BRENDA - Enzyme Database show
show all sequences of 1.1.5.4

Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli

van der Rest, M.E.; Frank, C.; Molenaar, D.; J. Bacteriol. 182, 6892-6899 (2000)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
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
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Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
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Source Tissue
Source Tissue
Commentary
Organism
Textmining
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
Escherichia coli
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Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
698558
Escherichia coli
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Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
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
?
-
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Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
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
Escherichia coli
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
698558
Escherichia coli
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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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17
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1
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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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723124
Luque-Almagro
Cyanide degradation by Pseudom ...
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes CECT 5344
Microbiology
157
739-746
2011
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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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698670
Mogi
Polymyxin B identified as an i ...
Mycolicibacterium smegmatis
J. Biochem.
146
491-499
2009
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3
2
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3
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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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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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673714
Foerster-Fromme
Malate:quinone oxidoreductase ...
Pseudomonas aeruginosa, Pseudomonas citronellolis
FEMS Microbiol. Lett.
246
25-31
2005
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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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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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287738
Molenaar
Functions of the membrane-asso ...
Corynebacterium glutamicum
J. Bacteriol.
182
6884-6891
2000
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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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287734
Imai
FAD-dependent malate dehydroge ...
Mycobacterium sp., Mycobacterium sp. Takeo
Biochim. Biophys. Acta
523
37-46
1978
2
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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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696072
Phizackerley
Cofactor requirements of the L ...
Pseudomonas putida, Pseudomonas putida Chester
Biochem. J.
101
524-535
1966
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