Information on EC 1.2.7.3 - 2-oxoglutarate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.2.7.3
-
RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reductive carboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
-
Citrate cycle (TCA cycle)
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-
incomplete reductive TCA cycle
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Metabolic pathways
-
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Microbial metabolism in diverse environments
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-
reductive TCA cycle I
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reductive TCA cycle II
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TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
-
TCA cycle VIII (helicobacter)
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-
citric acid cycle
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-
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating)
The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
37251-05-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O87870: alpha-subunit, Q8RJQ9: beta-subunit
O87870 and Q8RJQ9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen
show the reaction diagram
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
show the reaction diagram
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
show the reaction diagram
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized ferredoxin
show the reaction diagram
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + oxidized ferredoxin
show the reaction diagram
succinyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + oxidized ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
O87870 and Q8RJQ9
1.6 mol per mol of enzyme
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron-sulfur cluster
Mg2+
-
stimulates, 2.5 mM
additional information
-
no effect of Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuSO4
-
0.05 mM, complete inhibition
Sodium nitrite
-
high concentrations
ZnCl2
-
0.1 mM, complete inhibition
additional information
-
no inhibition: CO, no inhibition at 5 mM: sodium benzoate, NaF, sodium hypophosphite, NaN3, KCN, 2-oxohexanoate, pyruvate, 2-oxobutyrate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
0.9 mol per mol of enzyme, stimulates but is not essential, Km: 0.009 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 2.9
2-oxoglutarate
0.026 - 0.29
CoA
0.008 - 0.01
oxidized ferredoxin
0.00055 - 0.0025
reduced ferredoxin
0.25
succinyl-CoA
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17
2-oxoglutarate
Thauera aromatica
O87870 and Q8RJQ9
pH 7.8, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52 - 23.6
2-oxoglutarate
34
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
Sodium nitrite
-
pH 8.4, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.15
-
crude extract, pH 8.4, 80C
0.68
Q9AJM0 and Q9AJL9
70C, pH not specified in the publication
1.25
-
pH and temperature not specified in the publication
3.34
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0
70C, pH not specified in the publication, recombinant enzyme, oxidative decarboxylation of 2-oxoglutarate
4.8
O87870 and Q8RJQ9
pH 7.8, 30C
22.3
-
pH 8.4, 80C, purified enzyme
35.2
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
pH 7.8, 70C, recombinant Kor
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.8
-
optimum with a sharp drop on the acidic side
7.6 - 7.8
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2-oxoglutarate oxidation reaction
7.7
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
recombinant Kor
8.3
O87870 and Q8RJQ9
glycylglycine buffer
8.7
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
recombinant For, at 70C, optimum varies between buffers
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.7
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
pH 7.0: about 45% of maximal activity, pH 9.7: about 65% of maximal activity, recombinant For
7 - 9.5
-
50% activity at pH 7.0 and pH 9.5, inactive at pH 5.0 and pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
recombinant For enzyme
90
-
above, at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 90
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
60C: about 35% of maximal activity, 90C: about 50% of maximal activity, recombinant For, the recombinant For enzyme is inactive at room temperature
70 - 95
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inactive below 25C, drastical increase of activity at 70C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
2 * 43000 + 2 * 29000 + 2 * 23000 + 2 * 10000, alpha2-beta2-gamma2-delta2, SDS-PAGE
24000
-
1 * 10000 + 1 * 43000 + 1 * 33000 + 1 * 24000
29000
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2 * 43000 + 2 * 29000 + 2 * 23000 + 2 * 10000, alpha2-beta2-gamma2-delta2, SDS-PAGE
32678
Q9AJM0 and Q9AJL9
x * 67673 (subunit alpha) + x * 32678 (subunit beta), calculated from sequence
34000
O87870 and Q8RJQ9
2 * 66000 + 2 * 34000, alpha2-beta2, SDS-PAGE
35000
-
1 * 70000 + 1 * 35000, alphabeta, SDS-PAGE
66000
O87870 and Q8RJQ9
2 * 66000 + 2 * 34000, alpha2-beta2, SDS-PAGE
67673
Q9AJM0 and Q9AJL9
x * 67673 (subunit alpha) + x * 32678 (subunit beta), calculated from sequence
68000
Q9AJM0 and Q9AJL9
x * 68000 (alpha-subunit) + x * 33000 (beta-subunit), SDS-PAGE
70000
-
1 * 70000 + 1 * 35000, alphabeta, SDS-PAGE
105000
-
gel filtration
200000
O87870 and Q8RJQ9
gel filtration
210000
-
native PAGE
220000
-
sucrose density gradient sedimentation
230000
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
recombinant For, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
octamer
oligomer
tetramer
O87870 and Q8RJQ9
2 * 66000 + 2 * 34000, alpha2-beta2, SDS-PAGE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
recombinant For, about 90% loss of activity under aerobic conditions, about 30% loss of activity under anaerobic conditions
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.5 mM KCl 0.5 M, 10% glycerol 1 mM dithiothreitol, stabilize
O87870 and Q8RJQ9
stabilized under anaerobic conditions by a combination of dimercaptoethanol and FeSO4
-
Triton X-100 highly stablizes during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic conditions, 4C, 50% loss of activity after 1 day
O87870 and Q8RJQ9
288468
oxygen sensitive, half-life of about 5 min
-
288466
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, anaerobic conditions, 2,3-dimercaptoethanol plus FeSO4
-
4C, anaerobic conditions, 100% N2-atmosphere, 4 mM MgCl2, 1 mM dithiothreitol, 2 mM thiamine diphosphate, 10% glycerol, stable for at least 1 day
O87870 and Q8RJQ9
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
;
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
wild-type and recombinant enzyme
Q9AJM0 and Q9AJL9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli JM109
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0
expression in Escherichia coli; expression in Escherichia coli
Q93RA3 and Q93RA2, Q9AJM0 and Q9AJL9
expression of forDABGE in Escherichia coli JM109, structure of gene cluster; expression of korAB in Escherichia coli JM109, structure of gene cluster
D3DIA1 and D3DIA2 and D3DIA3 and D3DIA0 and Q93RA0, Q9AJM0 and Q9AJL9
korAB genes, expression in Escherichia coli
Q9AJM0 and Q9AJL9
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inducible by growth on aromatic substrates and under denitrifiying conditions 10 to 50fold
O87870 and Q8RJQ9
the expression of the oorDABC genes is activated by ferric uptake regulator under iron-replete conditions
the For enzyme is expressed constitutively during oxygen respiration. Little expression of For is observed during cultivation under conditions of nitrate respiration; the Kor enzyme is constitutively expressed during respiration of either oxygen or nitrate respiration
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