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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
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 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

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

?
-
-
-
?
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
?
-
-
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 ironâsulfur cluster
C12A
-
loss of ironâsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
-
loss of ironâsulfur 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 ironâsulfur cluster
C46A
-
loss of ironâsulfur 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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