Ligand oxalic acid

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Basic Ligand Information

Molecular Structure
Picture of oxalic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C2H2O4
oxalic acid
MUBZPKHOEPUJKR-UHFFFAOYSA-N
Synonyms:
ethanedioic acid, oxalate

Show all pahtways known for Show all pathways known for oxalic acid

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
oxalate + oxidized ferredoxin = CO2 + reduced ferredoxin
show the reaction diagram
-
succinyl-CoA + oxalate = succinate + oxalyl-CoA
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
glyoxylic acid + O2 + H2O = oxalate + H2O2
show the reaction diagram
-
-
acetate + oxalyl-CoA = acetyl-CoA + oxalate
show the reaction diagram
-
-
oxamate + H2O = oxalate + ammonia
show the reaction diagram
-
-
oxaloacetate + H2O = oxalate + acetate
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
oxalate + NADH = glyoxylate + NAD+
show the reaction diagram
-
oxalate + acetyl-CoA = oxalyl-CoA + acetate
show the reaction diagram
-
succinyl-CoA + oxalate = succinate + oxalyl-CoA
show the reaction diagram
-
oxalate + H+ = CO2
show the reaction diagram
-
ATP + oxalate + CoA = ADP + phosphate + oxalyl-CoA
show the reaction diagram
-
ATP + oxalate + CoA = ADP + phosphate + oxalyl-CoA
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
glyoxalate + O2 = oxalate + H2O2
show the reaction diagram
-
-
glyoxylate + O2 = oxalate + H2O2
show the reaction diagram
-
-
glyoxylate + acceptor = oxalate + reduced acceptor
show the reaction diagram
-
-
glyoxal + NAD+ + H2O = oxalate + NADH
show the reaction diagram
-
-
glyoxylic acid + NAD+ + H2O = oxalic acid + NADH
show the reaction diagram
-
-
glyoxylic acid + O2 + H2O = oxalate + H2O2
show the reaction diagram
-
-
glyoxylate + benzyl viologen = oxalic acid + reduced benzyl viologen
show the reaction diagram
-
-
acetate + oxalyl-CoA = acetyl-CoA + oxalate
show the reaction diagram
-
-
oxamate + H2O = oxalate + ammonia
show the reaction diagram
-
-
oxaloacetate + H2O = oxalate + acetate
show the reaction diagram
-
oxalacetate = oxalate + acetate
show the reaction diagram
-
-
oxaloacetate = acetate + oxalate
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates 42% at 2 mM with substrate 3,6-dimethoxyphenol, and 303% at 20 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
-
5 mM, 1.4fold activation
-
0.1 mM, 52% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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0.1 mM, 52% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
0.030 mM
-

Inhibitor in Enzyme-catalyzed Reactions (340 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
at pH 9.9
-
10% inhibition at 0.5 mM
-
1mM, 42.8% residual activity
-
inhibits only the cytosolic enzyme type with preference for hydroxypyruvate as substrate
-
16.7 mM, pH 7, 9% inhibition
-
inhibits L-malate oxidation reaction
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10 mM, 63.1% inhibition
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18% inhibition at 5 mM
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5 mM
-
forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
2 mM, 26% residual activity
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competitive
-
51% inhibition at 4 mM
-
34% inhibition at 1 mM
-
2 mM, 20% inhibition
-
60% inhibition at 5 mM, 96% inhibition at 10 mM
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substrate inhibition
-
moderate inhibitor
-
time-dependent inhibition
-
48% inhibition at 5 mM
-
at 6.67 mM 40% inhibition
-
competitive vs. 2-oxomalonate, uncompetitive vs. L-serine
-
competitive to ADP
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kinetics
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20 mM, 38% inhibition
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lysosomal enzyme
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competitive
-
competitive
47% inhibition of the tartaric acid-activated phlorizin hydrolase at 20 mM
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50 mM ammonium oxalate, 71% inhibition
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85% inhibition, restorage of 85% of activity by removal of oxalate by addition of Ca2+
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marked inhibition
-
9 mM
-
competitive inhibition, 2-6 mM
-
reversible by addition of Fe2+, Mn2+, or Co2+
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substrate inhibition
; weak binding competitive inhibitor
-
competitive inhibition
-
high concentrations cause a slight inhibition of ATP-diphosphate exchange

3D Structure of Enzyme-Ligand-Complex (PDB) (76 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (21 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.09
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
15
-
at pH 6.7 and 25°C

KM Value (109 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.058
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
22
-
at pH 6.7 and 25°C

Ki Value (66 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.12
-
pH 8.0, 30°C
0.006
-
pH 7.0, 25°C, recombinant wild-type enzyme
5.3
-
pH 7.0, 37°C
0.078
-
pH 7.5, 25°C
0.0000743
-
-
0.01
-
-
0.0000743
-
at 25°C
0.05
-
-
36
-
at pH 7.0
0.000018
-
-
1
-
pH 7.2
0.27
-
pH 8.0
0.09
-
pH not specified in the publication, temperature not specified in the publication
0.28
-
inhibits the phosphorylated enzyme
15
-
pH 8.1, 25°C
3
-
competitive, 30°C, pH 8.5
2
-
25°C, pH 7.5
1.6
-
in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.037
-
pH 7
1.6
-
; in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.00093
-
pH 8.0, 25°C

IC50 Value (8 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
1.8
-
-
0.12
-
-
0.12
-
at 25°C
0.41
-
0.2 mM, 71% of activity remaining, IC50: 0.41 mM

References & Links

Links to other databases for oxalic acid

ChEBI
PubChem
ChEBI
PubChem