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2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
additional information
?
-
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
A0L8G4; A0L8G5
-
-
-
r
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
A0L8G4; A0L8G5
-
-
-
r
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
O87870; Q8RJQ9
specific for 2-oxoglutarate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
pure enzyme does not utilize other 2-keto acids, such as pyruvate, phenylglyoxylate, indolepyruvate, 2-oxobutanoate or 2-oxoisovalerate, as substrates
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
pure enzyme does not utilize other 2-keto acids, such as pyruvate, phenylglyoxylate, indolepyruvate, 2-oxobutanoate or 2-oxoisovalerate, as substrates
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
-
-
-
r
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
-
-
-
r
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
involved in carbon dioxide fixation via a reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
involved in reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
one of the key enzymes of the reductive TCA cycle. The physiological function is the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate, growth under aerobic conditions. Under anaerobic conditions only the Kor enzyme is expressed. The enzyme For supports the optimal growth of the organism in the presence of oxygen
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
activity of the recombinant enzyme with 2-oxobutyrate, 2-oxoisocaproate, 2-oxoisovalerate, oxalacetate, oxomalonate, pyruvate or phosphoenolpyruvate is less than 5% of the activity with 2-oxoglutarate
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
-
no activity with oxalacetate, oxomalonate, 2-oxoisocaproate, or phosphoenolpyruvate. The enzyme reacts with 2-oxobutyrate, pyruvate, and 2-oxoisovalerate at an activity level of less than 0.4 to 0.7% relative to that with 2-oxoglutarate. The enzyme uses 2-oxoglutarate, coenzyme A, and one of several electron acceptors in substrate amounts (ferredoxin isolated from Hydrogenobacter thermophilus, flavin adenine dinucleotide, flavin mononucleotide, or methyl viologen). NAD+, NADP+, and ferredoxins from Chlorella spp. and Clostridium pasteurianum are ineffective
-
-
r
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
-
no activity with oxalacetate, oxomalonate, 2-oxoisocaproate, or phosphoenolpyruvate. The enzyme reacts with 2-oxobutyrate, pyruvate, and 2-oxoisovalerate at an activity level of less than 0.4 to 0.7% relative to that with 2-oxoglutarate. The enzyme uses 2-oxoglutarate, coenzyme A, and one of several electron acceptors in substrate amounts (ferredoxin isolated from Hydrogenobacter thermophilus, flavin adenine dinucleotide, flavin mononucleotide, or methyl viologen). NAD+, NADP+, and ferredoxins from Chlorella spp. and Clostridium pasteurianum are ineffective
-
-
r
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
involved in reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
one of the key enzymes of the reductive TCA cycle. The physiological function is the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate, growth under aerobic conditions. Under anaerobic conditions only the Kor enzyme is expressed. The enzyme For supports the optimal growth of the organism in the presence of oxygen
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
involved in carbon dioxide fixation via a reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
activity of the recombinant enzyme with 2-oxobutyrate, 2-oxoisocaproate, 2-oxoisovalerate, oxalacetate, oxomalonate, pyruvate or phosphoenolpyruvate is less than 5% of the activity with 2-oxoglutarate
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
A0L8G4; A0L8G5
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
A0L8G4; A0L8G5
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
may be involved in glutamate synthesis
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
of several ferredoxins tested, only those from the photosynthetic bacteria Chlorobium thiosulfatophilum, Chromatium, and Rhodospirillum rubrum are effective. The ferredoxins of Clostridium pasteurianum and spinach are poor substitutes for those of photosynthetic bacteria
-
-
r
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
may be involved in glutamate synthesis
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
O87870; Q8RJQ9
it is proposed that the enzyme couples the complete acetyl-CoA oxidation to aromatic ring reduction by the use of the low-potential electron shuttle ferredoxin
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
-
-
-
r
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
CO2 exchange reaction and CO2 fixation, reductive TCA-cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
key enzyme in reductive tricarboxylic acid cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
CO2 exchange reaction and CO2 fixation, reductive TCA-cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
-
-
-
r
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
key enzyme in reductive tricarboxylic acid cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
enzyme plays a role in synthesis, not in energy conservation
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
enzyme plays a role in synthesis, not in energy conservation
-
-
?
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
-
-
-
r
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
involved in reductive TCA-cycle
-
-
r
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
-
-
-
r
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
involved in reductive TCA-cycle
-
-
r
additional information
?
-
A0L8G4; A0L8G5
enzyme is both CO2-fixing and 2-oxoglutarate oxidizing. Negligible activity with other 2-oxoacids, including glyoxylate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, 3-methyl-2-oxovalerate, phenylpyruvate and oxaloacetate and 2-oxoadipate
-
-
-
additional information
?
-
A0L8G4; A0L8G5
enzyme is both CO2-fixing and 2-oxoglutarate oxidizing. Negligible activity with other 2-oxoacids, including glyoxylate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, 3-methyl-2-oxovalerate, phenylpyruvate and oxaloacetate and 2-oxoadipate
-
-
-
additional information
?
-
-
enzyme is both CO2-fixing and 2-oxoglutarate oxidizing. Negligible activity with other 2-oxoacids, including glyoxylate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, 3-methyl-2-oxovalerate, phenylpyruvate and oxaloacetate and 2-oxoadipate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
involved in carbon dioxide fixation via a reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
involved in reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
one of the key enzymes of the reductive TCA cycle. The physiological function is the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate, growth under aerobic conditions. Under anaerobic conditions only the Kor enzyme is expressed. The enzyme For supports the optimal growth of the organism in the presence of oxygen
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0
involved in reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
one of the key enzymes of the reductive TCA cycle. The physiological function is the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate, growth under aerobic conditions. Under anaerobic conditions only the Kor enzyme is expressed. The enzyme For supports the optimal growth of the organism in the presence of oxygen
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
Q9AJM0; Q9AJL9
involved in carbon dioxide fixation via a reductive TCA cycle
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
may be involved in glutamate synthesis
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
may be involved in glutamate synthesis
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
O87870; Q8RJQ9
it is proposed that the enzyme couples the complete acetyl-CoA oxidation to aromatic ring reduction by the use of the low-potential electron shuttle ferredoxin
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
CO2 exchange reaction and CO2 fixation, reductive TCA-cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
key enzyme in reductive tricarboxylic acid cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
CO2 exchange reaction and CO2 fixation, reductive TCA-cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
key enzyme in reductive tricarboxylic acid cycle
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
enzyme plays a role in synthesis, not in energy conservation
-
-
?
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
-
enzyme plays a role in synthesis, not in energy conservation
-
-
?
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
involved in reductive TCA-cycle
-
-
r
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
-
involved in reductive TCA-cycle
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.11 - 4.9
2-oxoglutarate
0.008 - 1.8
oxidized ferredoxin
0.00055 - 1.3
reduced ferredoxin
0.11
2-oxoglutarate
O87870; Q8RJQ9
pH 7.8, 30°C
0.25
2-oxoglutarate
-
pH 8.4, 80°C
0.64
2-oxoglutarate
A0L8G4; A0L8G5
mutant E45Q, pH 7.5, temperature not specified in the publication
0.97
2-oxoglutarate
A0L8G4; A0L8G5
wild-type, pH 7.0, temperature not specified in the publication
1.4
2-oxoglutarate
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
pH 7.8, 70°C, recombinant Kor
1.42
2-oxoglutarate
-
pH 7.6, 70°C
1.8
2-oxoglutarate
A0L8G4; A0L8G5
mutant Y436F, pH 7.5, temperature not specified in the publication
2.6
2-oxoglutarate
-
pH and temperature not specified in the publication
2.9
2-oxoglutarate
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
pH 7.8, 70°C, recombinant For
4.4
2-oxoglutarate
A0L8G4; A0L8G5
wild-type, pH 8.5, temperature not specified in the publication
4.9
2-oxoglutarate
A0L8G4; A0L8G5
wild-type, pH 7.5, temperature not specified in the publication
0.026
CoA
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
pH 7.8, 70°C, recombinant For
0.08
CoA
D3DIA1; D3DIA2; D3DIA3; D3DIA0; Q93RA0, Q9AJM0; Q9AJL9
pH 7.8, 70°C, recombinant Kor
0.29
CoA
O87870; Q8RJQ9
pH 7.8, 30°C
6.8
CoA
A0L8G4; A0L8G5
wild-type, pH 8.5, temperature not specified in the publication
10
CoA
A0L8G4; A0L8G5
wild-type, pH 7.0, temperature not specified in the publication
0.008
oxidized ferredoxin
-
pH 8.4, 80°C, ferredoxin from Pyrococcus furiosus
0.01
oxidized ferredoxin
O87870; Q8RJQ9
pH 7.8, 30°C
1.8
oxidized ferredoxin
A0L8G4; A0L8G5
wild-type, pH 7.0, temperature not specified in the publication
0.00055
reduced ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
isozyme Kor, in 10 mM MOPS, pH 6.8, at 70°C
0.0025
reduced ferredoxin
Q93RA3; Q93RA2, Q9AJM0; Q9AJL9
isozyme For, in 10 mM MOPS, pH 6.8, at 70°C
1.3
reduced ferredoxin
A0L8G4; A0L8G5
wild-type, pH 7.0, temperature not specified in the publication
0.25
succinyl-CoA
-
pH and temperature not specified in the publication
32
succinyl-CoA
A0L8G4; A0L8G5
wild-type, pH 7.0, temperature not specified in the publication
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Yoon, K.S.; Ishii, M.; Kodama, T.; Igarashi, Y.
Carboxylation reactions of pyruvate:ferredoxin oxidoreductase and 2-oxoglutarate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6
Biosci. Biotechnol. Biochem.
61
510-513
1997
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
-
brenda
Gehring, U.; Arnon, D.I.
Purification and properties of alpha-ketoglutarate synthase from a photosynthetic bacterium
J. Biol. Chem.
247
6963-6969
1972
Prosthecochloris vibrioformis f. thiosulfatophilum
brenda
Mai, X.; Adams, M.W.W.
Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis
J. Bacteriol.
178
5890-5896
1996
Thermococcus litoralis, Thermococcus litoralis DSM 5473
brenda
Yoon, K.S.; Ishii, M.; Igarashi, Y.; Kodama, T.
Purification and characterization of 2-oxoglutarate:ferredoxin oxidoreductase from a thermophilic, obligately chemolithoautotrophic bacterium, Hydrogenobacter thermophilus TK-6
J. Bacteriol.
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3365-3368
1996
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
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Drner, E.; Boll, M.
Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring
J. Bacteriol.
184
3975-3983
2002
Thauera aromatica (O87870 and Q8RJQ9), Thauera aromatica
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Yun, N.R.; Arai, H.; Ishii, M.; Igarashi, Y.
The genes for anabolic 2-oxoglutarate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6
Biochem. Biophys. Res. Commun.
282
589-594
2001
Hydrogenobacter thermophilus (Q9AJM0 and Q9AJL9), Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695 (Q9AJM0 and Q9AJL9)
brenda
Yun, N.R.; Yamamoto, M.; Arai, H.; Ishii, M.; Igarashi, Y.
A novel five-subunit-type 2-oxoglutalate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus TK-6
Biochem. Biophys. Res. Commun.
292
280-286
2002
Hydrogenobacter thermophilus (D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0), Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695 (D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0)
brenda
Yamamoto, M.; Arai, H.; Ishii, M.; Igarashi, Y.
Characterization of two different 2-oxoglutarate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus TK-6
Biochem. Biophys. Res. Commun.
312
1297-1302
2003
Hydrogenobacter thermophilus (D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0), Hydrogenobacter thermophilus (Q9AJM0 and Q9AJL9), Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695 (D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0), Hydrogenobacter thermophilus TK-6 / IAM 12695 (Q9AJM0 and Q9AJL9)
brenda
Yamamoto, M.; Arai, H.; Ishii, M.; Igarashi, Y.
Role of two 2-oxoglutarate:ferredoxin oxidoreductases in Hydrogenobacter thermophilus under aerobic and anaerobic conditions
FEMS Microbiol. Lett.
263
189-193
2006
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
brenda
Yamamoto, M.; Ikeda, T.; Arai, H.; Ishii, M.; Igarashi, Y.
Carboxylation reaction catalyzed by 2-oxoglutarate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus
Extremophiles
14
79-85
2010
Hydrogenobacter thermophilus (Q93RA3 and Q93RA2), Hydrogenobacter thermophilus (Q9AJM0 and Q9AJL9), Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695 (Q93RA3 and Q93RA2), Hydrogenobacter thermophilus TK-6 / IAM 12695 (Q9AJM0 and Q9AJL9)
brenda
Gilbreath, J.J.; West, A.L.; Pich, O.Q.; Carpenter, B.M.; Michel, S.; Merrell, D.S.
Fur activates expression of the 2-oxoglutarate oxidoreductase genes (oorDABC) in Helicobacter pylori
J. Bacteriol.
194
6490-6497
2012
Helicobacter pylori, Helicobacter pylori DSM 1
brenda
Buchanan, B.B.; Evans, M.C.W.
The synthesis of alpha-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium
Proc. Natl. Acad. Sci. USA
54
1212-1218
1965
Prosthecochloris vibrioformis f. thiosulfatophilum, Prosthecochloris vibrioformis f. thiosulfatophilum Tassajara
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus
brenda
Chen, P.Y.; Li, B.; Drennan, C.L.; Elliott, S.J.
A reverse TCA cycle 2-oxoacid ferredoxin oxidoreductase that makes C-C bonds from CO2
Joule
3
595-611
2019
Magnetococcus marinus (A0L8G4 and A0L8G5), Magnetococcus marinus MC-1 (A0L8G4 and A0L8G5), Magnetococcus marinus MC-1
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