BRENDA - Enzyme Database
show all sequences of 1.1.5.4

Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3

Kabashima, Y.; Sone, N.; Kusumoto, T.; Sakamoto, J.; J. Bioenerg. Biomembr. 45, 131-136 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis
Bacillus sp. (in: Bacteria)
Inhibitors
Inhibitors
Commentary
Organism
Structure
CoCl2
79% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
CuCl2
completely inhibits the enzyme at 0.01 mM
Bacillus sp. (in: Bacteria)
CuSO4
completely inhibits the enzyme at 0.1 mM
Bacillus sp. (in: Bacteria)
MnCl2
86% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
additional information
o-phenanthroline does not significantly affect activity
Bacillus sp. (in: Bacteria)
NaN3
65% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
NiSO4
67% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
pyridoxal 5'-phosphate
28% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, about, SDS-PAGE
Bacillus sp. (in: Bacteria)
92000
-
gel filtration
Bacillus sp. (in: Bacteria)
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + quinone
Bacillus sp. (in: Bacteria)
-
oxaloacetate + quinol
-
-
?
(S)-malate + quinone
Bacillus sp. (in: Bacteria) PS3
-
oxaloacetate + quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) PS3
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + dimethyl naphthoquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + dimethyl naphthoquinol
-
-
-
?
(S)-malate + dimethyl naphthoquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + dimethyl naphthoquinol
-
-
-
?
(S)-malate + duroquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + duroquinol
-
-
-
?
(S)-malate + duroquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + duroquinol
-
-
-
?
(S)-malate + menaquinone-1
menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + menaquinol-1
-
-
-
?
(S)-malate + quinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + quinol
-
-
-
?
(S)-malate + quinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + quinol
-
-
-
?
(S)-malate + ubiquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + ubiquinol
-
-
-
?
(S)-malate + ubiquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + ubiquinol
-
-
-
?
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
722575
Bacillus sp. (in: Bacteria)
?
-
-
-
-
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
722575
Bacillus sp. (in: Bacteria) PS3
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 50000, about, SDS-PAGE
Bacillus sp. (in: Bacteria)
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Bacillus sp. (in: Bacteria)
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Bacillus sp. (in: Bacteria)
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
noncovalently bound as a prosthetic group
Bacillus sp. (in: Bacteria)
menaquinone
-
Bacillus sp. (in: Bacteria)
additional information
the enzymeis active with duroquinone and dimethyl naphthoquinone
Bacillus sp. (in: Bacteria)
ubiquinone
-
Bacillus sp. (in: Bacteria)
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis
Bacillus sp. (in: Bacteria)
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
noncovalently bound as a prosthetic group
Bacillus sp. (in: Bacteria)
menaquinone
-
Bacillus sp. (in: Bacteria)
additional information
the enzymeis active with duroquinone and dimethyl naphthoquinone
Bacillus sp. (in: Bacteria)
ubiquinone
-
Bacillus sp. (in: Bacteria)
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CoCl2
79% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
CuCl2
completely inhibits the enzyme at 0.01 mM
Bacillus sp. (in: Bacteria)
CuSO4
completely inhibits the enzyme at 0.1 mM
Bacillus sp. (in: Bacteria)
MnCl2
86% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
additional information
o-phenanthroline does not significantly affect activity
Bacillus sp. (in: Bacteria)
NaN3
65% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
NiSO4
67% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
pyridoxal 5'-phosphate
28% inhibition at 1 mM
Bacillus sp. (in: Bacteria)
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, about, SDS-PAGE
Bacillus sp. (in: Bacteria)
92000
-
gel filtration
Bacillus sp. (in: Bacteria)
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + quinone
Bacillus sp. (in: Bacteria)
-
oxaloacetate + quinol
-
-
?
(S)-malate + quinone
Bacillus sp. (in: Bacteria) PS3
-
oxaloacetate + quinol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + dimethyl naphthoquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + dimethyl naphthoquinol
-
-
-
?
(S)-malate + dimethyl naphthoquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + dimethyl naphthoquinol
-
-
-
?
(S)-malate + duroquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + duroquinol
-
-
-
?
(S)-malate + duroquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + duroquinol
-
-
-
?
(S)-malate + menaquinone-1
menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + menaquinol-1
-
-
-
?
(S)-malate + quinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + quinol
-
-
-
?
(S)-malate + quinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + quinol
-
-
-
?
(S)-malate + ubiquinone
-
722575
Bacillus sp. (in: Bacteria)
oxaloacetate + ubiquinol
-
-
-
?
(S)-malate + ubiquinone
-
722575
Bacillus sp. (in: Bacteria) PS3
oxaloacetate + ubiquinol
-
-
-
?
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
722575
Bacillus sp. (in: Bacteria)
?
-
-
-
-
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
722575
Bacillus sp. (in: Bacteria) PS3
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 50000, about, SDS-PAGE
Bacillus sp. (in: Bacteria)
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Bacillus sp. (in: Bacteria)
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Bacillus sp. (in: Bacteria)
General Information
General Information
Commentary
Organism
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
Bacillus sp. (in: Bacteria)
General Information (protein specific)
General Information
Commentary
Organism
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
Bacillus sp. (in: Bacteria)
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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3
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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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1
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2
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6
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4
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1
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2
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1
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2
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-
-
4
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
698612
Mellgren
Mqo, a tricarboxylic acid cycl ...
Pseudomonas syringae
J. Bacteriol.
191
3132-3141
2009
-
-
-
-
-
-
-
-
-
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1
-
9
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1
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1
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1
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698670
Mogi
Polymyxin B identified as an i ...
Mycolicibacterium smegmatis
J. Biochem.
146
491-499
2009
-
-
-
-
-
-
3
2
-
-
-
-
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3
-
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1
-
1
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1
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1
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1
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1
3
1
2
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1
-
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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1
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1
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1
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1
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-
-
-
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-
-
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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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-
-
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1
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1
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1
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-
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696805
Mitsuhashi
Disruption of malate:quinone o ...
Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
2803-2806
2006
-
1
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1
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2
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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
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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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2
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2
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2
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2
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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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1
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1
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6
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1
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2
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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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1
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3
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1
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1
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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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1
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1
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1
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1
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1
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1
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287733
Molenaar
Biochemical and genetic charac ...
Corynebacterium glutamicum
Eur. J. Biochem.
254
395-403
1998
6
-
1
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1
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2
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1
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6
-
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1
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2
3
-
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-
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1
-
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6
-
1
1
-
-
-
-
1
-
-
2
-
-
1
-
-
-
1
-
-
-
2
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287734
Imai
FAD-dependent malate dehydroge ...
Mycobacterium sp., Mycobacterium sp. Takeo
Biochim. Biophys. Acta
523
37-46
1978
2
-
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-
-
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1
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3
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1
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1
1
2
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1
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1
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2
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1
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1
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1
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1
1
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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3
-
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1
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1
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1
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1
1
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3
-
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1
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3
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