Ligand malate

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Basic Ligand Information

Molecular Structure
Picture of malate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C4H6O5
malate
BJEPYKJPYRNKOW-UHFFFAOYSA-N
Synonyms:
beta-hydroxysuccinate, DL-malate, DL-malic acid, malic acid

Roles as Enzyme Ligand

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

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

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
oxaloacetate + NADH + H+ = malate + NAD+
show the reaction diagram
-
-
(S)-lactate + oxaloacetate = malate + pyruvate
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
DL-malate + acceptor = 2-oxosuccinate + reduced acceptor
show the reaction diagram
-
NADH + malate = NAD+ + ?
show the reaction diagram
-
DL-malic acid + NADPH + ATP = ? + NADP+ + AMP + phosphate
show the reaction diagram
-
DL-malic acid + O2 = ?
show the reaction diagram
-
malate + NAD+ = pyruvate + CO2 + NADH
show the reaction diagram
-
selenate + malate = ?
show the reaction diagram
-
DL-malate = DL-lactate + CO2
show the reaction diagram
-
DL-malate = maleate
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
oxaloacetate + NADH + H+ = malate + NAD+
show the reaction diagram
-
-
oxaloacetate + NADPH = malate + NADP+
show the reaction diagram
-
oxaloacetate + NAD(P)H = malate + NAD(P)+
show the reaction diagram
-
oxaloacetate + NADH + H+ = malate + NAD+
show the reaction diagram
-
-
oxaloacetate + NADH = malate + NAD+
show the reaction diagram
-
D-2-hydroxyglutarate + oxaloacetate = 2-oxoglutarate + malate
show the reaction diagram
-
-
(S)-lactate + oxaloacetate = malate + pyruvate
show the reaction diagram
-
beta-hydroxysuccinic semialdehyde + NADP+ + H2O = beta-hydroxysuccinate + NADPH + H+
show the reaction diagram
-
2-hydroxysuccinamate + H2O = malate + NH3
show the reaction diagram
-
-
acetyl-CoA + glyoxylate + H2O = malate + CoA
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (17 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
plus NADP+ and in synergism with ascorbate plus NADH increase of aldosterone synthetase activity in zona glomerulosa, no stimulation of 11beta-/18-hydroxylation
-
malate is stimulatory for the mitochondrial pyruvate dehydrogenase complex, but not for barley chloroplast pyruvate dehydrogenase complex. The stimulation is saturated below 1 mM malate and is related to the partially activated complex, which activity increases in the presence of malate by about twofold. Malate also reverses the reduction of pyruvate dehydrogenase complex activity in the presence of glycine
-
up to 50% increase in activity
-
5 mM
-
activation
-
stimulates the mitochondrial-matrix enzyme activity
-
stimulates the mitochondrial-matrix enzyme activity
-
enhances activity
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
-
slight activation of decarboxylation
-
activates
-

Inhibitor in Enzyme-catalyzed Reactions (91 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
noncompetitive versus NADP+ and isocitrate
-
at high concentration
-
competitive inhibition with respect to 2-oxoglutarate
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
-
5 mM, complete inhibition of NADH-linked activity
-
52% inhibition at 50 mM
-
78.6% residual activity at 10 mM
-
noncompetitive inhibition versus propionyl-CoA and versus oxaloacetate
-
1.0 mM, 50% inhibition
-
5 mM, 25% inhibition
-
approximately 20% inhibition at 1 mM
-
feedback inhibition
-
0.1 M, weak
-
weak
-
weak
-
37% residual activity at 20 mM
-
competitive inhibition
-
weak
-
diminishes hdc gene expression
-
D- and L-isomer
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Enzyme Kinetic Parameters

kcat Value (Turnover Number) (8 results)

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

KM Value (13 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
8
-
pH 4.5, 25°C, activity of cell extract

Ki Value (30 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.2
1.3
calculated from the slopes or intercepts
52
-
in citrate buffer, at pH 4.0 and 22°C
21.4
-
pH 8.0, 25°C
1
-
-

IC50 Value (14 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.0007
-
-
3.3
-
versus MtFBPaseII, pH and temperature not specified in the publication

References & Links

Links to other databases for malate

ChEBI
PubChem
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PubChem