Ligand NO

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Basic Ligand Information

Molecular Structure
Picture of NO (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
HNO
NO
PXGPLTODNUVGFL-YNNPMVKQSA-N
Synonyms:
nitric oxide, nitrogen oxide, nitroxyl, NO radical


Show all pahtways known for Show all BRENDA pathways known for NO

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (41 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
nitric oxide + H2O2 = ?
show the reaction diagram
-
NO + NAD(P)H + H+ = N2O + NAD(P)+ + H2O
show the reaction diagram
-
NO + 5 ferrocytochrome c + 5 H+ = NH3 + H2O + 5 ferricytochrome c
show the reaction diagram
-
nitroxyl + 2 ferrocytochrome c + O2 + H+ = nitrite + 2 ferricytochrome c + H2O
show the reaction diagram
-
NO + menaquinol = N2O + H2O + menaquinone
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (73 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-nitrosoglutathione + NADH = GSH + NAD+ + NO
show the reaction diagram
-
-
nitrite + NADH = NO + NAD+ + H2O
show the reaction diagram
-
-
hydrazine + H2O + ferricytochrome c = nitric oxide + ammonium + ferrocytochrome c
show the reaction diagram
-
-
hydroxylamine + 2 ferricytochrome c = nitroxyl + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
3 nitrite + 2 H+ = 2 nitric oxide + nitrate + H2O
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (213 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
nitric oxide + H2O2 = ?
show the reaction diagram
-
nitroxyl + 2 ferrocytochrome c + O2 + H+ = nitrite + 2 ferricytochrome c + H2O
show the reaction diagram
-
nitric oxide + NADH = nitrate + NAD+
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (364 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-nitrosoglutathione + NADH = GSH + NAD+ + NO
show the reaction diagram
-
-
nitroglycerin + NAD+ + H2O = 1,2-glyceryl dinitrate + NO + NADH + H+
show the reaction diagram
-
-
nitrite + NADH = nitric oxide + NAD+ + H2O
show the reaction diagram
-
-
hydrazine + H2O + ferricytochrome c = nitric oxide + ammonium + ferrocytochrome c
show the reaction diagram
-
-
3 nitrite + 2 H+ = 2 nitric oxide + nitrate + H2O
show the reaction diagram
-
peroxynitrite = NO + O22-
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (65 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
S-nitrosylation by nitric oxide at Cys279 enhances the enzymatic activity by about 25%
-
nitric oxide stimulates nonenzymatic ADP-ribosylation of NUDT5 at cysteine residues using ADP-ribose and consequently activates its enzyme activity
-
NO generated during hypoxia leads to activation of caspase-9 and results in initiation of caspase-cascade-dependent hypoxic neuronal death
-
NO stimulates non-enzymatic ADP-ribosylation, at cysteine residues in the presence of reductant, of NUDT5 using ADP-ribose and consequently activates its ADPRase activity. ADPRase activity in J774 macrophage cells is increased by the treatment with SNP, an exogenous NO generator, or TNF-alpha/IFN-gamma, endogenous NO inducers. NO has a regulatory role, overview
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stimulation of expression
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activation at moderate concentration, inhibition at high concentrations. Hemoglobin prevents both, activation and inhibition
-
induces expression of heavy and light subunit via direct exposure or interleukin-1 induced
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Inhibitor in Enzyme-catalyzed Reactions (93 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Cys residues contained within the zinc/thiolate active center may be primary sites of NO interaction
-
inhibition e.g. by NOC-18, a NO donor
-
from NO donors S-nitroso-N-acetylpenicillamine or S-nitrosoglutathione in vivo and in vitro, leads to increased S-glutathiolation of the enzyme
-
generated from 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, competitive inhibitor, nitrosylated catalase is kinetically labile, NO tends to dissociate rapidly from the active site, binding structure, overview. Kinetic analysis of dissociation of NO from the enzyme-inhibitor complex
-
high concentrations, competition with O2, augmented by miconazole
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feedback inhibition
-
in Huh7 human hepatoma cells, treatment with nitric oxide donors causes rapid post-translational down-regulation of the enzyme
-
overproduced NO in liver causes the suppression of FMO3 activity directly via reversible S-nitrosylation. Overproduced NO may be responsible, at least in part, for the impairment of the detoxification or metabolism by FMOs of xenobiotics, which include a number of therapeutic drugs
-
in Huh7 human hepatoma cells, treatment with nitric oxide donors causes rapid post-translational down-regulation of the enzyme
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reversible inhibition
-
dose-dependent inhibition of xanthine dehydrogenase and oxidase activity, reaction with an essential sulfur in the molybdenum center, that damages the molybdopterin
-
irreversible inhibitor
-
wild-type cultures are more sensitive to the addition of a pulse of NO when grown under fermentative conditions compared with anaerobic respiratory conditions, sensitivity of different wild-type and mutant strains, overview
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strong competitive inhibitor
-
substrate inhibition at high concentratins
-
inhibits GRK2 by S-nitrosylation at Cys340, regulatory function of S-nitrosylation
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a reduction of CaMKII activity by S-nitrosylation at Cys6 is observed, but only after prolonged exposure of over 5 min to NO donors
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inactivation, reactivation by reduction using cysteine or thioredoxin
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inactivation, phosphate protects
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inhibits adenovirus replication by targeting the adenovirus proteinase, inhibition is reversible with dithiothreitol
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reversible inhibition under dioxygen-depleted conditions with 100fold reduction of activity in the presence of 0.05 mM nitric oxide. At 12 min, air is re-introduced, resulting in the restoration of full OxDC catalytic activity, albeit after a time lag of approximately 5 min
-
fusion protein with beta-galactosidase
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complete inhibition at 3 mM
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brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed
-
activation at moderate concentration, reversible inhibition at high concentrations. Hemoglobin prevents both, activation and inhibition
-
irreversible in a concentration-dependent manner
-
NO, unlike VP-16, preferentially induces the formation of TOP2beta cleavable complexes in cells, induces skin melanomas formation in 7,12-dimethyl-benz[a]anthracene-initiated mice
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mediates reversible S-nitrosylation and inactivation of argininosuccinate synthetase in vitro and in lipopolysaccharide-treated cells and mice. S-nitrosylation of Cys132 is noth necessary and sufficient for the inhibition of argininosuccinate synthase by NO donors
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reversible inhibition
-
reversible inhibition
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Metals and Ions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
complexed with the enzyme, structure determination, binding kinetics
-
NO binding to a non-heme enzyme containing manganese allows examination of the factors governing the formation and detection of the MIII-O2.- species in all forms of th enzyme. NO, and presumably O2, binding is sensitive to both the nature of the catecholic substrate present and the nature of the active-site amino acid residue at position 200, spectral analysis, overview
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the iron-sulfur cluster in the N-terminus of the enzyme, RtelN, residues 1-312, is sensitive to hydrogen peroxide and nitric oxide, indicating that reactive oxygen/nitrogen species may modulate the DNA helicase activity of Rtel1 via modification of its iron-sulfur cluster but not significantly affect the DNA binding activity of RtelN
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3D Structure of Enzyme-Ligand-Complex (PDB) (86 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (31 results)

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

KM Value (16 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.3
-
pH 7.0, 20°C, reduction
0.0005
-
nitric oxide reduction, pH 7.5

Ki Value (13 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.00058
-
at pH 4.0 and 25°C
0.0135
-
-
0.0025
-
at pH 7.0 and 37°C
0.47
-
-
0.04
-
apparent value, pH and temperature not specified in the publication
0.32
-
-
0.035
-
reversible inhibition after brief exposure

IC50 Value (1 result)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.0001
-
pH and temperature not specified in the publication

References & Links