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Information on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)
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EC Tree
1.2.7.11 2-oxoacid oxidoreductase (ferredoxin)IUBMB Comments
Contains thiamine diphosphate and [4Fe-4S] clusters . 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).
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Word Map
- 1.2.7.11
- sulfolobus
- ferredoxins
- 2-oxoacids
- thiamin
-
thermoacidophilic
- pyrophosphate
- archaeon
-
ofors
-
pyruvate:ferredoxin
- 2-oxoglutarate
- tpp
-
iron-sulfur
- oxalate
- tokodaii
- 2-oxobutyrate
- africanus
- halobium
-
halobacterium
-
2-oxoglutarate:ferredoxin
- analysis
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
+
+
2
=
+
+
2
+
2
Synonyms
2-oxoacid:ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductases, stofor, stofor2, ape1473/1472, stofor1, 2-oxoacid ferredoxin oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoacid: ferredoxin oxidoreductase
2-oxoacid:ferredoxin oxidoreductase
2-oxoacid:ferredoxin oxidoreductases
OFOR
OFOR1
OFOR2
PFOR
Saci_2306
Saci_2307
StOFOR1
StOFOR2
2-oxoacid:ferredoxin oxidoreductase
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-
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StOFOR1
StOFOR1 and StOFOR2 are paralogs, the 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1. A paralogous gene set (stk_24350/stk_24330) of the StOFOR1 genes (stk_23000/stk_22980) is present in the Sulfolobus tokodaii genome. STK_24350 (alpha-subunit) and STK_24330 (beta-subunit) have similar domain architectures to STK_23000 and STK_22980, with high amino acid sequence identity for both subunits (59% and 71%). 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1, and there is no evidence for the expression of the tk_24350/stk_24330 genes
StOFOR1
StOFOR1 and StOFOR2 are paralogs, the 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1. A paralogous gene set (stk_24350/stk_24330) of the StOFOR1 genes (stk_23000/stk_22980) is present in the Sulfolobus tokodaii genome. STK_24350 (alpha-subunit) and STK_24330 (beta-subunit) have similar domain architectures to STK_23000 and STK_22980, with high amino acid sequence identity for both subunits (59% and 71%). 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1, and there is no evidence for the expression of the tk_24350/stk_24330 genes
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StOFOR2
there is no evidence for the expression of the StOFOR2 (tk_24350/stk_24330 genes) in Sulfolobus tokodaii. Recombinant protein samples of STK_24350/STK_24330 are prepared and this enzyme is designated as StOFOR2. StOFOR1 and StOFOR2 are paralog. The 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1. A paralogous gene set (stk_24350/stk_24330) of the StOFOR1 genes (stk_23000/stk_22980) is present in the Sulfolobus tokodaii genome. STK_24350 (alpha-subunit) and STK_24330 (beta-subunit) have similar domain architectures to STK_23000 and STK_22980, with high amino acid sequence identity for both subunits (59% and 71%)
StOFOR2
there is no evidence for the expression of the StOFOR2 (tk_24350/stk_24330 genes) in Sulfolobus tokodaii. Recombinant protein samples of STK_24350/STK_24330 are prepared and this enzyme is designated as StOFOR2. StOFOR1 and StOFOR2 are paralog. The 2-oxoacid oxidoreductase activity in Sulfolobus tokodaii cells is mainly due to StOFOR1. A paralogous gene set (stk_24350/stk_24330) of the StOFOR1 genes (stk_23000/stk_22980) is present in the Sulfolobus tokodaii genome. STK_24350 (alpha-subunit) and STK_24330 (beta-subunit) have similar domain architectures to STK_23000 and STK_22980, with high amino acid sequence identity for both subunits (59% and 71%)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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PATHWAY SOURCE
PATHWAYS
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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).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methylthiobutyrate + CoA + 2 methyl viologen
3-methylthiopropanoyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 48% of the activity compared to glyoxylate
-
-
?
2-oxoadipate + CoA + 2 methyl viologen
glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 49% of the activity compared to glyoxylate
-
-
?
2-oxobutanoate + CoA + 2 oxidized cytochrome c
propanoyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
2-oxoglutarate + CoA + 2 oxidized cytochrome c
succinyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
best substrate tested
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized methyl viologen
succinyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
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enzyme Ape1473/1472, 94% of the activity compared to glyoxylate
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-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinoyl-CoA + CO2 + reduced methyl viologen
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen + H+
4-hydroxyphenylpyruvate + CoA + 2 methyl viologen
(4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 16% of the activity compared to glyoxylate
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-
?
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
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-
-
r
glyoxylate + CoA + 2 oxidized methyl viologen
formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
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enzyme Ape1473/1472
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-
?
hydroxypyruvate + CoA + 2 methyl viologen
?
-
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+
pyruvate + CoA + 2 oxidized cytochrome c
acetyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
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-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
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-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
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-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
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-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
enzyme Ape1473/1472, 97% of the activity compared to glyoxylate
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-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
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-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
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-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
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?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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kcat/Km for 2-oxobutyrate is 60% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
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-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
kcat/Km for 2-oxobutyrate is 60% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
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-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
specific activity under optimal conditions is 36% of the specific activity with 2-oxobutyrate
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxobutyrate is 12% of the kcat/Km-value for pyruvate, a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxoglutarate is 12% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxoglutarate is 12% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxobutyrate is 12% of the kcat/Km-value for pyruvate, a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
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-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. Because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. Because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
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-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinoyl-CoA + CO2 + reduced methyl viologen
-
-
-
r
2-oxoglutarate + CoA + oxidized methyl viologen
succinoyl-CoA + CO2 + reduced methyl viologen
-
-
-
r
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
?
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
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-
-
r
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
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-
-
r
phenylpyruvate + CoA + 2 methyl viologen
phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 24% of the activity compared to glyoxylate
-
-
?
phenylpyruvate + CoA + 2 methyl viologen
phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 36% of the activity compared to glyoxylate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
specific activity under optimal conditions is 65% of the specific activity with 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Vmax/Km is 1.9fold higher than that for 2-oxoglutarate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Vmax/Km is 1.9fold higher than that for 2-oxoglutarate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Lys125 in subunit b is the critical residue that interacts with CoA
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. The carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit of
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. The carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit of
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 95% of the activity compared to glyoxylate
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
?
-
-
-
?
additional information
?
-
-
Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix
-
-
?
additional information
?
-
-
no activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape1473/1472
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
-
no activity with glyoxylate
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
enzyme is able to use low-potential ferredoxins of the green sulfur bacterium Chlorobium tepidum and of Sulfolobus acidocaldarius whereas CO2 fixation is not supported by the native ferredoxin of Desulfocurvibacter africanus. Methyl viologen as an artificial electron carrier also allows CO2 fixation
-
-
-
additional information
?
-
enzyme is able to use low-potential ferredoxins of the green sulfur bacterium Chlorobium tepidum and of Sulfolobus acidocaldarius whereas CO2 fixation is not supported by the native ferredoxin of Desulfocurvibacter africanus. Methyl viologen as an artificial electron carrier also allows CO2 fixation
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-
-
additional information
?
-
-
the YPITP-motif is essential for the turnover of the reaction rather than the affinity toward 2-oxoacid
-
-
?
additional information
?
-
-
the YPITP-motif is essential for the turnover of the reaction rather than the affinity toward 2-oxoacid
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
additional information
?
-
-
Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
the enzyme contains one [4Fe-4S]2+,1+ cluster
Ferredoxin
-
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
-
Ferredoxin
alpha/beta-subunit heterodimers lack an intramolecular ferredoxin domain. Because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
thiamine diphosphate
-
intact enzyme molecule contains two molecules of thiamin diphosphate
thiamine diphosphate
the enzyme contains one thiamine diphosphate per alphabeta structure
thiamine diphosphate
alpha/beta-subunit heterodimers contain thiamin diphosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S center
-
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
iron-sulfur centre
the enzyme contains one [4Fe-4S]2+,1+ cluster
Mg2+
Iron
contains one [4Fe-4S]2+,1+ cluster per alpha/beta structure
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-fluoro-7-nitrobenzofurazan
-
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
KCl
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of mutant enzymes
-
0.07
2-oxobutyrate
-
pH and temperature not specified in the publication
0.87
2-oxoglutarate
pH and temperature not specified in the publication
1.1
2-oxoglutarate
-
pH and temperature not specified in the publication
2.1
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR1
2.1
2-oxoglutarate
wild type enzyme, at pH 8.5 and 80°C
2.3
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation T349L in alpha-subunit
2.3
2-oxoglutarate
mutant enzyme T349L, at pH 8.5 and 80°C
3.2
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation S41A in alpha-subunit
3.2
2-oxoglutarate
mutant enzyme S41A, at pH 8.5 and 80°C
15
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR2
15
2-oxoglutarate
wild type enzyme, at pH 8.5 and 80°C
0.07
oxidized ferredoxin
-
cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication
0.07
oxidized ferredoxin
-
cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication
0.13
pyruvate