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(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
(S)-malate + a quinone
oxaloacetate + a quinol
(S)-malate + acceptor
oxaloacetate + reduced 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)
-
-
?
(S)-malate + dimethyl naphthoquinone
oxaloacetate + dimethyl naphthoquinol
(S)-malate + duroquinone
oxaloacetate + duroquinol
(S)-malate + menaquinone-1
oxaloacetate + menaquinol-1
-
menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
(S)-malate + quinone
oxaloacetate + quinol
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
(S)-malate + ubiquinone-0
oxaloacetate + ubiquinol-0
(S)-malate + ubiquinone-1
oxaloacetate + reduced ubiquinone-1
ubiquinone-1 is directly reduced by the enzyme
-
-
?
(S)-malate + ubiquinone-1
oxaloacetate + ubiquinol-1
-
-
-
-
?
(S)-malate + ubiquinone-6
oxaloacetate + ubiquinol-6
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
(S)-malate + vitamin K1
oxaloacetate + reduced vitamin K1
(S)-malate + vitamin K3
oxaloacetate + reduced vitamin K3
-
-
-
-
?
additional information
?
-
(S)-malate + 2,6-dichlorophenol indophenol

oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + 2,6-dichlorphenolindophenol

oxaloacetate + reduced 2,6-dichlorphenolindophenol
assay in presence of 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
?
(S)-malate + 2,6-dichlorphenolindophenol
oxaloacetate + reduced 2,6-dichlorphenolindophenol
assay in presence of 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
?
(S)-malate + a quinone

oxaloacetate + a quinol
-
-
-
-
?
(S)-malate + a quinone
oxaloacetate + a quinol
-
-
-
-
?
(S)-malate + dimethyl naphthoquinone

oxaloacetate + dimethyl naphthoquinol
-
-
-
-
?
(S)-malate + dimethyl naphthoquinone
oxaloacetate + dimethyl naphthoquinol
-
-
-
-
?
(S)-malate + duroquinone

oxaloacetate + duroquinol
-
-
-
-
?
(S)-malate + duroquinone
oxaloacetate + duroquinol
-
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol

oxaloacetate + reduced 2,6-dichlorophenol indophenol
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
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + oxidized 2,6-dichlorophenol indophenol
oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
(S)-malate + quinone

oxaloacetate + quinol
-
-
-
-
?
(S)-malate + quinone
oxaloacetate + quinol
-
-
-
-
?
(S)-malate + ubiquinone

oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
with dichlorophenolindophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
with dichlorophenolindophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone-0

oxaloacetate + ubiquinol-0
-
-
-
-
?
(S)-malate + ubiquinone-0
oxaloacetate + ubiquinol-0
-
-
-
-
?
(S)-malate + ubiquinone-6

oxaloacetate + ubiquinol-6
-
-
-
-
?
(S)-malate + ubiquinone-6
oxaloacetate + ubiquinol-6
-
-
-
-
?
(S)-malate + ubiquinone-9

oxaloacetate + ubiquinol-9
-
-
-
-
?
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
-
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
-
-
?
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
-
-
-
-
?
(S)-malate + ubiquinone-9
oxaloacetate + ubiquinol-9
-
in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor
-
-
?
(S)-malate + vitamin K1

oxaloacetate + reduced vitamin K1
-
-
-
-
?
(S)-malate + vitamin K1
oxaloacetate + reduced vitamin K1
-
-
-
-
?
(S)-malate + vitamin K1
oxaloacetate + reduced vitamin K1
-
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
Corynebacterium glutamicum possesses two types of L-malate dehydrogenase, a membrane-associated malate:quinone oxidoreductase (MQO) and a cytoplasmic malate dehydrogenase (MDH, EC 1.1.1.37). MQO, MDH, and succinate dehydrogenase (SDH) activities are regulated coordinately in response to the carbon and energy source for growth. Compared to growth on glucose, these activities are increased during growth on lactate, pyruvate, or acetate, substrates which require high citric acid cycle activity to sustain growth. MQO is the most important malate dehydrogenase in the physiology of Corynebacterium glutamicum. A mutant with a site-directed deletion in the mqo gene does not grow on minimal medium. Growth can be partially restored in this mutant by addition of the vitamin nicotinamide. In contrast, a double mutant lacking MQO and MDH does not grow even in the presence of nicotinamide. MDH is able to take over the function of MQO in an mqo mutant, but this requires the presence of nicotinamide in the growth medium. It is shown that addition of nicotinamide leads to a higher intracellular pyridine nucleotide concentration, which probably enables MDH to catalyze malate oxidation. Purified MDH catalyzes oxaloacetate reduction much more readily than malate oxidation at physiological pH. In a reconstituted system with isolated membranes and purified MDH, MQO and MDH catalyze the cyclic conversion of malate and oxaloacetate, leading to a net oxidation of NADH. Evidence is presented that this cyclic reaction also takes place in vivo
-
-
?
additional information
?
-
-
the loss of malate:quinone oxidoreductase activity down-regulates the flux of the tricarboxylic acid cycle to maintain the redox balance and results in redirection of oxaloacetate into L-lysine biosynthesis
-
-
?
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
-
-
?
additional information
?
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
a mutant with an interrupted putative mqo gene, in which malate:quinone oxidoreductase, an enzyme involved in the citric acid cycle/glyoxylate cycle, is defective, shows a severe growth defect on ethanol and is unable to grow on acetate
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate + a quinone
oxaloacetate + a quinol
(S)-malate + acceptor
oxaloacetate + reduced 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)
-
-
?
(S)-malate + quinone
oxaloacetate + quinol
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
additional information
?
-
(S)-malate + a quinone

oxaloacetate + a quinol
-
-
-
-
?
(S)-malate + a quinone
oxaloacetate + a quinol
-
-
-
-
?
(S)-malate + quinone

oxaloacetate + quinol
-
-
-
-
?
(S)-malate + quinone
oxaloacetate + quinol
-
-
-
-
?
(S)-malate + ubiquinone

oxaloacetate + ubiquinol
-
-
-
-
?
(S)-malate + ubiquinone
oxaloacetate + ubiquinol
-
-
-
-
?
additional information

?
-
-
Corynebacterium glutamicum possesses two types of L-malate dehydrogenase, a membrane-associated malate:quinone oxidoreductase (MQO) and a cytoplasmic malate dehydrogenase (MDH, EC 1.1.1.37). MQO, MDH, and succinate dehydrogenase (SDH) activities are regulated coordinately in response to the carbon and energy source for growth. Compared to growth on glucose, these activities are increased during growth on lactate, pyruvate, or acetate, substrates which require high citric acid cycle activity to sustain growth. MQO is the most important malate dehydrogenase in the physiology of Corynebacterium glutamicum. A mutant with a site-directed deletion in the mqo gene does not grow on minimal medium. Growth can be partially restored in this mutant by addition of the vitamin nicotinamide. In contrast, a double mutant lacking MQO and MDH does not grow even in the presence of nicotinamide. MDH is able to take over the function of MQO in an mqo mutant, but this requires the presence of nicotinamide in the growth medium. It is shown that addition of nicotinamide leads to a higher intracellular pyridine nucleotide concentration, which probably enables MDH to catalyze malate oxidation. Purified MDH catalyzes oxaloacetate reduction much more readily than malate oxidation at physiological pH. In a reconstituted system with isolated membranes and purified MDH, MQO and MDH catalyze the cyclic conversion of malate and oxaloacetate, leading to a net oxidation of NADH. Evidence is presented that this cyclic reaction also takes place in vivo
-
-
?
additional information
?
-
-
the loss of malate:quinone oxidoreductase activity down-regulates the flux of the tricarboxylic acid cycle to maintain the redox balance and results in redirection of oxaloacetate into L-lysine biosynthesis
-
-
?
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
-
-
?
additional information
?
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
-
the enzyme is part of both the electron transfer chain and the citric acid cycle
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
a mutant with an interrupted putative mqo gene, in which malate:quinone oxidoreductase, an enzyme involved in the citric acid cycle/glyoxylate cycle, is defective, shows a severe growth defect on ethanol and is unable to grow on acetate
-
-
?
additional information
?
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
-
the enzyme is required for growth on acetate and linear terpenes such as citronellol and citronellic acid
-
-
?
additional information
?
-
mutants lacking mqo function grow more slowly in culture than wild-type bacteria when dicarboxylates are the only available carbon source. Mqo may be required by DC3000 to meet nutritional requirements in the apoplast and may provide insight into the mechanisms underlying the important, but poorly understood process of adaptation to the host environment
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
menadione
-
triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
ubiquinone-0
-
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
-
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
FAD

-
Km: 0.0004 mM
FAD
-
in absence of FAD no reduction of 2,6-dichlorophenol indophenol is observed
FAD
is probably a tightly but non-covalently bound prosthetic group
FAD
-
the enzyme requires FAD and vitamin K for activity
FAD
-
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. Km-value for FAD is 0.0004 mM
FAD
-
noncovalently bound as a prosthetic group
ubiquinone

-
-
vitamin K1

-
the enzyme requires FAD and vitamin K for activity
vitamin K1
-
with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
additional information

-
no spectral evidence for the presence of a flavin or quinone in the purified enzyme
-
additional information
-
the enzyme is active with 2,6-dichlorophenolindophenol
-
additional information
-
the enzymeis active with duroquinone and dimethyl naphthoquinone
-
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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
vitamin K3
-
in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid

-
in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid
-
activity of purified enzyme is dependent on added phospholipid
Phospholipid
-
the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism
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Phizackerley, P.J.R.
Malate dehydrogenase (FAD-linked) from Pseudomonas ovalis Chester
Methods Enzymol.
13
135-140
1969
Pseudomonas putida, Pseudomonas putida Chester
-
brenda
Imai, K.; Brodie, A.F.
A phospholipid-requiring enzyme, malate-vitamin K reductase
J. Biol. Chem.
248
7487-7494
1973
Mycolicibacterium phlei
-
brenda
Molenaar, D.; Van Der Rest, M.E.; Petrovic, S.
Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum
Eur. J. Biochem.
254
395-403
1998
Corynebacterium glutamicum (O69282), Corynebacterium glutamicum
brenda
Imai, T.
FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties
Biochim. Biophys. Acta
523
37-46
1978
Mycobacterium sp., Mycobacterium sp. Takeo
brenda
Kather, B.; Stingl, K.; van der Rest, M.E.; Altendorf, K.; Molenaar, D.
Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase
J. Bacteriol.
182
3204-3209
2000
Helicobacter pylori (O24913), Helicobacter pylori
brenda
Molenaar, D.; van der Rest, M.E.; Drysch, A.; Yucel, R.
Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Corynebacterium glutamicum
J. Bacteriol.
182
6884-6891
2000
Corynebacterium glutamicum
brenda
Foerster-Fromme, K.; Jendrossek, D.
Malate:quinone oxidoreductase (MqoB) is required for growth on acetate and linear terpenes in Pseudomonas citronellolis
FEMS Microbiol. Lett.
246
25-31
2005
Pseudomonas citronellolis (Q5ECC3), Pseudomonas citronellolis, Pseudomonas aeruginosa (Q9HVF1), Pseudomonas aeruginosa
brenda
Diaz-Perez, A.L.; Roman-Doval, C.; Diaz-Perez, C.; Cervantes, C.; Sosa-Aguirre, C.R.; Lopez-Meza, J.E.; Campos-Garcia, J.
Identification of the aceA gene encoding isocitrate lyase required for the growth of Pseudomonas aeruginosa on acetate, acyclic terpenes and leucine
FEMS Microbiol. Lett.
269
309-316
2007
Pseudomonas aeruginosa (Q9HVF1)
brenda
Fleige, T.; Pfaff, N.; Gross, U.; Bohne, W.
Localisation of gluconeogenesis and tricarboxylic acid (TCA)-cycle enzymes and first functional analysis of the TCA cycle in Toxoplasma gondii
Int. J. Parasitol.
38
1121-1132
2008
Toxoplasma gondii (Q1KSF3)
brenda
Phizackerley, P.J.; Francis, M.J.
Cofactor requirements of the L-malate dehydrogenase of Pseudomonas ovalis Chester
Biochem. J.
101
524-535
1966
Pseudomonas putida, Pseudomonas putida Chester
brenda
Mitsuhashi, S.; Hayashi, M.; Ohnishi, J.; Ikeda, M.
Disruption of malate:quinone oxidoreductase increases L-lysine production by Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
2803-2806
2006
Corynebacterium glutamicum
brenda
van der Rest, M.E.; Frank, C.; Molenaar, D.
Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli
J. Bacteriol.
182
6892-6899
2000
Escherichia coli
brenda
Mellgren, E.M.; Kloek, A.P.; Kunkel, B.N.
Mqo, a tricarboxylic acid cycle enzyme, is required for virulence of Pseudomonas syringae pv. tomato strain DC3000 on Arabidopsis thaliana
J. Bacteriol.
191
3132-3141
2009
Pseudomonas syringae (Q887Z4)
brenda
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Mycolicibacterium smegmatis
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Pseudomonas oleovorans, Pseudomonas oleovorans CECT 5344
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Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PS3
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Microbiology
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Pseudomonas oleovorans, Pseudomonas oleovorans CECT 5344
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