Information on EC 1.1.5.4 - malate dehydrogenase (quinone)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.5.4
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RECOMMENDED NAME
GeneOntology No.
malate dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-malate + a quinone = oxaloacetate + reduced quinone
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Citrate cycle (TCA cycle)
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Metabolic pathways
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Microbial metabolism in diverse environments
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Pyruvate metabolism
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TCA cycle I (prokaryotic)
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TCA cycle VII (acetate-producers)
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TCA cycle VIII (helicobacter)
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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)+]).
CAS REGISTRY NUMBER
COMMENTARY hide
71822-24-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain Takeo
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Manually annotated by BRENDA team
strain Takeo
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Manually annotated by BRENDA team
gene mqoB
SwissProt
Manually annotated by BRENDA team
Chester
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Manually annotated by BRENDA team
Chester
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Manually annotated by BRENDA team
pv. tomato strain DC3000. Tn5 transposon insertion mutants (the Tn5 insertion disrupts the malate:quinone oxidoreductase gene) with reduced virulence on Arabidopsis thaliana
UniProt
Manually annotated by BRENDA team
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Swissprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
show the reaction diagram
(S)-malate + a quinone
oxaloacetate + a quinol
show the reaction diagram
(S)-malate + acceptor
oxaloacetate + reduced acceptor
show the reaction diagram
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)
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?
(S)-malate + dimethyl naphthoquinone
oxaloacetate + dimethyl naphthoquinol
show the reaction diagram
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?
(S)-malate + duroquinone
oxaloacetate + duroquinol
show the reaction diagram
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?
(S)-malate + menaquinone-1
oxaloacetate + menaquinol-1
show the reaction diagram
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menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor
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?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
(S)-malate + quinone
oxaloacetate + quinol
show the reaction diagram
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?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
show the reaction diagram
(S)-malate + ubiquinone-0
oxaloacetate + ubiquinol-0
show the reaction diagram
(S)-malate + ubiquinone-1
oxaloacetate + reduced ubiquinone-1
show the reaction diagram
ubiquinone-1 is directly reduced by the enzyme
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?
(S)-malate + ubiquinone-1
oxaloacetate + ubiquinol-1
show the reaction diagram
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?
(S)-malate + ubiquinone-6
oxaloacetate + ubiquinol-6
show the reaction diagram
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
show the reaction diagram
(S)-malate + vitamin K1
oxaloacetate + reduced vitamin K1
show the reaction diagram
(S)-malate + vitamin K3
oxaloacetate + reduced vitamin K3
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-malate + a quinone
oxaloacetate + a quinol
show the reaction diagram
(S)-malate + acceptor
oxaloacetate + reduced acceptor
show the reaction diagram
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)
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?
(S)-malate + quinone
oxaloacetate + quinol
show the reaction diagram
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?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
menadione
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triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
menaquinone
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ubiquinone
ubiquinone-0
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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
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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
vitamin K1
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-malate
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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
CoCl2
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79% inhibition at 1 mM
CuCl2
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completely inhibits the enzyme at 0.01 mM
CuSO4
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completely inhibits the enzyme at 0.1 mM
MnCl2
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86% inhibition at 1 mM
NaN3
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65% inhibition at 1 mM
nanaomycin A
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naphthoquinone derivative
NiSO4
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67% inhibition at 1 mM
Polymyxin B
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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
pyridoxal 5'-phosphate
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28% inhibition at 1 mM
Sodium amytal
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1 mM, competitive with respect to phosphatidylethanolamine, noncompetitive with respect to FAD
additional information
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o-phenanthroline does not significantly affect activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
Phospholipid
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
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in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45 - 2.6
(S)-malate
0.0024
ubiquinone 9
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pH 7.0, 20C
0.015
ubiquinone-1
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pH 7.4, 25C
0.0024
ubiquinone-9
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3
vitamin K3
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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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 hide
LITERATURE
IMAGE
additional information
additional information
Mycobacterium smegmatis
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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 hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
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isoelectric focusing, pH-range 6-8
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
not in cytosol, all analysed enzymes of the tricarboxylic acid cycle are localised in the mitochondrion
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000 - 55000
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gel filtration, sucrose density gradient centrifugation
53000
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monomeric enzyme form, gel filtration
92000
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gel filtration
164000
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aggregated form, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 50000, about, SDS-PAGE
monomer
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1 * 51000, at high salt concentrations the enzyme exists as a monomeric form which is more active than the aggregated form, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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24 h, 85% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 24 h, 70% loss of activity
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-20C, 0.3 M potassium phosphate buffer, pH 6.6, about 20% loss of activity after 2 weeks
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0C, 24 h, 50% loss of activity
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when frozen, the activity is stable for several months
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and His-tagged enzyme
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
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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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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