Ligand quinolin-8-ol

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Basic Ligand Information

Molecular Structure
Picture of quinolin-8-ol (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C9H7NO
quinolin-8-ol
MCJGNVYPOGVAJF-UHFFFAOYSA-N
Synonyms:
8-hydroxyquinoline, 8-hydroxy quinoline, 8-oxyquinoline, 8-Quinolinol, Hydroxyquinoline, oxyquinoline

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
8-Hydroxyquinoline + NADH + O2 = ?
show the reaction diagram
-
UDP-glucose + 8-hydroxyquinoline = UDP + 8-hydroxyquinolin-beta-D-glucoside
show the reaction diagram
-
oxyquinoline + H2O = ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, slight activation
-
1 mM, relative activity 110%
-
slight activation at 0.01 mM
-
stimulates if it reaches an equimolar concentration with Fe2+
-
0.4 mM concentration 400% activation
-
1.5fold stimulation at 0.1 mM
-
5% stimulation at 1 mM
-
activates
-
1 mM, enhances 36%
-
18% activation aat 1 mM
-
1 mM, 5% activation
-
118% activity at 3 mM
-
metal chelator required
-
5 mM, enhances activity
-

Inhibitor in Enzyme-catalyzed Reactions (208 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
complete inhibition at 10 mM
-
50% decrease at 0.67 mM
-
1mM, 45% residual activity
-
57% inhibition at 1 mM
-
1 mM, 100% inhibition with NAD+ as cofactor, 40% with NADP+ as cofactor
-
nearly complete inhibition at 2.5 mM
-
2 mM, 18% residual activity
-
1 mM, 55% residual activity
-
1 mM, 6% inhibition
-
50% inhibition at 2 mM
-
1 mM, 56% residual activity
-
1 mM, 50% inhibition
-
7.9% inhibition at 1 mM
-
80% residual activity at 1 mM
-
complete inhibition at 7.5 mM
-
weak
-
reversible by addition of Cu2+
-
1 mM, 35% inhibition
-
0.01 mM, 59% inhibition
-
5 mM 30 min
-
Fe3+-specific chelator, strong inhibition
-
1 mM, 90% loss of activity
-
; strong inhibition
-
slight
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
-
; 88% inhibition at 1 mM
-
5 mM, complete inhibition
-
5% residual activity at 1 mM
-
0.5 mM, 60% inhibition
-
76% residual activity at 1 mM
-
34% inhibition in the presence of 1 mM
-
1 mM, 20% residual activity
-
1 mM, 54% inhibition
-
16.7 mM, 25% inhibition
-
enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 83% inhibition
-
1 mM, 10% inhibition
-
reversible by the addition of Zn2+, Ni2+, Co2+
-
slight
-
33% inhibition at 1 mM
-
1 mM, 94% inhibition
-
1 mM, slight inhibition
-
77% inhibition at 5 mM
-
0.3 mM, 80% inhibition
-
1 mM, 50% inhibition
-
10 mM, 15% inhibition
-
0.1 mM
-
50% inhibition at 0.2 mM
-
7% inhibition at 5 mM
-
0.1 mM, 85% inhibition
-
time-dependent inactivation
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions
-
47.2% residual activity at 1 mM
-
at 2 mM, 50% residual activity
-
inhibits cleavage of alkylated dsDNA
-
2 mM, 28% residual activity
-
1 mM, 93% inhibition
-
2.0 mM, 84% inhibition
-
100% inhibition at 1 mM
-
10 mM, 68% inhibition
-
Zn2+ reverses, bovine serum albumin as substrate
-
0.1 mM at pH 10, 5 mM at pH 7
-
complexed with zinc, reactivation by addition of ZnSO4, MnSO4, MgSO4, CoSO4, FeSO4
-
60% inhibition at 3.3 mM
-
slight inhibition at 1 mM
-
very slight inhibition, 1 mM: 2% inhibition
-
2 mM, 65% inhibition
-
50% inhibition at 2 mM
-
85% residual activity at 0.5 mM
-
2 mM, 60% inhibition
-
1 mM
-
5 mM, 9.4% residual activity
-
36% inhibition at 1 mM
-
weak
-
Mn2+ or Mg2+ restore activity
-
1 mM, 49% inhibition
-
strong
-
26.1% inhibition at 1 mM
-
inhibition is partly reversed by ferric citrate, ascorbic acid and dehydroascorbic acid
-
59% inhibition at 1 mM
-
above 5 mM
-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

KM Value (5 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE

Ki Value (6 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.034
-
-
0.65
-
-
0.00058
-
pH 8, 25°C
0.214
-
25°C, pH 7.5

IC50 Value (7 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.75
-
in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37°C

References & Links

Links to other databases for quinolin-8-ol

ChEBI
PubChem
ChEBI
PubChem