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BRENDA support

Ligand glutathione disulfide

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Basic Ligand Information

Molecular Structure
Picture of glutathione disulfide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C20H32N6O12S2
glutathione disulfide
YPZRWBKMTBYPTK-BJDJZHNGSA-N
Synonyms:
(2S,2'S)-5,5'-[disulfanediylbis([(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl]imino)]bis(2-amino-5-oxopentanoic acid), G-S-S-G, glutathione-disulfide, glutathione disulfide[side 1], glutathione disulfide[side 2], GSSG, GSSG[side 1], GSSG[side 2], n(GSSG), oxidized glutathione
Pathway Source
Pathways
BRENDA
arachidonic acid metabolism, cysteine metabolism, glutathione metabolism, sulfate reduction
KEGG
Biosynthesis of cofactors, Chemical carcinogenesis - reactive oxygen species, Diabetic cardiomyopathy, Ferroptosis, Glutathione metabolism more
MetaCyc
alpha-linolenate metabolites biosynthesis, arachidonate metabolites biosynthesis, arsenic detoxification (mammals), ascorbate glutathione cycle, ascorbate recycling (cytosolic) more


Show all pahtways known for Show all BRENDA pathways known for glutathione disulfide

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
glutathione disulfide + NADH + H+ = 2 glutathione + NAD+
show the reaction diagram
-
AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione
show the reaction diagram
-
glutathione disulfide = glutathione
show the reaction diagram
-
ATP + H2O + glutathione disulfide[side 1] = ADP + phosphate + glutathione disulfide[side 2]
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (50 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2 GSH + NADP+ = GSSG + NADPH + H+
show the reaction diagram
-
glutathione + O2 = glutathione disulfide + H2O2
show the reaction diagram
-
GSH + homocystine = GSSG + homocysteine
show the reaction diagram
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CoA-glutathione + GSH = CoA + GSSG
show the reaction diagram
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cystine + GSH = cysteine + GSSG
show the reaction diagram
-
glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone
show the reaction diagram
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thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide
show the reaction diagram
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ATP + H2O + glutathione disulfide[side 1] = ADP + phosphate + glutathione disulfide[side 2]
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (40 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
GSSG + H2O2 = ?
show the reaction diagram
-
glutathione disulfide + 2 H2O = 2 glutathione + H2O2
show the reaction diagram
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ribonucleoside triphosphate + GSSG = 2'-deoxyribonucleoside triphosphate + GSH + H2O
show the reaction diagram
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glutathione disulfide + pyrimidodiazepine = 6-pyruvoyltetrahydropterin + glutathione
show the reaction diagram
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glutathione disulfide + NADH + H+ = 2 glutathione + NAD+
show the reaction diagram
-
coenzyme M disulfide + glutathione disulfide = 2 coenzyme M + glutathione
show the reaction diagram
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GSSG + reduced alkaline phosphatase = 2 GSH + oxidized alkaline phosphatase
show the reaction diagram
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CQQGFDGTQNSCK peptide containing amide-coupled tetraazacyclododecane-1,4,7,10-tetraacetic acid + GSSG = ?
show the reaction diagram
-
GSSG + GSH = GSSG + GSH
show the reaction diagram
-
[xanthine dehydrogenase] + oxidized glutathione = [xanthine oxidase] + glutathione
show the reaction diagram
-
AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione
show the reaction diagram
-
oxidized glutathione + H2O = ? + L-glutamate
show the reaction diagram
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oxidized glutathione + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (163 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
glutathione + H2O + NAD+ = GSSG + NADH + 2 H+
show the reaction diagram
-
2 glutathione + NAD+ = GSSG + NADH + H+
show the reaction diagram
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arsenate + glutathione = arsenite + glutathione disulfide + H2O
show the reaction diagram
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chanoclavine-I aldehyde + GSH + NADPH + H+ = agroclavine + GSSG + NADP+
show the reaction diagram
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L-cystine + glutathione = L-cysteine + GSSG
show the reaction diagram
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glutathione + NADP+ = glutathione disulfide + NADPH + H+
show the reaction diagram
-
2 GSH + NADP+ = GSSG + NADPH + H+
show the reaction diagram
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insulin disulfide + reduced glutathione = insulin dithiol + oxidized glutathione
show the reaction diagram
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5'-adenylyl sulfate + glutathione = AMP + sulfite + glutathione disulfide
show the reaction diagram
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L-methionine (R,S)-sulfoxide + glutathione = L-methionine + GSSG + H2O
show the reaction diagram
-
GSH + coenzyme Q1 = GSSG + reduced coenzyme Q1
show the reaction diagram
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adenylyl sulfate + GSH = AMP + sulfite + GSSG
show the reaction diagram
-
ATP + H2O + GSSG/out = ADP + phosphate + GSSG/in
show the reaction diagram
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ATP + H2O + glutathione disulfide[side 1] = ADP + phosphate + glutathione disulfide[side 2]
show the reaction diagram
-

Enzyme Cofactor/Cosubstrate (2 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (12 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
required for activity
-
leads to the formation of internal disulfide bonds between Cys66 and Cys232, activates the enzyme and allows it to function at a pH optimum in the physiological range
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activation
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oxidized glutathione enhances OpdB activity and affects the P1 preference of OpdB synergistically in a substrate-dependent manner
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enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, maximal activity by partial S-glutathionylation, overview
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activity is inhibited almost totally at 20 mM
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activates
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Inhibitor in Enzyme-catalyzed Reactions (84 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
reaction completely stopped at 3.333 mM
-
5 mM, 65% inhibition; 65% inhibition with 5 mM
-
90% loss of activity
-
75% of the dehydrogenase activity converted to oxidase activity at 0.5 mM
-
oxidized glutathione
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31% inhibition of anerobic, 25% inhibition of aerobic enzyme at 5 mM
-
strong, time dependent inhibition of thio-NADP+ reduction by NADH and acetylpyridine adenine dinucleotide reduction by NADPH, 50% inhibition after 40 min incubation in 26.7 mM glutathione disulfide, presence of NADPH accelerates inhibition 20fold
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substrate inhibition at moderate or high concentrations. Noncompetitive mode of inhibition in which the disulfide behaves as an affinity label-like reagent through its binding and reduction at an alternative site, leading the enzyme into an inactive state
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substrate inhibition above 0.8 mM
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1 mM, inhibition
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product inhibition
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reversible inhibition, forms mixed disulfides with the enzymes active site residue Cys239, inactivation kinetics, inhibition is reversible by glutaredoxin, not by DTT, glutaredoxin together with glutathione exhibits regulatory function in vivo
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inactivates by glutathionylation at Cys645
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0.5 mM, weak inhibition
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reversible inactivation, activity can be restored by treatment with dithiothreitol
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inactivation involves formation of a protein-protein disulfide rather than a protein-glutathione complex
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oxidized glutathione, weak
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0.1 mM, 17% inhibition
-
thiol reagents protect or reverse
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product inhibition, competitive with glutathione
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oxidized glutathione, inactivation and kinetics, adenosine 3'-phosphate 5'-phosphosulfate protects
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Es-D, not Es-B
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deactivates the enzyme activated by reduced thioredoxin f
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slight inhibition at 1 mM
-
concentrations above10 mM significantly decrease activity
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glutathionylation of caspase can occur at physiologically relevant concentrations of glutathione disulfide and results in the inhibition of caspase activation and activity
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complete inhibition at 5 mM
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25% inhibition at 1 mM
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ICL can be inactivated by glutathionylation and reactivated by glutaredoxin after reduced dithiothreitol treatment, whereas thioredoxin does not appear to regulate ICL activity
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about 16% residual activity at 1 mM
-
-
-
67% residual activity at 1 mM
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enzyme YtmJKLMN shows less than 10% inhibition at 0.05 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (63 results)

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Enzyme Kinetic Parameters

kcat Value (Turnover Number) (46 results)

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EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
146
-
pH 7.1, 25°C
5.1
-
-

KM Value (119 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
6.9
-
pH 7.1, 25°C
8.9
-
pH 6.8, 50°C
0.015
-
-
0.426
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in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.111
-
-

Ki Value (7 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
50
-
with 10 and 20 mM, inhibition of S-nitrosoglutathione reduction
2.5
-
pH and temperature not specified in the publication
0.331
-
pH 7.8, 25°C
10.7
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pH 7.8, 30°C, recombinant enzyme

IC50 Value (3 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
-999
-
0.5 mM, 19.9% inhibition
2.6
-
IC50: 2.0 mM for homodimeric enzyme, IC50: 2.6 mM for heterodimeric enzyme
0.547
-
recombinant enzyme

References & Links

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Links to other databases for glutathione disulfide

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ChEBI
PubChem
ChEBI
PubChem