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Information on EC 1.2.7.1 - pyruvate synthase
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EC Tree
1.2.7.1 pyruvate synthaseIUBMB Comments
Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. 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 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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Word Map
- 1.2.7.1
- ferredoxins
- acetyl-coa
- clostridium
- hydrogenase
- metronidazole
- hydrogenosomal
- trichomonas
- vaginalis
- thiamin
- histolytica
- entamoeba
- giardia
- desulfovibrio
- pasteurianum
-
low-potential
- duodenalis
-
trichomoniasis
- 2-oxoacids
- flavodoxins
-
adp-forming
- nitazoxanide
- formate-lyase
-
wood-ljungdahl
-
2-oxoacid:ferredoxin
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5-nitroimidazole
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acetogenic
-
metronidazole-resistant
- africanus
-
tritrichomonas
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hydrogen-producing
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foramen
-
amitochondriate
- synthesis
-
ferredoxin-type
- indolepyruvate
- biofuel production
- analysis
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
pyruvate:ferredoxin oxidoreductase, pyruvate ferredoxin oxidoreductase, pyruvate-ferredoxin oxidoreductase, pyruvate synthase, pfo a, ap120, pfora, pfor1, nifj1, pyruvate:ferredoxin oxidoreductase a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketobutyrate synthase
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-
-
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2-oxobutyrate-ferredoxin oxidoreductase
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-
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-
alpha-ketobutyrate synthase
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-
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alpha-ketobutyrate-ferredoxin oxidoreductase
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bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
EC 1.2.7.2
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-
formerly
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PFO
PFOR
PforA
PFR
PFR1
POR
PorEDABG
pyruvate ferredoxin oxidoreductase
pyruvate-ferredoxin oxidoreductase
pyruvate:ferredoxin oxidoreductase
synthase, 2-oxobutyrate
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-
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Tsac_0046
TTE0445
bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
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bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
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POR
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bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate
pyruvate:ferredoxin oxidoreductase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyruvate + CoA + oxidized ferredoxin = acetyl-CoA + CO2 + reduced ferredoxin + 2 H+
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PATHWAY SOURCE
PATHWAYS
KEGG
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Citrate cycle (TCA cycle), Citrate cycle (TCA cycle), Glycolysis / Gluconeogenesis, Glycolysis / Gluconeogenesis, Glycolysis / Gluconeogenesis, Glycolysis / Gluconeogenesis, Glycolysis / Gluconeogenesis, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, purine metabolism, Pyruvate metabolism, Pyruvate metabolism, Pyruvate metabolism, Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. 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 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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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-methyl-thio-butyrate + CoA + 2 methyl viologen
?
enzyme Ape2126/2128, 37% of the activity compared to pyruvate
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-
?
2-oxoadipate + CoA + 2 methyl viologen
?
enzyme Ape2126/2128, 37% of the activity compared to pyruvate
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-
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
enzyme Ape2126/2128, 98% of the activity compared to pyruvate
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
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-
-
r
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
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-
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r
glyoxylate + CoA + 2 oxidized methyl viologen
?
enzyme Ape2126/2128, 89% of the activity compared to pyruvate
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?
hydroxypyruvate + CoA + 2 methyl viologen
?
enzyme Ape2126/2128, 38% of the activity compared to pyruvate
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-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen
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-
-
-
?
pyruvate + CoA + oxidized nitro blue tetrazolium
acetyl-CoA + CO2 + reduced nitro blue tetrazolium + H+
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-
-
-
?
pyruvate + H2O + oxidized methyl viologen
acetyl-CoA + reduced methyl viologen + H+
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-
-
-
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
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-
-
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
coenzyme F420 is not reduced by the purified enzyme
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-
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
coenzyme F420 is not reduced by the purified enzyme
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-
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
-
the enzyme reacts with oxaloacetate at 4.8 activity relative to the activity against pyruvate
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
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the enzyme reacts with oxaloacetate at 4.8 activity relative to the activity against pyruvate
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
Hydrogenobacter thermophilus TK-6 / IAM 12695
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the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
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-
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
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-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
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-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
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?
oxaloacetate + CoA + oxidized methyl viologen
?
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the enzyme reacts with oxaloacetate at 40% activity relative to the activity against pyruvate
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?
oxaloacetate + CoA + oxidized methyl viologen
?
-
the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
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?
oxaloacetate + CoA + oxidized methyl viologen
?
Hydrogenobacter thermophilus TK-6 / IAM 12695
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the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate
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?
oxaloacetate + CoA + oxidized methyl viologen
?
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
?
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
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?
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
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-
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?
pyruvate + CoA + 2 oxidized benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
coenzyme F420 is not reduced by the purified enzyme
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?
pyruvate + CoA + 2 oxidized benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
coenzyme F420 is not reduced by the purified enzyme
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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-
-
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
no activity with NAD+ or NADP+ as electron aceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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-
-
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
no activity with NAD+ or NADP+ as electron aceptor
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
ferredoxin is an electron donor for the enzyme reaction in vivo
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
ferredoxin is an electron donor for the enzyme reaction in vivo
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
first enzyme of pyruvate catabolism
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
ferredoxin from Clostridium pasteurianum
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the enzyme is involved in catabolism of pyruvate
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the deazaflavin, coenzyme F420, which has been proposed to be the physiological electron acceptor of pyruvate oxidoreductase in methanogens, is not reduced by the purified enzyme. In addition to ferredoxin and viologen dyes, flavin nucleotides serve as electron acceptors
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
first enzyme of pyruvate catabolism
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
ferredoxin from Clostridium pasteurianum
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-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the enzyme is involved in catabolism of pyruvate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the deazaflavin, coenzyme F420, which has been proposed to be the physiological electron acceptor of pyruvate oxidoreductase in methanogens, is not reduced by the purified enzyme. In addition to ferredoxin and viologen dyes, flavin nucleotides serve as electron acceptors
-
-
?
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+
-
the enzyme catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor)
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
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+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
enzyme Ape2126/2128
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 2400032000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
-
-
?
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 + 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 + FMN
acetyl-CoA + CO2 + FMNH + H+
-
5-6times lower activity with FMN as compared to benzyl viologen
-
-
?
pyruvate + CoA + FMN
acetyl-CoA + CO2 + FMNH + H+
-
5-6times lower activity with FMN as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
best activity with benzyl viologen
-
-
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
best activity with benzyl viologen
-
-
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
Giardia intestinalis WB / CC 30957
-
-
-
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
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-
-
-
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
-
-
-
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, and hydroxypyruvate
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-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
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-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
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-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
3-4times lower activity with methyl viologen as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + oxidized methylene blue
acetyl-CoA + CO2 + reduced methylene blue + H+
-
2.5-3times lower activity with methylene blue as compared to benzyl viologen
-
-
?
pyruvate + CoA + oxidized methylene blue
acetyl-CoA + CO2 + reduced methylene blue + H+
-
-
-
?
additional information
?
-
activity with 2-oxoglutarate is 6% compared to the activity with pyruvate. No activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape2126/2128,
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-
?
additional information
?
-
-
the enzyme cannot use 2-oxoglutarate as substrate
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-
?
additional information
?
-
-
the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
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-
?
additional information
?
-
-
neither NAD+ nor NADP+ can be reduced by the enzyme
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-
?
additional information
?
-
-
the enzyme cannot use 2-oxoglutarate as substrate
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-
?
additional information
?
-
-
the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
-
-
?
additional information
?
-
-
neither NAD+ nor NADP+ can be reduced by the enzyme
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-
?
additional information
?
-
-
the enzyme is incapable of using NAD+ and NADP+ as electron acceptors
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-
?
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
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
?
additional information
?
-
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
-
-
?
additional information
?
-
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
-
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
-
no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate, phenyl pyruvate or indole pyruvate
-
-
?
additional information
?
-
the addition of pyruvate to oxidized POR produces an isotropic signal centered at g = 2.01, assigned to a (hydroxyethy1)thiamine pyrophosphate radical intermediate. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite
-
-
?
additional information
?
-
-
the addition of pyruvate to oxidized POR produces an isotropic signal centered at g = 2.01, assigned to a (hydroxyethy1)thiamine pyrophosphate radical intermediate. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite
-
-
?
additional information
?
-
-
CoA is absolutely required. No substrates: 2-oxoglutarate, phenyl pyruvate, or indolyl pyruvate
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-
?