Ligand quinolinic acid

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of quinolinic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C7H5NO4
quinolinic acid
CBMYJHIOYJEBSB-VXZRPZIYSA-N
Synonyms:
2,3-dicarboxypyridine, 2,3-pyridinedicarboxylic acid, excitotoxin quinolinate, pyridine-2,3-carboxylate, pyridine-2,3-dicarboxylate, pyridine-2,3-dicarboxylic acid, pyridine 2,3-dicarboxylate, quinolinate


Show all pahtways known for Show all BRENDA pathways known for quinolinic acid

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (15 results)

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

In Vivo Product in Enzyme-catalyzed Reactions (11 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O
show the reaction diagram
-
kynurenine + H2O = quinolinate
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2,3-dicarboxypyridine + NADH + O2 = 5,6-dihydroxy-5,6-dihydropyridine-2,3-dicarboxylate + NAD+ + H2O
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM 205% relative activity, 0.1 mM 120% relative activity
-
1 mM 171% activity, 0.1 mM 115% activity
-
allosteric activator
-
30% increase of activity at 0.1 mM
-

Inhibitor in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
competitive inhibition
-
competitive with respect to 2-oxoglutarate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
-
competitive
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
-
0.1 mM, 41% inhibition
-
non-competitive inhibitor, Ki: 3.9 mM
-
strongly inhibits the enzyme activated by ferroactivator and Fe2+, no inhibition of Mn2+-activated enzyme
1 mM, 61% residual activity
-
1 mM, complete inhibition of decarboxylation
-

3D Structure of Enzyme-Ligand-Complex (PDB) (82 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (15 results)

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

KM Value (30 results)

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

Ki Value (7 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.8
-
for the pI 5.6 enzyme
0.21
-
-
0.7
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.086
-
substrate phthalazine, pH 7.0, 37°C
18.3
-
at pH 7.0
3
-
pH 7.2
3.9
-
-

IC50 Value (1 result)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.42
-
IC50: 0.42 mM

References & Links

Links to other databases for quinolinic acid

ChEBI
PubChem
-
PubChem