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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-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
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-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
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 ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
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
-
-
?
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
-
-
-
r
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 ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + oxidized methyl viologen
?
additional information
?
-
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
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
-
-
-
r
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
-
-
-
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
?
-
-
-
?
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
?
-
-
no activity with glyoxylate
-
-
?
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
?
-
-
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 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
-
-
-
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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0.516
2-oxobutanoate
-
pH 7.0, 55°C
0.07 - 0.516
2-oxobutyrate
0.163 - 15
2-oxoglutarate
additional information
additional information
-
kinetic parameters of mutant enzymes
-
0.07
2-oxobutyrate
-
pH and temperature not specified in the publication
0.45
2-oxobutyrate
-
pH 7.5, 80°C, recombinant wild-type enzyme
0.48
2-oxobutyrate
-
pH 7.5, 80°C, natural enzyme
0.516
2-oxobutyrate
-
pH 7.0, 55°C
0.163
2-oxoglutarate
-
pH 7.0, 55°C
0.33
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256V
0.37
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256A
0.5
2-oxoglutarate
-
pH 8.5, 80°C, enzyme Ape1473/1472
0.72
2-oxoglutarate
-
pH 7.5, 80°C, recombinant enzyme
0.85
2-oxoglutarate
-
pH 7.5, 80°C, natural enzyme
0.85
2-oxoglutarate
-
pH 7.5, 80°C, recombinant wild-type enzyme
0.87
2-oxoglutarate
pH 6.8, 50°C
0.87
2-oxoglutarate
pH and temperature not specified in the publication
0.87
2-oxoglutarate
-
pH 7.5, 80°C, natural enzyme
0.89
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255S
1.1
2-oxoglutarate
-
pH and temperature not specified in the publication
1.1
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255L
1.2
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme P254G
1.3
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255M
1.5
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme P253F
2.1
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256S
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
3.3
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255V
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
0.05
CoA
-
pH 8.5, 80°C, mutant enzyme K173A
0.074
CoA
-
pH 8.5, 80°C, wild-type enzyme
1.17
CoA
-
pH 8.5, 80°C, mutant enzyme K125A
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
0.1
pyruvate
-
pH and temperature not specified in the publication
0.11
pyruvate
-
pH 7.5, 80°C, mutant enzyme T256S
0.13
pyruvate
-
pH 7.5, 80°C, mutant enzyme I255S
0.14
pyruvate
-
pH 7.5, 80°C, mutant enzyme T256A
0.17
pyruvate
-
pH 7.5, 80°C, mutant enzyme P254G
0.17
pyruvate
-
pH 7.5, 80°C, mutant enzyme T256V
0.19
pyruvate
-
pH 7.5, 80°C, mutant enzyme I255M
0.25
pyruvate
pH 6.8, 50°C
0.25
pyruvate
pH and temperature not specified in the publication
0.25
pyruvate
-
pH 7.5, 80°C, mutant enzyme I255V
0.275
pyruvate
-
pH 7.0, 55°C
0.28
pyruvate
-
pH 7.5, 80°C, mutant enzyme I255L
0.28
pyruvate
-
pH 7.5, 80°C, natural and recombinant wild-type enzyme
0.28
pyruvate
-
pH 7.5, 80°C, naturale enzyme
0.31
pyruvate
-
pH 7.5, 80°C, mutant enzyme P253F
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
0.33
pyruvate
-
pH 7.5, 80°C, recombinant enzyme
0.38
pyruvate
-
pH 8.5, 80°C, enzyme Ape1473/1472
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
1.6
pyruvate
wild type enzyme, at pH 8.5 and 80°C
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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
P257A
-
no enzyme activity at either 50 or 80°C
P257G
-
no enzyme activity at either 50 or 80°C
P257V
-
no enzyme activity at either 50 or 80°C
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
Y253A
-
no enzyme activity at either 50 or 80°C
Y253F
-
kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
Y253W
-
no enzyme activity at either 50 or 80°C
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
-
C12/15A
-
loss of ironsulfur cluster
C12A
-
loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
-
loss of ironsulfur 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 ironsulfur cluster
C46A
-
loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
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
D468A
-
inactive with 2-oxoglutarate and pyruvate as substrate
-
K49I
-
inactive with 2-oxoglutarate as substrate
-
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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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
Witt, A.; Pozzi, R.; Diesch, S.; Haedicke, O.; Grammel, H.
New light on ancient enzymes - in vitro CO2 fixation by pyruvate synthase of Desulfovibrio africanus and Sulfolobus acidocaldarius
FEBS J.
286
4494-4508
2019
Sulfolobus acidocaldarius (Q4J6I9 and Q4J6I8), Sulfolobus acidocaldarius DSM 639 (Q4J6I9 and Q4J6I8)
brenda