Information on EC 1.1.5.4 - malate dehydrogenase (quinone) and Organism(s) Corynebacterium glutamicum and UniProt Accession O69282

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This record set is specific for:
Corynebacterium glutamicum
UNIPROT: O69282


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


The taxonomic range for the selected organisms is: Corynebacterium glutamicum

EC NUMBER
COMMENTARY hide
1.1.5.4
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RECOMMENDED NAME
GeneOntology No.
malate dehydrogenase (quinone)
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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Citrate cycle (TCA cycle)
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Pyruvate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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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
a mutant completely lacking Mqo activity grows poorly on several substrates tested
UniProt
Manually annotated by BRENDA team
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
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?
(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 + ubiquinone-1
oxaloacetate + reduced ubiquinone-1
show the reaction diagram
ubiquinone-1 is directly reduced by the enzyme
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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 + 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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?
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
is probably a tightly but non-covalently bound prosthetic group
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
a peripheral membrane protein that can be released from the membrane by addition of chelators
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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