Ligand dipicolinic acid

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Basic Ligand Information

Molecular Structure
Picture of dipicolinic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C7H5NO4
dipicolinic acid
WJJMNDUMQPNECX-UHFFFAOYSA-N
Synonyms:
2,6-dicarboxypyridine, 2,6-dipicolinic acid, 2,6-pyridindicarboxylic acid, 2,6-pyridinedicarboxylate, 2,6-pyridine dicarboxylate, 2,6-pyridinedicarboxylic acid, 2,6-pyridine dicarboxylic acid, dipicolinate, dipicolinate dianion, pyridin-2,6-dicarboxylic acid, pyridine-2,6-dicarboxylate, pyridine-2,6-dicarboxylic acid, pyridine 2,6-dicarboxylate, pyridine 2,6-dicarboxylic acid, pyridine dicarboxylate

Show all pahtways known for Show all pathways known for dipicolinic acid

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
-
activator
-
1 mM 220% relative activity, 0.1 mM 186% relative activity
-
1 mM 150% activity, 0.1 mM 144% activity
-

Inhibitor in Enzyme-catalyzed Reactions (120 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
40 mM, 99% inhibition after 1 h, complete loss of enzyme-bound Zn2+
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
-
competitive with respect to Fe2+ and noncompetitive with respect to 2-oxoglutarate
-
1 mM, 24% inhibition
-
82% residual activity at 1 mM
-
a metal chelator, complete inhibition
-
IC50 is 0.0025 mM
-
97% inhibition at 5 mM, Mg2+, Zn2+, and Co2+ partly protect
-
0.02 mM, complete inhibition
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
-
1 mM, 33% inhibition
-
zinc can be removed by dialysis against the metal chelator dipicolinate with the complete loss of catalytic activity
-
competitive
metal-chelating inhibitor
-
complete inhibition by metal-chelating agents in 50 mM Tris-HCl buffer (pH 8.0) at 30°C
-

3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

Enzyme Kinetic Parameters

Ki Value (15 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0368
-
at pH 8.0 and 25°C
0.7
-
pH 7.2
0.003
-
-
0.0227
-
wild type enzyme, at pH 7.0 and 22°C

IC50 Value (11 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.0422
-
IC50: 0.0422 mM
0.0025
-
IC50 is 0.0025 mM
20
-
IC50: 20 mM, competitive inhibitor

References & Links

Links to other databases for dipicolinic acid

ChEBI
PubChem
ChEBI
PubChem