Information on EC 1.2.7.8 - indolepyruvate ferredoxin oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.7.8
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RECOMMENDED NAME
GeneOntology No.
indolepyruvate ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+
show the reaction diagram
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phenylalanine metabolism
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tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
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).
CAS REGISTRY NUMBER
COMMENTARY hide
158886-06-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Marburg, DSM 2133
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Q6LZB6 and Q6LZB5, Q6M0F5 and Q6M0F6
Methanococcus maripaludis has two IOR homologs. A deletion mutant for one of these homologs contains76, 74, and 42% lower activity for phenylpyruvate, p-hydoxyphenylpyruvate, 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; Methanococcus maripaludis has two IOR homologs. A deletion mutant for one of these homologs contains76, 74, and 42% lower activity for phenylpyruvate, p-hydoxyphenylpyruvate, 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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
2-keto-4-methylthiobutyrate + CoA + oxidized ferredoxin
CO2 + reduced ferredoxin + 3-methylthiopropionyl-CoA
show the reaction diagram
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r
2-ketoisocaproate + CoA + oxidized ferredoxin
CO2 + reduced ferredoxin + isovaleryl-CoA
show the reaction diagram
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r
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
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?
4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
? + CO2 + reduced ferredoxin + H+
show the reaction diagram
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
show the reaction diagram
p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
phenylpyruvate + CoA + oxidized methyl viologen
phenylacetyl-CoA + CO2 + reduced methyl viologen + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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Km-value 0.06 mM
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[4Fe-4S]-center
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
(indol-3-yl)pyruvate
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in 50 mM TAPS buffer (pH 9.0), at 80C
0.13
4-hydroxyphenylpyruvate
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in 50 mM TAPS buffer (pH 9.0), at 80C; pH 9.0, 80C
0.015 - 0.021
CoA
0.048
Ferredoxin
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0.22 - 0.25
Indolepyruvate
0.06
oxidized ferredoxin
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in 50 mM TAPS buffer (pH 9.0), at 80C
0.11
p-hydroxyphenylpyruvate
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pH 8.4, 80C
0.018 - 1.4
phenylpyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.5
KCN
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pH 8.4, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.01
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cell-free extract, in 50 mM TAPS buffer (pH 9.0), at 80C
87
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74fold purified enzyme, purified by an effective affinity chromatography technique
121
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after 120fold purification, in 50 mM TAPS buffer (pH 9.0), at 80C; pH 9.0, 80C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10.5
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at 80C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
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exhibits optimal activity above at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 70C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
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2 * 67000 + 2 * 21000, SDS-PAGE; 2 * 67000, alpha-subunit, plus 2 * 21000, beta-subunit, SDS-PAGE
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
155000
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sedimentation equilibrium and sedimentation velocity experiments
170000
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gel filtration
180000
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gel filtration
192000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
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not active at pH 5.2 and pH 11.0
644700
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 110
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a slight decrease in activity is observed below 90C for at least 4 h. The enzyme exhibits a half-life of 62 min at 100C, 40 min at 103C, 20 min at 105C, 5 min at 108C, and less than 5 min at 110C
80
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virtually inactive at 25C, quite thermostable, with a half-life of activity at 80C of about 80 min under anaerobic conditions
100
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half-life 62 min
105
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half-life 20 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during a long complicated purification process, the enzyme loses much activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
25C, 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 23C
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644700
half-life in presence of air is 15 min at 25C
O07835 and O07836
644701
irreversibly inactivated by oxygen
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639362
the enzyme is oxygen-sensitive with a half-life of 7 h at 25C under aerobic conditions
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725574
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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; 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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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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)
O07835 and O07836
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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development of an effective affinity chromatography technique
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