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Information on EC 1.1.5.4 - malate dehydrogenase (quinone)
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1.1.5.4 malate dehydrogenase (quinone)IUBMB Comments
A flavoprotein (FAD). Vitamin K and several other quinones can act as acceptors. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.1.299 (malate dehydrogenase [NAD(P)+]).
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Word Map
- 1.1.5.4
- oxaloacetate
- glutamicum
-
phospholipid-requiring
-
pyrroloquinoline
-
lipid-depleted
-
1.1.1.37
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
malate:quinone oxidoreductase, malate oxidase, malate quinone oxidoreductase, pfmqo, malate-quinone oxidoreductase, malate-vitamin k reductase, menaquinone reductase, fad-dependent malate dehydrogenase, l-malate:quinone oxidoreductase, malate dehydrogenase (acceptor), 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.3.3
-
-
formerly
-
EC 1.1.99.16
-
-
formerly
-
FAD-dependent malate dehydrogenase
L-malate-quinone oxidoreductase
malate-quinone oxidoreductase
malate: quinone oxidoreductase
malate:quinine oxidoreductase
malate:quinone oxidoreductase
menaquinone reductase
Mqo
MqoB
malate:quinone oxidoreductase
-
encoded by the gene mqo (previously called yojH)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-malate + a quinone = oxaloacetate + reduced quinone
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate:quinone oxidoreductase
A flavoprotein (FAD). Vitamin K and several other quinones can act as acceptors. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.1.299 (malate dehydrogenase [NAD(P)+]).
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CAS REGISTRY NUMBER
COMMENTARY
71822-24-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
(S)-malate + acceptor
oxaloacetate + reduced acceptor
the enzyme takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. A mutant completely lacking Mqo activity grows poorly on several substrates tested. This enzyme might be especially important when a net flux from malate to oxaloacetate is required, but the intracellular concentrations of the reactants are unfavourable for the NAD-dependent reaction (EC 1.1.1.37)
-
-
?
(S)-malate + menaquinone-1
oxaloacetate + menaquinol-1
-
menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
(S)-malate + ubiquinone-1
oxaloacetate + reduced ubiquinone-1
ubiquinone-1 is directly reduced by the enzyme
-
-
?
lactose + 2,6-dichlorophenolindophenol
lactobionic acid + reduced 2,6-dichlorophenolindophenol
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
49.3% of the activity with lactose
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
49.3% of the activity with lactose
-
-
?
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
assay in presence of 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
?
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
assay in presence of 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
?
(S)-malate + decylubiquinone
oxaloacetate + decylubiquinol
-
-
-
?
(S)-malate + dimethyl naphthoquinone
oxaloacetate + dimethyl naphthoquinol
-
-
-
-
?
(S)-malate + dimethyl naphthoquinone
oxaloacetate + dimethyl naphthoquinol
-
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
the route of electrons in this assay is unclear, but it probably leads from the enzyme either directly or via quinones to 2,6-dichlorophenol indophenol. The malate-dependent 2,6-dichlorophenol indophenol reduction rate catalyzed by Helicobacter pylori membranes could be stimulated by 30 to 50% by the addition of 60 mM ubiquinone-1. This suggests that quinones play, at least in part, an intermediary role in the reduction of the dye
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
the enzyme is involved in three pathways (mitochondrial electron transport chain, the tricarboxylic acid cycle and the fumarate cycle)
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
with dichlorophenolindophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
Pseudomonas oleovorans CECT 5344
-
with dichlorophenolindophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
-
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
-
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
-
-
?
(S)-malate + vitamin K1
oxaloacetate + reduced vitamin K1
-
-
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
64.3% of the activity with lactose
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
64.3% of the activity with lactose
-
-
?
lactose + 2,6-dichlorophenolindophenol
lactobionic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
lactose + 2,6-dichlorophenolindophenol
lactobionic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
additional information
?
-
-
the enzyme shows specificity towards ubiquinone, duroquinone, and dimethyl naphthoquinone in addition to menaquinone. And the enzyme also shows malate dehydrogenase activity, EC 1.1.1.37, overview
-
-
?
additional information
?
-
-
the enzyme shows specificity towards ubiquinone, duroquinone, and dimethyl naphthoquinone in addition to menaquinone. And the enzyme also shows malate dehydrogenase activity, EC 1.1.1.37, overview
-
-
?
additional information
?
-
-
Corynebacterium glutamicum possesses two types of L-malate dehydrogenase, a membrane-associated malate:quinone oxidoreductase (MQO) and a cytoplasmic malate dehydrogenase (MDH, EC 1.1.1.37). MQO, MDH, and succinate dehydrogenase (SDH) activities are regulated coordinately in response to the carbon and energy source for growth. Compared to growth on glucose, these activities are increased during growth on lactate, pyruvate, or acetate, substrates which require high citric acid cycle activity to sustain growth. MQO is the most important malate dehydrogenase in the physiology of Corynebacterium glutamicum. A mutant with a site-directed deletion in the mqo gene does not grow on minimal medium. Growth can be partially restored in this mutant by addition of the vitamin nicotinamide. In contrast, a double mutant lacking MQO and MDH does not grow even in the presence of nicotinamide. MDH is able to take over the function of MQO in an mqo mutant, but this requires the presence of nicotinamide in the growth medium. It is shown that addition of nicotinamide leads to a higher intracellular pyridine nucleotide concentration, which probably enables MDH to catalyze malate oxidation. Purified MDH catalyzes oxaloacetate reduction much more readily than malate oxidation at physiological pH. In a reconstituted system with isolated membranes and purified MDH, MQO and MDH catalyze the cyclic conversion of malate and oxaloacetate, leading to a net oxidation of NADH. Evidence is presented that this cyclic reaction also takes place in vivo
-
-
?
additional information
?
-
-
the loss of malate:quinone oxidoreductase activity down-regulates the flux of the tricarboxylic acid cycle to maintain the redox balance and results in redirection of oxaloacetate into L-lysine biosynthesis
-
-
?
additional information
?
-
-
NAD-dependent malate dehydrogenase (MDH, EC 1.1.1.37) does not repress mqo expression. MQO and MDH are active at the same time in Escherichia coli. No significant role for MQO in malate oxidation in wild-type Escherichia coli. Comparing growth of the mdh single mutant to that of the double mutant containing mdh and mqo deletions indicates that MQO partly takes over the function of MDH in an mdh mutant
-
-
?
additional information
?
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
a mutant with an interrupted putative mqo gene, in which malate:quinone oxidoreductase, an enzyme involved in the citric acid cycle/glyoxylate cycle, is defective, shows a severe growth defect on ethanol and is unable to grow on acetate
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment
-
-
?
additional information
?
-
the enzyme only oxidized disaccharides with reducing-end glucosyl residues, such as lactose, but not monosaccharides
-
-
-
additional information
?
-
-
the enzyme only oxidized disaccharides with reducing-end glucosyl residues, such as lactose, but not monosaccharides
-
-
-
additional information
?
-
the enzyme only oxidized disaccharides with reducing-end glucosyl residues, such as lactose, but not monosaccharides
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + acceptor
oxaloacetate + reduced acceptor
the enzyme takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. A mutant completely lacking Mqo activity grows poorly on several substrates tested. This enzyme might be especially important when a net flux from malate to oxaloacetate is required, but the intracellular concentrations of the reactants are unfavourable for the NAD-dependent reaction (EC 1.1.1.37)
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
the enzyme is involved in three pathways (mitochondrial electron transport chain, the tricarboxylic acid cycle and the fumarate cycle)
-
-
?
additional information
?
-
-
Corynebacterium glutamicum possesses two types of L-malate dehydrogenase, a membrane-associated malate:quinone oxidoreductase (MQO) and a cytoplasmic malate dehydrogenase (MDH, EC 1.1.1.37). MQO, MDH, and succinate dehydrogenase (SDH) activities are regulated coordinately in response to the carbon and energy source for growth. Compared to growth on glucose, these activities are increased during growth on lactate, pyruvate, or acetate, substrates which require high citric acid cycle activity to sustain growth. MQO is the most important malate dehydrogenase in the physiology of Corynebacterium glutamicum. A mutant with a site-directed deletion in the mqo gene does not grow on minimal medium. Growth can be partially restored in this mutant by addition of the vitamin nicotinamide. In contrast, a double mutant lacking MQO and MDH does not grow even in the presence of nicotinamide. MDH is able to take over the function of MQO in an mqo mutant, but this requires the presence of nicotinamide in the growth medium. It is shown that addition of nicotinamide leads to a higher intracellular pyridine nucleotide concentration, which probably enables MDH to catalyze malate oxidation. Purified MDH catalyzes oxaloacetate reduction much more readily than malate oxidation at physiological pH. In a reconstituted system with isolated membranes and purified MDH, MQO and MDH catalyze the cyclic conversion of malate and oxaloacetate, leading to a net oxidation of NADH. Evidence is presented that this cyclic reaction also takes place in vivo
-
-
?
additional information
?
-
-
the loss of malate:quinone oxidoreductase activity down-regulates the flux of the tricarboxylic acid cycle to maintain the redox balance and results in redirection of oxaloacetate into L-lysine biosynthesis
-
-
?
additional information
?
-
-
NAD-dependent malate dehydrogenase (MDH, EC 1.1.1.37) does not repress mqo expression. MQO and MDH are active at the same time in Escherichia coli. No significant role for MQO in malate oxidation in wild-type Escherichia coli. Comparing growth of the mdh single mutant to that of the double mutant containing mdh and mqo deletions indicates that MQO partly takes over the function of MDH in an mdh mutant
-
-
?
additional information
?
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
a mutant with an interrupted putative mqo gene, in which malate:quinone oxidoreductase, an enzyme involved in the citric acid cycle/glyoxylate cycle, is defective, shows a severe growth defect on ethanol and is unable to grow on acetate
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
menadione
-
triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
ubiquinone-0
-
triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone
ubiquinone-1
the route of electrons in this assay is unclear, but it probably leads from the enzyme either directly or via quinones to 2,6-dichlorophenol indophenol. The malate-dependent 2,6-dichlorophenol indophenol reduction rate catalyzed by Helicobacter pylori membranes could be stimulated by 30 to 50% by the addition of 60 mM ubiquinone-1. This suggests that quinones play, at least in part, an intermediary role in the reduction of the dye
ubiquinone-9
-
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM
FAD
-
in absence of FAD no reduction of 2,6-dichlorophenol indophenol is observed
FAD
is probably a tightly but non-covalently bound prosthetic group
FAD
-
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. Km-value for FAD is 0.0004 mM
vitamin K1
-
with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
additional information
-
no spectral evidence for the presence of a flavin or quinone in the purified enzyme
-
additional information
-
the enzyme is active with 2,6-dichlorophenolindophenol
-
additional information
-
the enzymeis active with duroquinone and dimethyl naphthoquinone
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-malate
-
in the presence of polymyxin B, enzyme kinetics changes from the Michaelis-Menten type to substrate inhibition kinetics with the substrate inhibition constant Ksi of 57.4 microg/ml
1,1'-[furan-2,5-diylbis(3-chloro-1,4-phenylene)]bisguanidine
inhibits growth of cultured parasite
-
2-cycloheptyl-5-[4-methoxy-3-[4-[4-(2H-tetrazol-5-yl)phenoxy]butoxy]phenyl]-4,4-dimethylpyrazol-3-one
inhibits growth of cultured parasite
-
2-[3-chloro-4-[5-[2-chloro-4-(diaminomethylideneamino)phenyl]furan-2-yl]phenyl]guanidine
inhibits growth of cultured parasite
-
3-cycloheptyl-4abeta,5,8,8abeta-tetrahydro-1-[3-[4-[4-(2H-tetrazole-5-yl)phenoxy]butoxy]-4-methoxyphenyl]phthalazine-4(3H)-one
inhibits growth of cultured parasite
-
3-[7-[(3,5-dimethylbenzyl)oxy]-4,8-dimethyl-2-oxo-2H-chromen-3-yl]propanoic acid
-
-
5-bromo-2-chloro-N-(5-mercapto-1,3,4-thiadiazol-2-yl)benzamide
-
-
ferulenol
inhibits parasite growth and shows strong synergism in combination with atovaquone, an anti-malarial and bc1 complex inhibitor
-
Polymyxin B
-
cationic decapeptide. Primary site of action is the quinone-binding site, amino acid sequence is examined and possible binding sites for L-malate and quinones are found
Sodium amytal
-
1 mM, competitive with respect to phosphatidylethanolamine, noncompetitive with respect to FAD
additional information
-
o-phenanthroline does not significantly affect activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methyl-1,4-naphthoquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
decylubiquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
duroquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
ubiquinone-0
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
ubiquinone-1
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
vitamin K3
-
in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid
-
in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid
-
activity of purified enzyme is dependent on added phospholipid
Phospholipid
-
the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Mqo, a tricarboxylic acid cycle enzyme, is required for virulence of Pseudomonas syringae pv. tomato strain DC3000 on Arabidopsis thaliana.
Malaria
Oxidative phosphorylation and rotenone-insensitive malate- and NADH-quinone oxidoreductases in Plasmodium yoelii yoelii mitochondria in situ.
Malaria
Suppression of experimental cerebral malaria by disruption of malate:quinone oxidoreductase.
Malaria, Cerebral
Suppression of experimental cerebral malaria by disruption of malate:quinone oxidoreductase.
Tuberculosis
Variations in the pathways of malate oxidation and phosphorylation in different species of Mycobacteria.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
in the presence of polymyxin B, enzyme kinetics changes from the Michaelis-Menten type to substrate inhibition kinetics with the substrate inhibition constant Ksi of 57.4 microg/ml. Polymyxin B inhibits the malate-dependent reaction noncompetitively with the Ki value of 7.0 microg/ml
-