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Information on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)
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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
- 2-oxoglutarate
-
pyruvate:ferredoxin
- tpp
-
iron-sulfur
- tokodaii
- oxalate
- 2-oxobutyrate
-
2-oxoglutarate:ferredoxin
- halobium
-
halobacterium
- africanus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
+
+
2
=
+
+
2
+
2
Synonyms
2-ketoacid:ferredoxin oxidoreductase, 2-oxoacid: ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductases, Ape1473/1472, KOR, OFOR, OFOR1, OFOR2, StOFOR, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoacid: ferredoxin oxidoreductase
2-oxoacid:ferredoxin oxidoreductase
2-oxoacid:ferredoxin oxidoreductases
OFOR
OFOR1
OFOR2
StOFOR1
StOFOR2
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
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+
-
enzyme Ape1473/1472, 94% of the activity compared to glyoxylate
-
-
?
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
-
-
?
glyoxylate + CoA + 2 oxidized methyl viologen
formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472
-
-
?
hydroxypyruvate + CoA + 2 methyl viologen
?
-
enzyme Ape1473/1472, 55% of the activity compared to glyoxylate
-
-
?
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+
-
-
-
-
?
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-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
enzyme Ape1473/1472, 97% of the activity compared to glyoxylate
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
?
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
-
-
?
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
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
?
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
-
-
?
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+
-
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+
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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+
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
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
?
-
-
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 [4Fe–4S]2+ cluster, ligated by 4 Cys residues, C12, C15, C46, and C197. All four Cys are required to fold a [4Fe–4S] 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
-
10–20% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 46–65% 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
0.25
pyruvate
pH and temperature not specified in the publication
0.32
pyruvate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR1
0.32
pyruvate
wild type enzyme, at pH 8.5 and 80°C
0.49
pyruvate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation S41A in alpha-subunit
0.49
pyruvate
mutant enzyme S41A, at pH 8.5 and 80°C
0.51
pyruvate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation T349L in alpha-subunit
0.51
pyruvate
mutant enzyme T349L, at pH 8.5 and 80°C
0.91
pyruvate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation K49I in alpha-subunit
0.91
pyruvate
mutant enzyme K49I, at pH 8.5 and 80°C
1.6
pyruvate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 50% of maximal activity, pH 9.0: about 50% of maximal activity
7.5 - 10
-
pH 7.5: about 70% of maximal activity, pH 10.0: about 70% of maximal activity, enzyme Ape1473/1472
8 - 9
-
pH 8.0: 65% of maximal activity, pH 9.0: optimum, inactive below pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90 - 110
-
70°C: 17% of maximal activity, 90°C: about 40% of maximal activity, 110°C: maximal activity, enzyme Ape1473/1472
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P72578: alpha-subunit, and P72579: beta-subunit
UniProt
brenda
Q96XT2: alpha-subunit (ST2435), Q96XT4: beta-subunit (ST2433); 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
UniProt
brenda
Q96Y66: alpha-subunit (ST2300), Q96Y68: beta-subunit (ST2298)
UniProt
brenda
Q96XT2: alpha-subunit (ST2435), Q96XT4: beta-subunit (ST2433); 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
UniProt
brenda
Q96Y66: alpha-subunit (ST2300), Q96Y68: beta-subunit (ST2298)
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
can utilize both pyruvate and 2-oxoglutarate, playing a key role in the central metabolism
metabolism
there is no evidence for the expression of the StOFOR2 (tk_24350/stk_24330 genes) in Sulfolobus tokodaii. It may be expressed in vivo under some culture conditions
metabolism
-
there is no evidence for the expression of the StOFOR2 (tk_24350/stk_24330 genes) in Sulfolobus tokodaii. It may be expressed in vivo under some culture conditions
metabolism
-
can utilize both pyruvate and 2-oxoglutarate, playing a key role in the central metabolism
Show AA Sequence and Transmembrane Helices (2180 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
34410
-
1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472
67405
-
1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472
69000
70000
34000
-
1 * 69000 (alpha-subunit) + 1 * 34000 (beta-subunit), SDS-PAGE, MALDI-TOF mass spectrometry
34000
-
1 * 69000, alpha-subuit, + 1 * 34000, beta-subunit, SDS-PAGE and MALDI-TOF
69000
-
1 * 69000 (alpha-subunit) + 1 * 34000 (beta-subunit), SDS-PAGE, MALDI-TOF mass spectrometry
69000
-
1 * 69000, alpha-subuit, + 1 * 34000, beta-subunit, SDS-PAGE and MALDI-TOF
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
dimer
-
1 * 69000, alpha-subuit, + 1 * 34000, beta-subunit, SDS-PAGE and MALDI-TOF
dimer
-
1 * 69000, alpha-subuit, + 1 * 34000, beta-subunit, SDS-PAGE and MALDI-TOF
dimer
-
1 * 69000, alpha-subuit, + 1 * 34000, beta-subunit, SDS-PAGE and MALDI-TOF
heterodimer
-
1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472
heterodimer
-
1 * 69000 (alpha-subunit) + 1 * 34000 (beta-subunit), SDS-PAGE, MALDI-TOF mass spectrometry
heterodimer
-
1 * 69000 (alpha-subunit) + 1 * 34000 (beta-subunit), SDS-PAGE, MALDI-TOF mass spectrometry
heterodimer
-
1 * 69000 (alpha-subunit) + 1 * 34000 (beta-subunit), SDS-PAGE, MALDI-TOF mass spectrometry
heterodimer
crystals consist of two protomers (1 and 2), each of which consists of one heterodimer of alpha- and beta-subunits
heterodimer
1 * 70000 + 1 * 34000, SDS-PAGE
heterodimer
-
crystals consist of two protomers (1 and 2), each of which consists of one heterodimer of alpha- and beta-subunits
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown at 20°C using sitting drop vapor diffusion. The structure of the recombinant enzyme StOFOR2 by the single-wavelength anomalous dispersion method is solved using a selenomethionine(SeMet)-labeled protein crystal, and the structures of the ligand-free (2.1 Å resolution) and pyruvate-complexed (2.2 Å) forms are determined. In the structure of the recombinant enzyme StOFOR2 in unreacted pyruvate complex form, the carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit. The binding pockets of the 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii surrounding the methyl or propyl group of the ligands are wider than that of 2-oxoacid oxidoreductase enzymes from Desulfovbrio africanus. A possible complex structural model is constructed by placing a Zn2+-containing dicluster ferredoxin of Sulfolobus tokodaii into the large pocket of the recombinant StOFOR2 enzyme, providing insight into the electron transfer between the two redox proteins
crystals of the StOFOR1 enzyme are prepared by co-crystallization with 50 mM 2-oxobutyrate and 1 mM CoA. Crystals are grown at 25°C using sitting drop vapor diffusion. In the structure of StOFOR1 co-crystallized with 2-oxobutyrate, electron density corresponding to a 1-hydroxypropyl group (post-decarboxylation state) is observed at the thiazole ring of thiamine diphosphate. The binding pockets of the 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii surrounding the methyl or propyl group of the ligands are wider than that of 2-oxoacid oxidoreductase enzymes from Desulfovbrio africanus
sitting drop vapor diffusion method, using 0.7 M ammonium tartrate dibasic and 0.1 M Tris-HCl (pH 8.5)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I255L
-
kcat/Km for pyruvate is 11% of wild-type value, kcat/KM for 2-oxoglutarate is 21% of wild-type value
I255M
-
kcat/Km for pyruvate is 13% of wild-type value, kcat/KM for 2-oxoglutarate is 2% of wild-type value
I255S
-
kcat/Km for pyruvate is 23% of wild-type value, kcat/KM for 2-oxoglutarate is 35% of wild-type value
I255V
-
kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value
P254G
-
kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value
T256A
T256S
-
kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
T256V
-
kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
Y253F
-
kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
T256A
T256S
-
kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
T256V
-
kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
Y253F
-
kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
C12A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C197A
-
the enzyme retains an unidentified type of iron–sulfur cluster
C46A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
D468A
K125A
-
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
-
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
K49I
S41A
T349L
S41A
-
the mutant shows reduced activity compared to the wild type enzyme
T349L
-
the mutant shows reduced activity compared to the wild type enzyme
D468A
-
mutant enzyme StOFOR1 with mutation D468A in alpha-subunit. Vmax with pyruvate as substrate is 1.3% compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
K49I
-
mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
S41A
-
mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme
T349L
-
mutant enzyme StOFOR1 with mutation T349L in alpha-subunit. Vmax with pyruvate as substrate is 43% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 74% compared to wild-type enzyme, Km with pyruvate as substrate is 1.6fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.1fold higher as compared to wild-type enzyme
T256A
-
kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme
T256A
-
kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
T256A
-
kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme
T256A
-
kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
D468A
mutant enzyme StOFOR1 with mutation D468A in alpha-subunit. Vmax with pyruvate as substrate is 1.3% compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
D468A
inactive with 2-oxoglutarate and pyruvate as substrate
K49I
mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
K49I
inactive with 2-oxoglutarate as substrate
S41A
the mutant shows reduced activity compared to the wild type enzyme
S41A
mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme
T349L
the mutant shows reduced activity compared to the wild type enzyme
T349L
mutant enzyme StOFOR1 with mutation T349L in alpha-subunit. Vmax with pyruvate as substrate is 43% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 74% compared to wild-type enzyme, Km with pyruvate as substrate is 1.6fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.1fold higher as compared to wild-type enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
pH 7.2, 30 min, about 20% loss of activity, natural and recombinant wild-type enzyme
80
80
-
pH 7.2, 30 min, about 40% loss of activity, natural and recombinant wild-type enzyme
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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 0°C
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme can be stored after dialysis against 20 mM potassium phosphate buffer, pH 6.8
20°C, 4°C or -80°C, activity in cytosolic fraction is not very stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43 (DE3) cells
expression in Escherichia coli (DE3)
expression in Escherichia coli, wild-type recombinant enzyme is indistinguishable from the natural one in every criterion investigated
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kerscher, L.; Oesterhelt, D.
Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium
Eur. J. Biochem.
116
587-594
1981
Halobacterium salinarum
brenda
Zhang, Q.; Iwaaki, T.; Wakagi, T.; Oshima, T.
2-Oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7
J. Biochem.
120
587-599
1996
Sulfolobus sp. (P72578 and P72579), Sulfolobus sp., Sulfolobus sp. 7 (P72578 and P72579)
brenda
Fukuda, E.; Wakagi, T.
Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7
Biochim. Biophys. Acta
1597
74-80
2002
Sulfolobus sp., Sulfolobus sp. 7
brenda
Nishizawa, Y.; Yabuki, T.; Fukuda, E.; Wakagi, T.
Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1
FEBS Lett.
579
2319-2322
2005
Aeropyrum pernix
brenda
Park, Y.J.; Yoo, C.B.; Choi, S.Y.; Lee, H.B.
Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1
J. Biochem. Mol. Biol.
39
46-54
2006
Saccharolobus solfataricus, Saccharolobus solfataricus P1, Saccharolobus solfataricus DSM 1616
brenda
Luo, J.; Fukuda, E.; Takase, H.; Fushinobu, S.; Shoun, H.; Wakagi, T.
Identification of the lysine residue responsible for coenzyme A binding in the heterodimeric 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus tokodaii, a thermoacidophilic archaeon, using 4-fluoro-7-nitrobenzofurazan as an affinity label
Biochim. Biophys. Acta
1794
335-340
2009
Sulfurisphaera tokodaii
brenda
Fukuda, E.; Kino, H.; Matsuzawa, H.; Wakagi, T.
Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes
Eur. J. Biochem.
268
5639-5646
2001
Sulfolobus sp., Sulfolobus sp. 7
brenda
Yan, Z.; Fushinobu, S.; Wakagi, T.
Four Cys residues in heterodimeric 2-oxoacid:ferredoxin oxidoreductase are required for CoA-dependent oxidative decarboxylation but not for a non-oxidative decarboxylation
Biochim. Biophys. Acta
1844
736-743
2014
Sulfurisphaera tokodaii
brenda
Iwasaki, T.; Wakagi, T.; Oshima, T.
Ferredoxin-dependent redox system of a thermoacidophilic archaeon, Sulfolobus sp. strain 7. Purification and characterization of a novel reduced ferredoxin-reoxidizing iron-sulfur flavoprotein
J. Biol. Chem.
270
17878-17883
1995
Sulfolobus sp., Sulfolobus sp. 7
brenda
Iwasaki, T.; Oshima, T.
Ferredoxin and related enzymes from Sulfolobus
Methods Enzymol.
334
3-22
2001
Sulfolobus sp. (P72578 and P72579), Sulfolobus sp. 7 (P72578 and P72579)
brenda
Yan, Z.; Maruyama, A.; Arakawa, T.; Fushinobu, S.; Wakagi, T.
Crystal structures of archaeal 2-oxoacid:ferredoxin oxidoreductases from Sulfolobus tokodaii
Sci. Rep.
6
33061
2016
Sulfurisphaera tokodaii (Q96XT2 and Q96XT4), Sulfurisphaera tokodaii (Q96XT4), Sulfurisphaera tokodaii (Q96Y66 and Q96Y68), Sulfurisphaera tokodaii (Q96Y68), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q96XT4), Sulfurisphaera tokodaii 7 (Q96Y68), Sulfurisphaera tokodaii DSM 16993 (Q96XT2 and Q96XT4), Sulfurisphaera tokodaii DSM 16993 (Q96Y66 and Q96Y68)
brenda
Gibson, M.I.; Chen, P.Y.; Drennan, C.L.
A structural phylogeny for understanding 2-oxoacid oxidoreductase function
Curr. Opin. Struct. Biol.
41
54-61
2016
Desulfocurvibacter africanus, Saccharolobus solfataricus
brenda
Li, B.; Elliott, S.
The catalytic bias of 2-oxoacid: ferredoxin oxidoreductase in CO2: evolution and reduction through a ferredoxin-mediated electrocatalytic assay
Electrochim. Acta
199
349-356
2016
Desulfocurvibacter africanus, Hydrogenobacter thermophilus
-
brenda
Yokooji, Y.; Sato, T.; Fujiwara, S.; Imanaka, T.; Atomi, H.
Genetic examination of initial amino acid oxidation and glutamate catabolism in the hyperthermophilic archaeon Thermococcus kodakarensis
J. Bacteriol.
195
1940-1948
2013
Thermococcus kodakarensis
brenda
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