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BRENDA support

Ligand malonic acid

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Basic Ligand Information

Molecular Structure
Picture of malonic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C3H4O4
malonic acid
OFOBLEOULBTSOW-UHFFFAOYSA-N
Synonyms:
an alpha,omega-dicarboxylate, an alpha,omega-dicarboxylic acid, an alphaomega-dicarboxylic acid, dicarboxylate, malonate, propanedioic acid

Related pathways

Pathway Source
Pathways
MetaCyc
afrormosin conjugates interconversion, biochanin A conjugates interconversion, daidzein conjugates interconversion, ethene and chloroethene degradation, fatty acid biosynthesis initiation (mitochondria) more


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

Roles as Enzyme Ligand

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

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
malonate + acetyl-[acyl-carrier protein] = acetate + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA + malonate = acetate + malonyl-CoA
show the reaction diagram
-
malonate + H+ = acetate + CO2
show the reaction diagram
-
ATP + malonate + CoA = AMP + diphosphate + malonyl-CoA
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
3-oxopropanoate + NAD+ + H2O = malonate + NADH
show the reaction diagram
-
-
monoamidated dicarboxylate + H2O = dicarboxylate + ammonia
show the reaction diagram
-
ureidomalonic acid + H2O = malonate + urea
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
malonate + NADH = malonic semialdehyde + NAD+ + H2O
show the reaction diagram
-
acetyl-CoA + malonate = malonyl-CoA + acetate
show the reaction diagram
malonate + acetyl-[acyl-carrier protein] = acetate + malonyl-[acyl-carrier protein]
show the reaction diagram
-
malonate + H+ = acetate + CO2
show the reaction diagram
-
ATP + malonate + CoA = AMP + diphosphate + malonyl-CoA
show the reaction diagram
-
ATP + malonate + CoA = ADP + phosphate + malonyl-CoA
show the reaction diagram
-
malonate + H+ = acetate + CO2
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
malonic semialdehyde + NADP+ + H2O = malonate + NADPH + H+
show the reaction diagram
-
malonate semialdehyde + NAD+ + H2O = malonate + NADH + 2 H+
show the reaction diagram
-
-
malonate semialdehyde + NADP+ + H2O = malonate + NADPH + 2 H+
show the reaction diagram
-
-
malonyl-CoA + acetate = acetyl-CoA + malonate
show the reaction diagram
-
O-malonyl-L-homoserine + L-cysteine = L-cystathionine + malonate
show the reaction diagram
-
malonyl-CoA + malonate = malonyl-CoA + malonate
show the reaction diagram
-
-
malonyl-CoA = malonate + CoA
show the reaction diagram
-
-
malonyl-CoA + H2O = malonate + CoA
show the reaction diagram
-
malonyl-CoA + H2O = malonate + CoA
show the reaction diagram
-
-
malonyl-CoA + H2O = malonate + CoA
show the reaction diagram
-
-
ureidomalonic acid + H2O = malonate + urea
show the reaction diagram
-
-
barbiturate + 2 H2O = malonate + urea
show the reaction diagram
-
malononitrile + H2O = malonic acid + NH3
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (33 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
inhibits at pH 7.8, increases activity at pH 5.8
activates
-
0.030 mM
-

Inhibitor in Enzyme-catalyzed Reactions (210 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
at pH 9.9
-
competitive against L-serine, noncompetitive against NADP+
-
competitive inhibition
-
inhibition only in absence of AMP
-
reversible inhibition, IC50: 0.34 mM
-
50 mM, complete loss of activity
-
competitive inhibitor
-
about 25% inhibition at 1 mM
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
-
inhibition mechanism of malonate, overview
competitive inhibition
-
weak
-
above 20 mM
-
competitive inhibition
-
competitive, Ki: 20 mM
-
9 mM
-
about 68% residual activity at 25 mM
-
reversible inhibition
reversible inhibition
10 mM, 15% inhibition
-
-
-

3D Structure of Enzyme-Ligand-Complex (PDB) (2672 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (6 results)

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

KM Value (21 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.5
-
pH 6.0

Ki Value (34 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
3.8
-
-
5.9
-
-
7.4
-
competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate
0.57
-
-
3
-
in citrate buffer, at pH 4.0 and 22°C
24
-
at pH 7.0
0.4
-
pH 6.0
108
-
pH 8.0, 25°C, aspartokinase III
2.1
-
pH 8.5, 30°C
21
-
pH 8.1, 25°C
20
-
competitive

IC50 Value (5 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.34
-
reversible inhibition, IC50: 0.34 mM
5.3
-
pH 8.3, 37°C
1.31
-
pH and temperature not specified in the publication

References & Links

Links to other databases for malonic acid

EXTERNAL LINKS