Ligand S-nitrosoglutathione

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Basic Ligand Information

Molecular Structure
Picture of S-nitrosoglutathione (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C10H16N4O7S
S-nitrosoglutathione
HYHSBSXUHZOYLX-WDSKDSINSA-N
Synonyms:
nitrosoglutathione, S-nitroso-glutathione, S-nitrosylglutathione
Pathway Source
Pathways

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (17 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-nitrosoglutathione + NADPH + H+ = ? + NADP+
show the reaction diagram
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S-nitrosoglutathione + NADH + H2O = ?
show the reaction diagram
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S-nitrosoglutathione + NADH = ?
show the reaction diagram
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S-nitrosoglutathione + NADPH + H+ = ? + NADP+
show the reaction diagram
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S-nitrosoglutathione + NADPH + H+ = ? + NADP+
show the reaction diagram
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S-nitroso-glutathione + glycyl-glycine = S-nitroso-cysteinylglycine + gamma-L-glutamyl-glycyl-glycine
show the reaction diagram
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S-nitrosylglutathione + H2O = nitrous acid + glutathione
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
ADH3-mediated alcohol oxidation is promoted in the presence of S-nitrosoglutathione
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stimulation of isoform PDE5 phosphorylation and activity, resulting in increased levels of cGMP in gastric smooth muscle cells. Concurrent activation of cells with acetylcholine augments stimulation and attenuates cGMP levels
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stimulates the enzyme activity via NO production, stimulation is inhibited by acetylcholine
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Inhibitor in Enzyme-catalyzed Reactions (39 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
about 80% residual activity at 2 mM
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70.5% inhibtion at 5 mM of the leaf enzyme, 37.3% of the root enzyme
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hyperoxia attenuates the inhibitory effect of NO on HIF-1alpha prolyl hydroxylation
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i.e. GSNO, the glycine decarboxylase complex, GDC activity is inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues, overview. The inhibition of GDC activity after GSNO treatment can be an indirect effect of ROS induced by inhibition of complex I
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100% inhibition at 3 mM or higher concentration
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0.5 and 2 mM, 58% and 65% inhibition, respectively
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induces 84% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
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hexokinase is particularly susceptible to protein structure modifications when exposed to even low concentrations of S-nitrosoglutathione. Biologically relevant [S-nitrosoglutathione]/[hexokinase] causes a significant decrease in Vmax with glucose (but not with fructose), along with oxidation of 5 Met and nitration of 4 Tyr. Preincubation of hexokinase with glucose abrogates the effect of S-nitrosoglutathione whereas fructose is ineffective
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dithiothreitol prevents enzyme inhibition and fully restores enzyme activity
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GSNO, the chloroplast FBPase isoform cFBP1 is efficiently S-nitrosylated in vitro. GSNO inhibits the FBPase activity in the mutant C173S/C178S but not in mutant C153S. 0.02 mM GSNO produces a 75% activity inhibition in the mutant C173S/C178S, compared with the nontreated protein, S-nitrosylation of FBPase mutants in the Cys of the redox regulatory domain
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S-nitrosoglutathione treatment decreases the catalytic activity parameters of PtpA by half
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inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
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0.1 mM, complete inhibition
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HDAC8 can be S-nitrosylated by S-nitrosoglutathione in vitro, and the activity of HDAC8 is significantly inhibited when incubated with S-nitrosoglutathione and S-nitrosocysteine in a time- and dosage-dependent manner. Sodium nitroprusside and dithiothreitol cannot reverse this inhibition
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50% inhibition at 0.050 mM
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inhibition likely via S-transnitrosation
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inactivation by nitrosylation
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irreversible inactivation both in presence and absence of substrate
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GSNO, inhibition of human serine racemase by S-nitrosylation at Cys133, Cys128,and Cys269. The time-course is markedly biphasic, with a fast phase associated with the reaction of Cys113. The inhibition results from a conformational change rather than the direct displacement of ATP. Effect of nitrosylation on the cross-talk between ATP binding site and active site, both ATP and glycine bind to their respective sites with the same affinity regardless of the nitrosylation state
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isozyme MtGS2a activity is inhibited by thiol residue nitrosylation
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3D Structure of Enzyme-Ligand-Complex (PDB) (12 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (15 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (23 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.398
-
pH 8.0, 37°C

Ki Value (2 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.67
-
wild-type, pH 7.4, temperature not specified in the publication
0.305
-
pH 6.2, 25°C

IC50 Value (1 result)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
1.2
-
pH 8.0, 37°C

References & Links

Links to other databases for S-nitrosoglutathione

ChEBI
PubChem
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PubChem