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EC Tree
IUBMB Comments Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, 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 examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
indolepyruvate ferredoxin oxidoreductase, phenylpyruvate oxidase,
more
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3-(indol-3-yl)pyruvate synthase (ferredoxin)
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arylpyruvate-ferredoxin oxidoreductase
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hydroxyphenylpyruvate oxidase
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indolepyruvate oxidase
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indolepyruvate-ferredoxin oxidoreductase
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indolepyruvate:Fd oxidoreductase
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phenylpyruvate oxidase
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IOR
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IOR
Methanococcus maripaludis has two IOR homologs
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(indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
this enzyme, which is found in archaea, is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see aslo EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7., 2-oxoisovalerate ferredoxin reductase and EC 1.2.7.9, 2-oxoglutarate ferredoxin oxidoreductase). Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates
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oxidative decarboxylation
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3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)
Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, 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 examples of other members of this family, 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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(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
2-keto-4-methylthiobutyrate + CoA + oxidized ferredoxin
CO2 + reduced ferredoxin + 3-methylthiopropionyl-CoA
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r
2-ketoisocaproate + CoA + oxidized ferredoxin
CO2 + reduced ferredoxin + isovaleryl-CoA
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r
3-methyl-2-oxobutanoate + H2O + oxidized methyl viologen
S-(2-methylpropanoyl)-CoA + reduced methyl viologen + H+
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?
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin + H+
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?
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
? + CO2 + reduced ferredoxin + H+
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
phenylpyruvate + CoA + oxidized methyl viologen
phenylacetyl-CoA + CO2 + reduced methyl viologen + H+
additional information
?
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(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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biosynthesis of amino acids from fatty acids
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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involved in peptide fermentation and metabolism of aromatic amino acids
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
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?
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
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?
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
? + CO2 + reduced ferredoxin + H+
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?
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
? + CO2 + reduced ferredoxin + H+
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?
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
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?
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
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?
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
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?
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
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?
p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
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r
p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
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r
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
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r
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
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r
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
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r
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
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?
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
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?
phenylpyruvate + CoA + oxidized methyl viologen
phenylacetyl-CoA + CO2 + reduced methyl viologen + H+
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?
phenylpyruvate + CoA + oxidized methyl viologen
phenylacetyl-CoA + CO2 + reduced methyl viologen + H+
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?
additional information
?
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pyruvate and transaminated forms of the amino acids aspartate, valine, glutamate and alanine, 2-ketobutyrate, oxalacetate, 2-ketoisovalerate, 2-ketoglutarate, 2-ketomalonate and phenylglyoxylate are not oxidized
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?
additional information
?
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pyruvate, 2-ketoisovalerate, 2-ketoglutarate, 2 ketobutyrate, and phenylglyoxylate are no substrates
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?
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(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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biosynthesis of amino acids from fatty acids
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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involved in peptide fermentation and metabolism of aromatic amino acids
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
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r
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
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?
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
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?
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Ferredoxin
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Km-value 0.06 mM
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additional information
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not inhibited by CO, unaffected by sodium nitrite, not inhibited by sodium fluoride or sodium azide, sodium benzoate, phenylacetate, pyruvate, 2-ketoglutarate and oxamate have no effect on activity
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thiamine diphosphate
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thiamine diphosphate
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activity increases about 8fold, Km for thiamine diphosphate 0.004 mM
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0.22
(indol-3-yl)pyruvate
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in 50 mM TAPS buffer (pH 9.0), at 80°C
0.13
4-hydroxyphenylpyruvate
0.22 - 0.25
Indolepyruvate
0.048 - 0.06
oxidized ferredoxin
0.11
p-hydroxyphenylpyruvate
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pH 8.4, 80°C
0.018 - 1.4
phenylpyruvate
0.13
4-hydroxyphenylpyruvate
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pH 9.0, 80°C
0.13
4-hydroxyphenylpyruvate
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in 50 mM TAPS buffer (pH 9.0), at 80°C
0.015
CoA
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pH 9.0, 80°C
0.017
CoA
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pH 8.4, 80°C, substrate indolepyruvate
0.02
CoA
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pH 8.0, 65°C, substrate phenylpyruvate, benzyl viologen as electron acceptor
0.021
CoA
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pH 8.4, 80°C, substrate phenylpyruvate
0.22
Indolepyruvate
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pH 9.0, 80°C
0.25
Indolepyruvate
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pH 8.4, 80°C
0.048
oxidized ferredoxin
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pH 8.4, 80°C
0.06
oxidized ferredoxin
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in 50 mM TAPS buffer (pH 9.0), at 80°C
0.018
phenylpyruvate
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in 50 mM TAPS buffer (pH 9.0), at 80°C
0.095
phenylpyruvate
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pH 8.4, 80°C
0.108
phenylpyruvate
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pH 9.0, 80°C
1.4
phenylpyruvate
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pH 8.0, 65°C
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1.01
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cell-free extract, in 50 mM TAPS buffer (pH 9.0), at 80°C
87
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74fold purified enzyme, purified by an effective affinity chromatography technique
121
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pH 9.0, 80°C
121
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after 120fold purification, in 50 mM TAPS buffer (pH 9.0), at 80°C
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90
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exhibits optimal activity above at pH 8.0
70
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80
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20 - 30
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negligible activity
60 - 100
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dramatic increase of activity
70 - 90
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shows dramatic increase in activity above 70°C
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brenda
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brenda
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brenda
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brenda
Q6LZB6: subunit alpha 2, Q6LZB5: subunit beta 2
SwissProt
brenda
Q6M0F5: subunit alpha 1, Q6M0F6: subunit beta 1
SwissProt
brenda
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brenda
DSM 3638
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brenda
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brenda
KOD1
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brenda
KOD1, 2.7 kB DNA fragment containing ior genes, DNA sequence
UniProt
brenda
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brenda
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malfunction
Methanococcus maripaludis has two IOR homologs. A deletion mutant for one of these homologs contains 76, 74, and 42% lower activity for phenylpyruvate, p-hydroxyphenylpyruvate, and indolepyruvate oxidation, respectively, than the wild type. Growth of this mutant in minimal medium is inhibited by the aryl acids, but the aromatic amino aciuds partially restore growth
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155000
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sedimentation equilibrium and sedimentation velocity experiments
24000
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2 * 71000 + 2 * 24000, alpha2,beta2, SDS-PAGE
66000
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2 * 66000 + 2 * 23000, alpha2,beta2, SDS-PAGE
71000
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2 * 71000 + 2 * 24000, alpha2,beta2, SDS-PAGE
21000
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2 * 67000 + 2 * 21000, SDS-PAGE
21000
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2 * 67000, alpha-subunit, plus 2 * 21000, beta-subunit, SDS-PAGE
23000
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2 * 66000 + 2 * 23000, alpha2,beta2, SDS-PAGE
23000
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2 * 67000 + 2 * 23000, alpha2,beta2, SDS-PAGE
67000
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2 * 67000 + 2 * 23000, alpha2,beta2, SDS-PAGE
67000
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2 * 67000 + 2 * 21000, SDS-PAGE
67000
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2 * 67000, alpha-subunit, plus 2 * 21000, beta-subunit, SDS-PAGE
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heterotetramer
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2 * 67000 + 2 * 21000, SDS-PAGE
heterotetramer
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2 * 67000 + 2 * 21000, SDS-PAGE
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tetramer
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tetramer
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2 * 67000 + 2 * 23000, alpha2,beta2, SDS-PAGE
tetramer
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2 * 67000 + 2 * 23000, alpha2,beta2, SDS-PAGE
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tetramer
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2 * 66000 + 2 * 23000, alpha2,beta2, SDS-PAGE
tetramer
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2 * 71000 + 2 * 24000, alpha2,beta2, SDS-PAGE
tetramer
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2 * 67000, alpha-subunit, plus 2 * 21000, beta-subunit, SDS-PAGE
tetramer
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2 * 67000, alpha-subunit, plus 2 * 21000, beta-subunit, SDS-PAGE
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8 - 10
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not active at pH 5.2 and pH 11.0
644700
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60 - 110
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a slight decrease in activity is observed below 90°C for at least 4 h. The enzyme exhibits a half-life of 62 min at 100°C, 40 min at 103°C, 20 min at 105°C, 5 min at 108°C, and less than 5 min at 110°C
80
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virtually inactive at 25°C, quite thermostable, with a half-life of activity at 80°C of about 80 min under anaerobic conditions
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during a long complicated purification process, the enzyme loses much activity
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25°C, aerobic conditions, half-life 7 h
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725574
enzyme is sensitive to inactivation by O2, losing 50% of its activity after exposure to air for 20 min at 23°C
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644700
half-life in presence of air is 15 min at 25°C
644701
irreversibly inactivated by oxygen
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639362
the enzyme is oxygen-sensitive with a half-life of 7 h at 25°C under aerobic conditions
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725574
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by affinity chromatography, 74fold
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purification under extremely anaerobic conditions in presence of 2mM dithiothreitol and 2mM sodium dithionite to protect against oxygen attack, and also 1mM MgSO4,1mM thiamine diphosphate and 0.2M NaCl, additives which have been found to stabilize
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under extremely anaerobic conditions with all buffers containing 2 mM dithiothreitol and 2 mM dithiothreitol. Q Sepharose column chromatography, hydroxyapatite column chromatography, Blue Sepharose column chromatography, and Superdex 200 gel filtration
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gene cloning and sequence analysis of the IOR gene, 2 genes iorA and iorB, encoding alpha and beta subunits are tandemly arranged, KOD1-IOR overproduced in anaerobically incubated Escherichia coli BL21(DE3)
gene cloning and sequence analysis of the IOR gene, 2 genes iorA and iorB, encoding alpha and beta subunits are tandemly arranged, KOD1-IOR overproduced in anaerobically incubated Escherichia coli BL21(DE3)
gene cloning and sequence analysis of the IOR gene, 2 genes iorA and iorB, encoding alpha and beta subunits are tandemly arranged, KOD1-IOR overproduced in anaerobically incubated Escherichia coli BL21(DE3)
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activity decreases significantly when the organism is grown on maltose plus S(0)
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analysis
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development of an effective affinity chromatography technique
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Schut, G.J.; Menon, A.L.; Adams, M.W.W.
2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis
Methods Enzymol.
331
144-158
2001
Methanothermobacter thermautotrophicus, Pyrococcus furiosus
brenda
Tersteegen, A.; Linder, D.; Thauer, R.K.; Hedderich, R.
Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum
Eur. J. Biochem.
244
862-868
1997
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Mai, X.; Adams, M.W.
Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A new enzyme involved in peptide fermentation
J. Biol. Chem.
269
16726-16732
1994
Pyrococcus furiosus
brenda
Siddiqui, M.A.; Fujiwara, S.; Imanaka, T.
Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1 possesses a mosaic structure showing features of various oxidoreductases
Mol. Gen. Genet.
254
433-439
1997
Thermococcus kodakarensis, Thermococcus kodakarensis (O07835 and O07836)
brenda
Siddiqui, M.A.; Fujiwara, S.; Takagi, M.; Imanaka, T.
In vitro heat effect on heterooligomeric subunit assembly of thermostable indolepyruvate ferredoxin oxidoreductase
FEBS Lett.
434
372-376
1998
Pyrococcus furiosus, Thermococcus kodakarensis
brenda
Siddiqui, M.A.; Imai, T.
Purification of an anaerobic oxidoreductase from the hyperthermophilic archaeon by affinity chromatography
J. Chem. Soc. Pak.
29
390-393
2007
Thermococcus profundus
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brenda
Ozawa, Y.; Siddiqui, M.A.; Takahashi, Y.; Urushiyama, A.; Ohmori, D.; Yamakura, F.; Arisaka, F.; Imai, T.
Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron-sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus
J. Biosci. Bioeng.
114
23-27
2012
Thermococcus profundus, Thermococcus profundus DSM DT5432
brenda
Porat, I.; Waters, B.W.; Teng, Q.; Whitman, W.B.
Two biosynthetic pathways for aromatic amino acids in the archaeon Methanococcus maripaludis
J. Bacteriol.
186
4940-4950
2004
Methanococcus maripaludis (Q6LZB6 and Q6LZB5), Methanococcus maripaludis (Q6M0F5 and Q6M0F6)
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus
brenda
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