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show all sequences of 1.1.5.4

Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum

Molenaar, D.; Van Der Rest, M.E.; Petrovic, S.; Eur. J. Biochem. 254, 395-403 (1998)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Lipid
activates
Corynebacterium glutamicum
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Cloned(Commentary)
Commentary
Organism
-
Corynebacterium glutamicum
Inhibitors
Inhibitors
Commentary
Organism
Structure
KSCN
-
Corynebacterium glutamicum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
a peripheral membrane protein that can be released from the membrane by addition of chelators
Corynebacterium glutamicum
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + acceptor
Corynebacterium glutamicum
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)
oxaloacetate + reduced acceptor
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
O69282
a mutant completely lacking Mqo activity grows poorly on several substrates tested
-
Purification (Commentary)
Commentary
Organism
native and His-tagged enzyme
Corynebacterium glutamicum
Storage Stability
Storage Stability
Organism
when frozen, the activity is stable for several months
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + 2,6-dichlorophenol indophenol
-
287733
Corynebacterium glutamicum
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + 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)
287733
Corynebacterium glutamicum
oxaloacetate + reduced acceptor
-
-
-
?
(S)-malate + ubiquinone-1
ubiquinone-1 is directly reduced by the enzyme
287733
Corynebacterium glutamicum
oxaloacetate + reduced ubiquinone-1
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
is probably a tightly but non-covalently bound prosthetic group
Corynebacterium glutamicum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Lipid
activates
Corynebacterium glutamicum
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
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
is probably a tightly but non-covalently bound prosthetic group
Corynebacterium glutamicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
KSCN
-
Corynebacterium glutamicum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
a peripheral membrane protein that can be released from the membrane by addition of chelators
Corynebacterium glutamicum
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + acceptor
Corynebacterium glutamicum
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)
oxaloacetate + reduced acceptor
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native and His-tagged enzyme
Corynebacterium glutamicum
Storage Stability (protein specific)
Storage Stability
Organism
when frozen, the activity is stable for several months
Corynebacterium glutamicum
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
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + 2,6-dichlorophenol indophenol
-
287733
Corynebacterium glutamicum
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + 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)
287733
Corynebacterium glutamicum
oxaloacetate + reduced acceptor
-
-
-
?
(S)-malate + ubiquinone-1
ubiquinone-1 is directly reduced by the enzyme
287733
Corynebacterium glutamicum
oxaloacetate + reduced ubiquinone-1
-
-
-
?
Other publictions for EC 1.1.5.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
722575
Kabashima
Purification and characterizat ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PS3
J. Bioenerg. Biomembr.
45
131-136
2013
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1
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8
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2
2
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17
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11
1
1
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1
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4
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1
4
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8
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2
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11
1
1
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1
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1
1
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-
721563
Igeno
Metabolic adaptation of Pseudo ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
Biochem. Soc. Trans.
39
1849-1853
2011
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2
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1
1
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723124
Luque-Almagro
Cyanide degradation by Pseudom ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
Microbiology
157
739-746
2011
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6
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4
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1
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1
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2
2
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698612
Mellgren
Mqo, a tricarboxylic acid cycl ...
Pseudomonas syringae
J. Bacteriol.
191
3132-3141
2009
-
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-
-
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-
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1
-
9
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698670
Mogi
Polymyxin B identified as an i ...
Mycolicibacterium smegmatis
J. Biochem.
146
491-499
2009
-
-
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-
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3
2
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3
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1
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1
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1
3
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2
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1
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1
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1
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687185
Fleige
Localisation of gluconeogenesi ...
Toxoplasma gondii
Int. J. Parasitol.
38
1121-1132
2008
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1
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-
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1
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1
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679906
Diaz-Perez
Identification of the aceA gen ...
Pseudomonas aeruginosa
FEMS Microbiol. Lett.
269
309-316
2007
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696805
Mitsuhashi
Disruption of malate:quinone o ...
Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
2803-2806
2006
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1
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1
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1
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673714
Foerster-Fromme
Malate:quinone oxidoreductase ...
Pseudomonas aeruginosa, Pseudomonas citronellolis
FEMS Microbiol. Lett.
246
25-31
2005
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2
-
2
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2
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2
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6
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4
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2
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4
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2
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287737
Kather
Another unusual type of citric ...
Helicobacter pylori
J. Bacteriol.
182
3204-3209
2000
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1
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1
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1
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6
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287738
Molenaar
Functions of the membrane-asso ...
Corynebacterium glutamicum
J. Bacteriol.
182
6884-6891
2000
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3
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3
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698558
van der Rest
Functions of the membrane-asso ...
Escherichia coli
J. Bacteriol.
182
6892-6899
2000
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287733
Molenaar
Biochemical and genetic charac ...
Corynebacterium glutamicum
Eur. J. Biochem.
254
395-403
1998
6
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1
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6
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3
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287734
Imai
FAD-dependent malate dehydroge ...
Mycobacterium sp., Mycobacterium sp. Takeo
Biochim. Biophys. Acta
523
37-46
1978
2
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1
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2
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1
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287730
Imai
-
A phospholipid-requiring enzym ...
Mycolicibacterium phlei
J. Biol. Chem.
248
7487-7494
1973
1
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287619
Phizackerley
-
Malate dehydrogenase (FAD-link ...
Pseudomonas putida, Pseudomonas putida Chester
Methods Enzymol.
13
135-140
1969
1
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1
3
1
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11
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696072
Phizackerley
Cofactor requirements of the L ...
Pseudomonas putida, Pseudomonas putida Chester
Biochem. J.
101
524-535
1966
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