substrate
11
glutathione
37°C, pH 7.4
2.9
thiosulfate
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pH 8.1, 37°C
3.2
thiosulfate
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pH 8.5, 27°C
17
thiosulfate
cosubstrate glutathione, 37°C, pH 7.4
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0.43
thiosulfate
37°C, pH 7.4
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0.039
glutathione
37°C, pH 7.4
0.025
thiosulfate
37°C, pH 7.4
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118
sulfate
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pH 8.5, 27°C
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additional information
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5.1
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isoelectric focusing using ampholytes pH 4-6 and pH 2-10
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cf. EC 2.8.1.1
UniProt
brenda
Red Star brand
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brenda
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brenda
lwolffi
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brenda
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apical localization in colonic crypts
brenda
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brenda
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TSTD1_HUMAN
115
0
12530
Swiss-Prot
other Location (Reliability: 2 )
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17000
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SDS-PAGE, gel filtration
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monomer
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1 * 17000, SDS-PAGE
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1.04 A resolution crystal structure displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase
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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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-35°C, 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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-40°C, 50 mM Tris-acetate, pH 8.0, 0.5 mM Na2S2O3, 50% glycerol, stable for at least 9 months
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expression in Escherichia coli
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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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Aird, B.A.; Heinrikson, R.L.; Westley, J.
Isolation and characterization of a prokaryotic sulfurtransferase
J. Biol. Chem.
262
17327-17335
1987
Acinetobacter calcoaceticus
brenda
Uhteg, L.; Westley, J.
Purification and steady-state kinetic analysis of yeast thiosulfate reductase
Arch. Biochem. Biophys.
195
211-222
1979
Saccharomyces cerevisiae
brenda
Chauncey, T.R.; Westley, J.
Improved purification and sulfhydryl analysis of thiosulfate reductase
Biochim. Biophys. Acta
744
304-311
1983
Saccharomyces cerevisiae
brenda
Chauncey, T.R.; Westley, J.
The catalytic mechanism of yeast thiosulfate reductase
J. Biol. Chem.
258
15037-15045
1983
Saccharomyces cerevisiae
brenda
Aird, B.A.; Horowitz, P.M.
A physical characterization of sulfane sulfurtransferase
Biochim. Biophys. Acta
1038
10-17
1990
Acinetobacter calcoaceticus
brenda
Libiad, M.; Motl, N.; Akey, D.L.; Sakamoto, N.; Fearon, E.R.; Smith, J.L.; Banerjee, R.
Thiosulfate sulfurtransferase-like domain-containing 1 protein interacts with thioredoxin
J. Biol. Chem.
293
2675-2686
2018
Homo sapiens (Q8NFU3)
brenda
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2.8.1.3 thiosulfate-thiol sulfurtransferase
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