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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
-
corynebacterium
- glutamicum
-
phospholipid-requiring
-
lipid-depleted
-
pyrroloquinoline
-
1.1.1.37
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
FAD-dependent malate dehydrogenase, L-malate-quinone oxidoreductase, malate dehydrogenase, malate dehydrogenase (acceptor), malate-quinone oxidoreductase, malate-vitamin K reductase, malate: quinone oxidoreductase, malate:quinine oxidoreductase, malate:quinone oxidoreductase, malate:quinone reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
?
(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-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 + a quinone
oxaloacetate + a quinol
-
-
-
-
?
(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
-
with dichlorophenolindophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
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
-
-
-
-
?
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
?
-
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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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
O69282
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 + a quinone
oxaloacetate + a quinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
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
?
-
O24913
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
-
additional information
?
-
Q9HVF1
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
-
additional information
?
-
Q9HVF1
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
?
-
Q5ECC3
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
-
additional information
?
-
Q887Z4
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
is probably a tightly but non-covalently bound prosthetic group
FAD
-
in absence of FAD no reduction of 2,6-dichlorophenol indophenol is observed
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 enzymeis active with duroquinone and dimethyl naphthoquinone
-
additional information
-
the enzyme is active with 2,6-dichlorophenolindophenol
-
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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
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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KM VALUE [mM]
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
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Mycolicibacterium smegmatis
-
IC50 for polymyxin B is 4.2 microg/ml, IC50 for nanaomycin is 49 microg/ml
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pv. tomato strain DC3000. Tn5 transposon insertion mutants (the Tn5 insertion disrupts the malate:quinone oxidoreductase gene) with reduced virulence on Arabidopsis thaliana
UniProt
brenda
a mutant completely lacking Mqo activity grows poorly on several substrates tested
UniProt
brenda
the L-lysine-producing mutant, Corynebacterium glutamicum B-6 carries a nonsense mutation in the mqo gene
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
expression of the mqo gene and, consequently, MQO activity are regulated by carbon and energy source for growth. In batch cultures, MQO activity is highest during exponential growth and decreases sharply after onset of the stationary phase
brenda
additional information
-
effect of the carbon source in the growth of Pseudomonas pseudoalcaligenes CECT5344 with cyanide as a nitrogen source compared to ammonium, overview. Strain CECT5344 requires an additional carbon source for assimilating cyanide as a nitrogen source
brenda
additional information
-
effect of the carbon source in the growth of Pseudomonas pseudoalcaligenes CECT5344 with cyanide as a nitrogen source compared to ammonium, overview. Strain CECT5344 requires an additional carbon source for assimilating cyanide as a nitrogen source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
not in cytosol, all analysed enzymes of the tricarboxylic acid –cycle are localised in the mitochondrion
brenda
a peripheral membrane protein that can be released from the membrane by addition of chelators
brenda
-
bound to the cell-wall membrane; firmly bound to
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
the enzyme is involved in cyanide degradation in association with the cyanide-insensitive electron-transfer chain
physiological function
-
the enzyme is a component of the electron transfer chain in Pseudomonas pseudoalcaligenes CECT5344 cells, overview
physiological function
-
the enzyme is a component of the electron transfer chain in Pseudomonas pseudoalcaligenes CECT5344 cells, overview; the enzyme is involved in cyanide degradation in association with the cyanide-insensitive electron-transfer chain
-
additional information
-
because of the differences in the redox potentials of NAD+ and quinones, the MQO-catalyzed reaction progresses spontaneously compared to the MDH-catalyzed reaction, EC 1.1.1.37
additional information
-
oxaloacetate reacts chemically inside the cyanide-insensitive cells to produce a cyanohydrin (2-hydroxynitrile), which is further converted to ammonium. The nitrile is transiently accumulated in cyanide-containing media
additional information
-
because of the differences in the redox potentials of NAD+ and quinones, the MQO-catalyzed reaction progresses spontaneously compared to the MDH-catalyzed reaction, EC 1.1.1.37
-
additional information
-
oxaloacetate reacts chemically inside the cyanide-insensitive cells to produce a cyanohydrin (2-hydroxynitrile), which is further converted to ammonium. The nitrile is transiently accumulated in cyanide-containing media
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
-
1 * 51000, at high salt concentrations the enzyme exists as a monomeric form which is more active than the aggregated form, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
1 * 51000, at high salt concentrations the enzyme exists as a monomeric form which is more active than the aggregated form, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of mqoB mutants by Tn5-Tc transposon insertion, class I mutants show strongly reduced growth on citronellol and citronellic acid, class II mutants grow normally on citronellic acid but reduced on citronellol, class III mutants are auxotroph, overview
additional information
-
construction of mqoB mutants by Tn5-Tc transposon insertion, class I mutants show strongly reduced growth on citronellol and citronellic acid, class II mutants grow normally on citronellic acid but reduced on citronellol, class III mutants are auxotroph, overview
additional information
construction of mqoB mutants by Tn5-Tc transposon insertion, class I mutants show strongly reduced growth on citronellol and citronellic acid, class II mutants grow normally on citronellic acid but reduced on citronellol, class III mutants are auxotroph, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.3 M potassium phosphate buffer, pH 6.6, about 20% loss of activity after 2 weeks
-
when stored on ice, the half-life is approximately 120 h, important stabilizing conditions for storage on ice are the presence of EDTA and EGTA. the presence of glycerol, and pH 6. The presence of Mg2+ and Ca2+ has a destabilizing effect
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
as c-myc-tag and pSag-S9-GFP-Cat, transfection into Toxoplasma gondii by electroporation
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
expression of the HP0086 sequence from a plasmid induces high MQO activity in mqo deletion mutants of Escherichia coli or Corynebacterium glutamicum
gene mqoB, DNA and amino acid sequence determination, analysis, and comparison, expression of mutant enzymes in Escherichia coli strain JM109
gene mqoB, DNA and amino acid sequence determination, analysis, and comparison, expression of mutant enzymes in Escherichia coli strain JM109
gene mqoB, DNA and amino acid sequence determination, analysis, and comparison, expression of mutant enzymes in Escherichia coli strain JM109
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the disruption of the mqo gene results in increased L-lysine production. The mutation supports industrial levels of L-lysine production in Corynebacterium glutamicum
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Phizackerley, P.J.R.
Malate dehydrogenase (FAD-linked) from Pseudomonas ovalis Chester
Methods Enzymol.
13
135-140
1969
Pseudomonas putida, Pseudomonas putida Chester
-
brenda
Imai, K.; Brodie, A.F.
A phospholipid-requiring enzyme, malate-vitamin K reductase
J. Biol. Chem.
248
7487-7494
1973
Mycolicibacterium phlei
-
brenda
Molenaar, D.; Van Der Rest, M.E.; Petrovic, S.
Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum
Eur. J. Biochem.
254
395-403
1998
Corynebacterium glutamicum, Corynebacterium glutamicum (O69282)
brenda
Imai, T.
FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties
Biochim. Biophys. Acta
523
37-46
1978
Mycobacterium sp., Mycobacterium sp. Takeo
brenda
Kather, B.; Stingl, K.; van der Rest, M.E.; Altendorf, K.; Molenaar, D.
Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase
J. Bacteriol.
182
3204-3209
2000
Helicobacter pylori, Helicobacter pylori (O24913)
brenda
Molenaar, D.; van der Rest, M.E.; Drysch, A.; Yucel, R.
Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Corynebacterium glutamicum
J. Bacteriol.
182
6884-6891
2000
Corynebacterium glutamicum
brenda
Foerster-Fromme, K.; Jendrossek, D.
Malate:quinone oxidoreductase (MqoB) is required for growth on acetate and linear terpenes in Pseudomonas citronellolis
FEMS Microbiol. Lett.
246
25-31
2005
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HVF1), Pseudomonas citronellolis, Pseudomonas citronellolis (Q5ECC3)
brenda
Diaz-Perez, A.L.; Roman-Doval, C.; Diaz-Perez, C.; Cervantes, C.; Sosa-Aguirre, C.R.; Lopez-Meza, J.E.; Campos-Garcia, J.
Identification of the aceA gene encoding isocitrate lyase required for the growth of Pseudomonas aeruginosa on acetate, acyclic terpenes and leucine
FEMS Microbiol. Lett.
269
309-316
2007
Pseudomonas aeruginosa (Q9HVF1)
brenda
Fleige, T.; Pfaff, N.; Gross, U.; Bohne, W.
Localisation of gluconeogenesis and tricarboxylic acid (TCA)-cycle enzymes and first functional analysis of the TCA cycle in Toxoplasma gondii
Int. J. Parasitol.
38
1121-1132
2008
Toxoplasma gondii (Q1KSF3)
brenda
Phizackerley, P.J.; Francis, M.J.
Cofactor requirements of the L-malate dehydrogenase of Pseudomonas ovalis Chester
Biochem. J.
101
524-535
1966
Pseudomonas putida, Pseudomonas putida Chester
brenda
Mitsuhashi, S.; Hayashi, M.; Ohnishi, J.; Ikeda, M.
Disruption of malate:quinone oxidoreductase increases L-lysine production by Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
2803-2806
2006
Corynebacterium glutamicum
brenda
van der Rest, M.E.; Frank, C.; Molenaar, D.
Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli
J. Bacteriol.
182
6892-6899
2000
Escherichia coli
brenda
Mellgren, E.M.; Kloek, A.P.; Kunkel, B.N.
Mqo, a tricarboxylic acid cycle enzyme, is required for virulence of Pseudomonas syringae pv. tomato strain DC3000 on Arabidopsis thaliana
J. Bacteriol.
191
3132-3141
2009
Pseudomonas syringae (Q887Z4)
brenda
Mogi, T.; Murase, Y.; Mori, M.; Shiomi, K.; Omura, S.; Paranagama, M.P.; Kita, K.
Polymyxin B identified as an inhibitor of alternative NADH dehydrogenase and malate: quinone oxidoreductase from the Gram-positive bacterium Mycobacterium smegmatis
J. Biochem.
146
491-499
2009
Mycolicibacterium smegmatis
brenda
Igeno, M.; Becerra, G.; Guijo, M.; Merchan, F.; Blasco, R.
Metabolic adaptation of Pseudomonas pseudoalcaligenes CECT5344 to cyanide: role of malate-quinone oxidoreductases, aconitase and fumarase isoenzymes
Biochem. Soc. Trans.
39
1849-1853
2011
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
brenda
Kabashima, Y.; Sone, N.; Kusumoto, T.; Sakamoto, J.
Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3
J. Bioenerg. Biomembr.
45
131-136
2013
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PS3
brenda
Luque-Almagro, V.M.; Merchan, F.; Blasco, R.; Igeno, M.I.; Martinez-Luque, M.; Moreno-Vivian, C.; Castillo, F.; Roldan, M.D.
Cyanide degradation by Pseudomonas pseudoalcaligenes CECT5344 involves a malate:quinone oxidoreductase and an associated cyanide-insensitive electron transfer chain
Microbiology
157
739-746
2011
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
brenda
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