Information on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.7.11
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RECOMMENDED NAME
GeneOntology No.
2-oxoacid oxidoreductase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
isoleucine metabolism
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threonine metabolism
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Glycolysis / Gluconeogenesis
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Citrate cycle (TCA cycle)
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Pyruvate metabolism
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Butanoate metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
2-oxocarboxylate:ferredoxin 2-oxidoreductase (decarboxylating, CoA-acylating)
Contains thiamine diphosphate and [4Fe-4S] clusters [2]. 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 example, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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-oxo-4-methylthiobutyrate + CoA + 2 methyl viologen
3-methylthiopropanoyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472, 48% of the activity compared to glyoxylate
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-
?
2-oxoadipate + CoA + 2 methyl viologen
glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472, 49% of the activity compared to glyoxylate
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?
2-oxobutanoate + CoA + 2 oxidized cytochrome c
propanoyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
show the reaction diagram
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?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
show the reaction diagram
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enzyme Ape1473/1472, 97% of the activity compared to glyoxylate
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?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-oxoglutarate + CoA + 2 oxidized cytochrome c
succinyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
show the reaction diagram
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best substrate tested
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?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
2-oxoglutarate + CoA + 2 oxidized methyl viologen
succinyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472, 94% of the activity compared to glyoxylate
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-
?
4-hydroxyphenylpyruvate + CoA + 2 methyl viologen
(4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472, 16% of the activity compared to glyoxylate
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?
glyoxylate + CoA + 2 oxidized methyl viologen
formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472
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?
hydroxypyruvate + CoA + 2 methyl viologen
?
show the reaction diagram
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enzyme Ape1473/1472, 55% of the activity compared to glyoxylate
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?
phenylpyruvate + CoA + 2 methyl viologen
phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
pyruvate + CoA + 2 oxidized cytochrome c
acetyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
show the reaction diagram
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
show the reaction diagram
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enzyme Ape1473/1472, 95% of the activity compared to glyoxylate
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?
additional information
?
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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
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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?
additional information
?
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Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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enzyme contains a dicluster, [3Fe-4S][4Fe-4S], type ferredoxin of 11000 Da by SDS-PAGE and of 11180 Da by MALDI-TOF mass spectrometry
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iron-sulfur centre
P72578 and P72579
the enzyme contains one [4Fe-4S]2+,1+ cluster
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S center
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the enzyme has one [4Fe4S]2+ cluster, ligated by 4 Cys residues, C12, C15, C46, and C197. All four Cys are required to fold a [4Fe4S] cluster for oxidative decarboxylation of pyruvate including the formation of a stable hydroxyethyl-thiamine diphosphate radical
iron-sulfur centre
P72578 and P72579
the enzyme contains one [4Fe-4S]2+,1+ cluster
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-fluoro-7-nitrobenzofurazan
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0.001 mM inhibitor with 0.01 mM enzyme decreases the activity by about 20% and 0.003 mM inhibitor with 0.01 mM enzyme decreases the activity by around 50%. Inactivation is prevented by CoA
CoA
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substrate inhibition
KCl
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1020% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 4665% activation is reached, and further increased concentrations of KCl are inhibitory, enzyme Ape1473/1472
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.516
2-oxobutanoate
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pH 7.0, 55C
0.07 - 0.516
2-oxobutyrate
0.163 - 3.3
2-oxoglutarate
0.05 - 1.17
CoA
0.07
oxidized ferredoxin
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cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication; cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication
0.1 - 0.38
pyruvate
additional information
additional information
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kinetic parameters of mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
2-oxobutanoate
Sulfolobus solfataricus
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pH 7.0, 55C
1.55
2-oxobutyrate
Sulfolobus solfataricus
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pH 7.0, 55C
1.7 - 19
2-oxoglutarate
2.2 - 51
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
2-oxobutanoate
390
0.52 - 46.2
2-oxoglutarate
34
7.2 - 182
pyruvate
31
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52.6
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pH 7.0, 55C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
P72578 and P72579
assay at
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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pH 6.0: about 50% of maximal activity, pH 9.0: about 50% of maximal activity
7.5 - 10
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pH 7.5: about 70% of maximal activity, pH 10.0: about 70% of maximal activity, enzyme Ape1473/1472
8 - 9
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pH 8.0: 65% of maximal activity, pH 9.0: optimum, inactive below pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
P72578 and P72579
assay at
110
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enzyme Ape1473/1472
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 52
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the enzyme is twice as active at 52C as at 25C
90 - 110
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70C: 17% of maximal activity, 90C: about 40% of maximal activity, 110C: maximal activity, enzyme Ape1473/1472
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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gel filtration, enzyme Ape1473/1472
103000
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native PAGE
105000
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gel filtration
165000
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sedimentation velocity experiments
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
tetramer
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2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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pH 7.2, 30 min, about 20% loss of activity, natural and recombinant wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzymes requires high salt concentrations for stability. The half-life at 0.1 M KCl in 50 mM Tris/HC1 pH 8.0 is 3 h at 0C
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is stable against oxygen
P72578 and P72579
288435
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified enzyme can be stored after dialysis against 20 mM potassium phosphate buffer, pH 6.8
P72578 and P72579
20C, 4C or -80C, activity in cytosolic fraction is not very stable
P72578 and P72579
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme Ape1473/1472
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wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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P72578 and P72579
expression in Escherichia coli, enzyme Ape1473/1472
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expression in Escherichia coli, wild-type recombinant enzyme is indistinguishable from the natural one in every criterion investigated
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expression of mutant enzymes K125A and K173A in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I255L
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kcat/Km for pyruvate is 11% of wild-type value, kcat/KM for 2-oxoglutarate is 21% of wild-type value
I255M
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kcat/Km for pyruvate is 13% of wild-type value, kcat/KM for 2-oxoglutarate is 2% of wild-type value
I255S
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kcat/Km for pyruvate is 23% of wild-type value, kcat/KM for 2-oxoglutarate is 35% of wild-type value
I255V
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kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value
P254G
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kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value
P257A
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no enzyme activity at either 50 or 80C
P257G
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no enzyme activity at either 50 or 80C
P257V
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no enzyme activity at either 50 or 80C
T256A
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kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme; kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
T256S
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kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
T256V
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kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
Y253A
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no enzyme activity at either 50 or 80C
Y253F
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kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
Y253W
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no enzyme activity at either 50 or 80C
T256A
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kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme; kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
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T256S
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kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
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T256V
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kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
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Y253F
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kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
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C12/15A
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loss of ironsulfur cluster
C12A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C197A
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the enzyme retains an unidentified type of ironsulfur cluster
C46A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
K125A
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the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme
K173A
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the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme