Ligand S-sulfanylglutathione
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Basic Ligand Information
Molecular Structure

C10H17N3O6S2
S-sulfanylglutathione
QBOLVLBSUGJHGB-WDSKDSINSA-N
glutathione persulfide, GSS-
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)
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S-sulfanylglutathione + O2 = sulfite + glutathione + H+
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
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Substrate in Enzyme-catalyzed Reactions (2 results)
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S-sulfanylglutathione + O2 = glutathione + sulfite
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S-sulfanylglutathione + O2 = sulfite + glutathione + H+
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Product in Enzyme-catalyzed Reactions (8 results)
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glutathione + sulfite + 2 H+ = S-sulfanylglutathione + O2 + H2O
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sulfide + reduced glutathione + coenzyme Q1 = glutathione persulfide + reduced coenzyme Q1
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hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
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hydrogen sulfide + glutathione + coenzyme Q = S-sulfanylglutathione + reduced coenzyme Q
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hydrogen sulfide + glutathione + coenzyme Q1 = S-sulfanylglutathione + reduced coenzyme Q1
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hydrogen sulfide + glutathione + coenzyme Q10 = S-sulfanylglutathione + reduced coenzyme Q10
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hydrogen sulfide + glutathione + coenzyme Q1 = glutathione persulfide + H+ + reduced coenzyme Q1
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S-sulfoglutathione + 6 reduced ferredoxin + 6 H+ = glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (3 results)
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recombinant mutant C314S, pH 7.4, 22°C
5
-
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
6.5
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recombinant wild-type enzyme, pH 7.4, 22°C
143
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KM Value (3 results)
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recombinant mutant C314S, pH 7.4, 22°C
0.037
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recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
0.0078
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recombinant wild-type enzyme, pH 7.4, 22°C
0.07
-
References & Links
Literature References (2)
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Staphylococcus aureus CstB is a novel multidomain persulfide dioxygenase-sulfurtransferase involved in hydrogen sulfide detoxification
2015
Shen, J.; Keithly, M.E.; Armstrong, R.N.; Higgins, K.A.; Edmonds, K.A.; Giedroc, D.P.
Biochemistry
54
4542-4554
Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation
2017
Motl, N.; Skiba, M.A.; Kabil, O.; Smith, J.L.; Banerjee, R.
J. Biol. Chem.
292
14026-14038
Links to other databases for S-sulfanylglutathione