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Information on EC 1.2.7.1 - pyruvate synthase
for references in articles please use BRENDA:EC1.2.7.1
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.7 With an iron-sulfur protein as acceptor
1.2.7.1 pyruvate synthase
IUBMB 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).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 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
-
5-nitroimidazole
-
acetogenic
-
metronidazole-resistant
- africanus
-
tritrichomonas
-
hydrogen-producing
-
foramen
-
amitochondriate
- synthesis
-
ferredoxin-type
- indolepyruvate
- biofuel production
- analysis
- biotechnology
Reaction Schemes
showSynonyms
pyruvate:ferredoxin oxidoreductase, pyruvate ferredoxin oxidoreductase, pyruvate-ferredoxin oxidoreductase, pyruvate synthase, pfo a, ap120, pfora, pfor1, nifj1, pyruvate:ferredoxin oxidoreductase a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketobutyrate synthase
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-
-
-
2-oxobutyrate-ferredoxin oxidoreductase
-
-
-
-
alpha-ketobutyrate synthase
-
-
-
-
alpha-ketobutyrate-ferredoxin oxidoreductase
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-
-
-
bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
EC 1.2.7.2
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-
formerly
-
PFO
PFOR
PforA
PFR
PFR1
POR
PorEDABG
pyruvate ferredoxin oxidoreductase
pyruvate-ferredoxin oxidoreductase
pyruvate:ferredoxin oxidoreductase
synthase, 2-oxobutyrate
-
-
-
-
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
MetaCyc
Entner-Doudoroff pathway II (non-phosphorylative), gluconeogenesis II (Methanobacterium thermoautotrophicum), incomplete reductive TCA cycle, isopropanol biosynthesis (engineered), L-alanine degradation V (oxidative Stickland reaction), L-glutamate degradation VII (to butanoate), lactate fermentation to acetate, CO2 and hydrogen (Desulfovibrionales), purine nucleobases degradation II (anaerobic), pyruvate decarboxylation to acetyl CoA III, pyruvate fermentation to acetate I, pyruvate fermentation to acetate III, pyruvate fermentation to acetate VI, pyruvate fermentation to acetate VII, pyruvate fermentation to acetone, pyruvate fermentation to butanoate, pyruvate fermentation to butanol I, pyruvate fermentation to ethanol III, pyruvate fermentation to hexanol (engineered), reductive glycine pathway of autotrophic CO2 fixation, reductive monocarboxylic acid cycle, reductive TCA cycle I, reductive TCA cycle II
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methyl-thio-butyrate + CoA + 2 methyl viologen
?
Substrates: enzyme Ape2126/2128, 37% of the activity compared to pyruvate
Products: -
Products: -
?
2-oxoadipate + CoA + 2 methyl viologen
?
Substrates: enzyme Ape2126/2128, 37% of the activity compared to pyruvate
Products: -
Products: -
?
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
Substrates: enzyme Ape2126/2128, 98% of the activity compared to pyruvate
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
r
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
Substrates: -
Products: -
Products: -
r
glyoxylate + CoA + 2 oxidized methyl viologen
?
Substrates: enzyme Ape2126/2128, 89% of the activity compared to pyruvate
Products: -
Products: -
?
hydroxypyruvate + CoA + 2 methyl viologen
?
Substrates: enzyme Ape2126/2128, 38% of the activity compared to pyruvate
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized nitro blue tetrazolium
acetyl-CoA + CO2 + reduced nitro blue tetrazolium + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + H2O + oxidized methyl viologen
acetyl-CoA + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: coenzyme F420 is not reduced by the purified enzyme
Products: -
Products: -
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: coenzyme F420 is not reduced by the purified enzyme
Products: -
Products: -
?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
propanoyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
-
Substrates: the enzyme reacts with oxaloacetate at 4.8 activity relative to the activity against pyruvate
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
-
Substrates: the enzyme reacts with oxaloacetate at 4.8 activity relative to the activity against pyruvate
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
-
Substrates: the enzyme reacts with 2-oxobutyrate and oxaloacetate at 3–8% activity relative to the activity against pyruvate
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: the enzyme reacts with 2-oxobutyrate and oxaloacetate at 3–8% activity relative to the activity against pyruvate
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
Substrates: 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 24000–32000/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
Products: -
Products: -
?
2-oxobutyrate + CoA + oxidized methyl viologen
propanoyl-CoA + CO2 + reduced methyl viologen
Substrates: 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 24000–32000/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
Products: -
Products: -
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
Substrates: 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 24000–32000/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
Products: -
Products: -
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
?
Substrates: 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 24000–32000/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
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
?
-
Substrates: the enzyme reacts with oxaloacetate at 40% activity relative to the activity against pyruvate
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
?
-
Substrates: the enzyme reacts with 2-oxobutyrate and oxaloacetate at 3–8% activity relative to the activity against pyruvate
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
?
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: the enzyme reacts with 2-oxobutyrate and oxaloacetate at 3–8% activity relative to the activity against pyruvate
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
?
Substrates: 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 24000–32000/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
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
?
Substrates: 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 24000–32000/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
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + CoA + oxidized methyl viologen
? + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: coenzyme F420 is not reduced by the purified enzyme
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized benzyl viologen
acetyl-CoA + CO2 + 2 reduced benzyl viologen
Substrates: coenzyme F420 is not reduced by the purified enzyme
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: no activity with NAD+ or NADP+ as electron aceptor
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: no activity with NAD+ or NADP+ as electron aceptor
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: ferredoxin is an electron donor for the enzyme reaction in vivo
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: ferredoxin is an electron donor for the enzyme reaction in vivo
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: 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 24000–32000/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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: 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 24000–32000/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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: first enzyme of pyruvate catabolism
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: ferredoxin from Clostridium pasteurianum
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: the enzyme is involved in catabolism of pyruvate
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: 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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: first enzyme of pyruvate catabolism
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: ferredoxin from Clostridium pasteurianum
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: the enzyme is involved in catabolism of pyruvate
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: 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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: 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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: 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)
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: 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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: enzyme Ape2126/2128
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: 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 24000–32000/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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: 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 24000–32000/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
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + FMN
acetyl-CoA + CO2 + FMNH + H+
-
Substrates: 5-6times lower activity with FMN as compared to benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + FMN
acetyl-CoA + CO2 + FMNH + H+
-
Substrates: 5-6times lower activity with FMN as compared to benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
Substrates: best activity with benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
Substrates: best activity with benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized benzyl viologen
acetyl-CoA + CO2 + reduced benzyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
Giardia intestinalis WB / CC 30957
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
Substrates: -
Products: -
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?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, and hydroxypyruvate
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: 3-4times lower activity with methyl viologen as compared to benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized methylene blue
acetyl-CoA + CO2 + reduced methylene blue + H+
-
Substrates: 2.5-3times lower activity with methylene blue as compared to benzyl viologen
Products: -
Products: -
?
pyruvate + CoA + oxidized methylene blue
acetyl-CoA + CO2 + reduced methylene blue + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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,
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot use 2-oxoglutarate as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
Products: -
Products: -
?
additional information
?
-
-
Substrates: neither NAD+ nor NADP+ can be reduced by the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot use 2-oxoglutarate as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
Products: -
Products: -
?
additional information
?
-
-
Substrates: neither NAD+ nor NADP+ can be reduced by the enzyme
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is incapable of using NAD+ and NADP+ as electron acceptors
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
Products: -
Products: -
?
additional information
?
-
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-oxoglutarate, phenyl pyruvate or indole pyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
-
Substrates: CoA is absolutely required. No substrates: 2-oxoglutarate, phenyl pyruvate, or indolyl pyruvate
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?
additional information
?
-
Substrates: Incubation of the oxidized enzyme with CoA results in the partial reduction of a iron-sulfur center, which is not seen in the dithionite-reduced enzyme. 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: Incubation of the oxidized enzyme with CoA results in the partial reduction of a iron-sulfur center, which is not seen in the dithionite-reduced enzyme. 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
Products: -
Products: -
?
additional information
?
-
Substrates: Incubation of the oxidized enzyme with CoA results in the partial reduction of a iron-sulfur center, which is not seen in the dithionite-reduced enzyme. 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: 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+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: ferredoxin is an electron donor for the enzyme reaction in vivo
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: ferredoxin is an electron donor for the enzyme reaction in vivo
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: first enzyme of pyruvate catabolism
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: the enzyme is involved in catabolism of pyruvate
Products: -
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: first enzyme of pyruvate catabolism
Products: -
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: the enzyme is involved in catabolism of pyruvate
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Substrates: 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
Products: -
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?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
Giardia intestinalis WB / CC 30957
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin 1
acetyl-CoA + CO2 + reduced ferredoxin 1 + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + oxidized ferredoxin 2
acetyl-CoA + CO2 + reduced ferredoxin 2 + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot use 2-oxoglutarate as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot use 2-oxoglutarate as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to transfer electrons from pyruvate to the [Fe-Fe]-hydrogenase HYDA1, using the ferredoxins PETF and FDX2 as electron carriers
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
it is possible that flavins play an important regulatory or structural role in the enzyme
Ferredoxin
-
ferredoxin contains eight atoms of iron and eight acid-labile sulfur groups per molecule. The molecular mass is 6400 Da, the isoelelctric point 3.4. Ferredoxin is stable for at least 1 h at 70°C
-
FMN
it is possible that flavins play an important regulatory or structural role in the enzyme
CoA
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor
CoA
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor. The pyruvate decarboxylase activity accepts desulfo-CoA
thiamine diphosphate
-
essential cofactor, upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
thiamine diphosphate
-
per mol, the enzyme contains 0.8 mol thiamine diphosphate
thiamine diphosphate
contains 1 mol thiamine diphosphate per mol of enzyme
thiamine diphosphate
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
thiamine diphosphate
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
thiamine diphosphate
the enzyme contained 1 mol/mol thiamine diphosphate
[4Fe-4S]-center
-
the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
[4Fe-4S]-center
enzyme contains an extremely thermostable [4Fe-4S] ferredoxin. The Fe-S cluster has three cysteines and one aspartate as the cluster ligands. The 4Fe ferredoxin is degraded to 3Fe ferredoxin during aerobic purification. The aerobically-purified ferredoxin is reversibly converted back to the [4Fe-4S] ferredoxin by the addition of ferrous ions under reducing conditions. The anaerobically-purified [4Fe-4S] ferredoxin is quite stable, little degradtion is observed over 20 h at 100°C, while the half-life of the aerobically-purified ferredoxin is 10 h at 100°C
[4Fe-4S]-center
protein contains at least two [4Fe-4S] ferredoxin-type clusters
[4Fe-4S]-center
protein contains at least two [4Fe-4S] ferredoxin-type clusters
[4Fe-4S]-center
-
proteins contains at least two ferredoxin-type [4Fe-4S] clusters per molecule. Km value for ferredoxin is 0.026 microM
[4Fe-4S]-center
the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP
[4Fe-4S]-center
the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP
additional information
the enzyme is not coenzyme F420-dependent
-
additional information
FAD, FMN and lipoic acid are not found
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S cluster
-
the enzyme contains three [4Fe-4S]2+/1+ clusters all with very low reduction potentials
Iron
Iron-sulfur cluster
porE encodes the 21500 Da subunit that contains a high cysteinyl residue content and a motif indicative of a [Fe–S] cluster. Subunit porF also also has a high cysteinyl residue content, and two [Fe–S] cluster motifs. Based upon these results, it is proposed that PorE and PorF are components of a specialized system required to transfer low-potential electrons for pyruvate biosynthesis
Mg2+
Iron
-
per mol, the enzyme contains 9 mol of non-heme iron, and 8 mol of acid-labile sulfur. No inhibition by sodium arsenite
Iron
contains about 12 mol of non-heme iron per mol of enzyme
Iron
-
the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
Mg2+
-
upon addition of Mg2+, an ion that stabilizes thiamine diphosphate, the enzymatic activity almost doubles
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dioxygen
-
the enzyme is inactivated by dioxygen. Less than 50% of the original activity remains when the protein (0.23 mg/ml in 50 mM Tris/HCl pH 7.5) is exposed to air for 80 min at 25°C. Attempts to reactivate the enzyme by anoxic incubation in the presence of 2 mM dithiothreitol fail
Dithionite
with 5 mM dithionite, the half-life is 7 h at 2 °C, with about 90% of the original activity being lost after 24 h
glyoxylate
20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6%
NaCl
-
the addition of 0.3 M NaCl causes a significant inhibition (up to 80%) of the activity
thiamin diphosphate
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
[4Fe-4S]-center
CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
KCl
10–20% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 46–65% activation is reached, and further increased concentrations of KCl are inhibitory, enzyme Ape2126/2128
additional information
-
the enzyme is not inhibited by sodium nitrite (50 mM) or carbon monoxide (100% CO as gas phase)
-
additional information
no substrate inhibition with CoA up to 0.1 mM. Slightly or not inhibited at all by glyoxylate, nitrite, CO or potential physiological effectors. Not inhibited by CO. Potential affectors such as ATP, ADP, AMP, cAMP, GTP, GDP, GMP, NAD+, NADH, and glyceraldehyde 3-phosphate, at concentrations of 2 mM, do not affect the activity
-
additional information
-
not inhibitory: carbon monoxide, sodium cyanide, sodium fluoride, sodium azide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
the purified enzyme is slightly stimulated by high phosphate concentrations. Addition of 200 mM potassium (or sodium) phosphate stimulates the enzyme activity 3-4fold
thioredoxin 1
-
the Desulfovibrio vulgaris thioredoxin1 system activates the enzyme
additional information
-
dithiothreitol has no influence on the activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Amebiasis
Comparison between R-phycocyanin-labeled and R-phycoerythrin-labeled monoclonal antibody (Mab) probes for the detection of Entamoeba histolytica trophozoites.
Clostridium Infections
Identification and cloning of two immunogenic Clostridium perfringens proteins, elongation factor Tu (EF-Tu) and pyruvate:ferredoxin oxidoreductase (PFO) of C. perfringens.
Coinfection
Vaccination with Clostridium perfringens recombinant proteins in combination with Montanide™ ISA 71 VG adjuvant increases protection against experimental necrotic enteritis in commercial broiler chickens.
Cysts
Synthesis of pyruvate: ferredoxin oxidoreductase and alcohol dehydrogenase E enzymes during Giardia intestinalis excystation.
Embolism
Massive pulmonary embolism with a large thrombus stuck in patent foramen ovale - an impending paradoxical embolism.
Infections
Amixicile, a Novel Inhibitor of Pyruvate:Ferredoxin Oxidoreductase, Shows Efficacy against Clostridium difficile in a Mouse Infection Model.
Infections
Enteroaggregative Escherichia coli (EAEC) Strain in a Novel Weaned Mouse Model: Exacerbation by Malnutrition, Biofilm as a Virulence Factor, and Treatment by Nitazoxanide.
Ischemic Stroke
Massive pulmonary embolism with a large thrombus stuck in patent foramen ovale - an impending paradoxical embolism.
Ischemic Stroke
Spontaneous large right-to-left shunt and migraine headache with aura are risk factors for recurrent stroke in patients with a patent foramen ovale.
Migraine Disorders
Early post-procedural migraine attack predicts migraine resolution after patent foramen ovale transcatheter closure.
Pulmonary Embolism
Massive pulmonary embolism with a large thrombus stuck in patent foramen ovale - an impending paradoxical embolism.
Stroke
The Risk of Paradoxical Embolism (RoPE) Study: Developing risk models for application to ongoing randomized trials of percutaneous patent foramen ovale closure for cryptogenic stroke.
Thrombophilia
Spontaneous large right-to-left shunt and migraine headache with aura are risk factors for recurrent stroke in patients with a patent foramen ovale.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.205
2-oxobutyrate
pH 8.6, 37°C
0.264
oxaloacetate
pH 8.6, 37°C
0.0046
oxidized ferredoxin 1
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
-
0.0037
oxidized ferredoxin 2
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
-
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
0.0052
CoA
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
0.67
CoA
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
0.07
Oxidized benzyl viologen
37°C, pH 7.0
0.07
Oxidized benzyl viologen
clostridial ferredoxin, pH 7, 37°C
0.03
oxidized ferredoxin
37°C, pH 7.0, ferredoxin from Clostridium pasteurianum
0.03
oxidized ferredoxin
clostridial ferredoxin, pH 7, 37°C
0.14
oxidized methyl viologen
pH 8.4, 80°C
2.33
oxidized methyl viologen
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
0.115
pyruvate
pH 8.6, 37°C
0.16
pyruvate
-
in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
1.65
pyruvate
-
in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
2-oxobutyrate
pH 8.6, 37°C
18
oxaloacetate
pH 8.6, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.6
2-oxobutyrate
pH 8.6, 37°C
68.2
oxaloacetate
pH 8.6, 37°C
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
234.8
pyruvate
pH 8.6, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
-
50°C, pH not specified in the publication, enzyme from lactate-grown cells
0.3
pH 8.6, 37°C, substrate: indol-3-pyruvate
0.4
-
using cytochrome c as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
12
-
using benzyl viologen as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
2.3
-
using FMN as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
3.6
pH 8.6, 37°C, substrate: 2-oxobutyrate
3.7
-
using methyl viologen as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
4.5
-
using spinach ferredoxin 1 as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
4.7
-
using methylene blue as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
6.3
-
using Chlamydomonas reinhardtii ferredoxin 1 as electron acceptor, in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25 °C
6.5
pH 8.6, 37°C, substrate: oxaloacetate
7.4
pH 8.6, 37°C, substrate: pyruvate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
at 37 °C, maximal activity is obtained at pH 7.3
7.5
8.4
8.5
8.4
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity
8.4
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
pH 5.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
6 - 10
pH 6.0: about 45% of maximal activity, pH 10.0: about 60% of maximal activity, enzyme Ape2126/2128
6 - 8
-
the enzyme retains more than 70% of the initial activity at pH 6.0-8.0, even after 30 min incubation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
59
60
at pH 7.3, the temperature optimum is 60°C
65
80
90
95
90
pyruvate ferredoxin oxidoreductase activity
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30 - 50
-
the enzyme retains more than 60% of the initial activity 30-50°C, even after 30 min incubation
37 - 60
the activity detected at 60°C is five times the activity detected at 37°C
40 - 70
40°C: about 50% of maximal activity, 70°C: about 45% of maximal activity
43 - 71
43°C: about 55% of maximal activity, 71°C: about 5% of maximal activity
80 - 110
80°C: 45% of maximal activity, 110°C: 95% of maximal activity, enzyme Ape2126/2128
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit PorA
UniProt
brenda
Hydrogenobacter thermophilus TK-6 / IAM 12695
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
SwissProt
brenda
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
SwissProt
brenda
V9NGI4, i.e. subunit PorB, V9NFX1, i.e. subunit PorD, V9NGQ2 i.e. subunit PorG, V9NHA1 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
-
brenda
W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
UniProt
brenda
W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
UniProt
brenda
D3DJK0 i.e. alpha-subunit PorA, D3DJJ8 i.e. gamma-subunit PorG
D3DJK0; D3DJJ8
UniProt
brenda
Hydrogenobacter thermophilus TK-6 / IAM 12695
D3DJK0 i.e. alpha-subunit PorA, D3DJJ8 i.e. gamma-subunit PorG
D3DJK0; D3DJJ8
UniProt
brenda
P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
SwissProt
brenda
P80521: subunit PorA, P80522: subunit PorB, P80523: subunit PorC, P80524: subunit PorD
SwissProt
brenda
P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
SwissProt
brenda
P80521: subunit PorA, P80522: subunit PorB, P80523: subunit PorC, P80524: subunit PorD
SwissProt
brenda
Q51804 i.e. subunit PorA, Q51805 i.e. subunit PorB, Q51803 i.e. subunit PorD, Q51799 i.e. subunit PorG
UniProt
brenda
Q5JIJ8 i.e. delta subunit, Q5JIJ7 i.e. alpha subunit, Q5JIJ6 i.e. beta subunit
Q5JIJ8; Q5JIJ7; Q5JIJ6
UniProt
brenda
O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
UniProt
brenda
Q56317, i.e. subunit PorB, O05650, i.e. subunit PorC, Q56316 i.e. subunit PorD, O05651 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
-
brenda
O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
UniProt
brenda
Q56317, i.e. subunit PorB, O05650, i.e. subunit PorC, Q56316 i.e. subunit PorD, O05651 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
resistance to metronidazole is associated with enzyme down-regulation
metabolism
physiological function
metabolism
the enzyme is involved in catabolism of pyruvate
metabolism
-
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
physiological function
-
PFOR is translated after the second phase of the excystation process
physiological function
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
physiological function
-
the enzyme is a surface-associated cell-binding protein that lacks enzyme activity and is involved in cytoadherence to host cells
physiological function
first enzyme of pyruvate catabolism
physiological function
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
physiological function
Q5JIJ8; Q5JIJ7; Q5JIJ6
in a cytosolic hydrogenase-deficient strain, pyruvate:ferredoxin oxidoreductase POR and 2-oxoisovalerate:ferredoxin oxidoreductase VOR specifically function in oxidation of pyruvate and branched-chain amino acids, respectively, and the lack of POR or VOR is compensated for by promoting the oxidation of another substrate driven by the remaining oxidoreductase
physiological function
pyruvate ferredoxin oxidoreductase, encoded by PforA, plays a key role in pyruvate dissimilation. Although the pfl gene encoding pyruvate formate-lyase is normally expressed at low levels, it is crucial for biosynthesis in Thermoanaerobacterium saccharolyticum. In pforA deletion strains, pfl expression increases and is able to partially compensate for the loss of pyruvate ferredoxin oxidoreductase activity. Deletion of both pforA and pfl results in a strain that requires acetate and formate for growth and produces lactate as the primary fermentation product, achieving 88% theoretical lactate yield
physiological function
Zn-dependent dehydrogenase 2-ADH, pyruvate-ferredoxin oxidoreductase PFOR and several glycolytic enzymes coexist in a protein complex. Native 2-ADH is present in two forms, PFOR-bound and PFOR-free. The enzyme activity of 2-ADH is inhibited in a non-competitive mode by PFOR, implying the interaction of 2-ADH and PFOR negatively regulate alcohol formation
physiological function
-
the enzyme is involved in proliferation, adhesion to host cells, and abscess formation, thereby influencing the pathogenicity of Trichomonas vaginalis
physiological function
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
physiological function
-
Zn-dependent dehydrogenase 2-ADH, pyruvate-ferredoxin oxidoreductase PFOR and several glycolytic enzymes coexist in a protein complex. Native 2-ADH is present in two forms, PFOR-bound and PFOR-free. The enzyme activity of 2-ADH is inhibited in a non-competitive mode by PFOR, implying the interaction of 2-ADH and PFOR negatively regulate alcohol formation
-
physiological function
-
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
-
physiological function
-
pyruvate ferredoxin oxidoreductase, encoded by PforA, plays a key role in pyruvate dissimilation. Although the pfl gene encoding pyruvate formate-lyase is normally expressed at low levels, it is crucial for biosynthesis in Thermoanaerobacterium saccharolyticum. In pforA deletion strains, pfl expression increases and is able to partially compensate for the loss of pyruvate ferredoxin oxidoreductase activity. Deletion of both pforA and pfl results in a strain that requires acetate and formate for growth and produces lactate as the primary fermentation product, achieving 88% theoretical lactate yield
-
Show AA Sequence and Transmembrane Helices (5606 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
120000
13000
130000
14000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
15000
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
21300
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
22000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
23000
240000
25000
26000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
26100
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
280000
-
dimer, non-denaturing gradient gel in absence of reducing agent
30000
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
32300
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
34000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
34936
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128
35000
43000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
44300
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
45000
46000
48000
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
545000
-
tetramer, non-denaturing gradient gel in absence of reducing agent
71639
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128
8900
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
13000
1 * 46000 + 1 * 35000 + 1 * 23000 + 1 * 13000, SDS-PAGE
13000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
23000
1 * 46000 + 1 * 35000 + 1 * 23000 + 1 * 13000, SDS-PAGE
23000
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
25000
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
35000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
35000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
35000
1 * 46000 + 1 * 35000 + 1 * 23000 + 1 * 13000, SDS-PAGE
45000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
46000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
46000
1 * 46000 + 1 * 35000 + 1 * 23000 + 1 * 13000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
heterodimer
homodimer
multimer
-
x * 43000, plus x * 34000, plus x * 23000, plus x * 13000, SDS-PAGE
octamer
tetramer
additional information
?
x * 130000, calculated from sequence, x * 128000, SDS-PAGE
?
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
?
-
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
-
?
x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE
?
alphabetagammadelta structure, 1 * 48000 (subunit PorA) + 1 * 30000 (subunit PorB) + 1 * 25000 (subunit PorC) + 1 * 15000 (subunit PorD), SDS-PAGE
?
-
alphabetagammadelta structure, 1 * 48000 (subunit PorA) + 1 * 30000 (subunit PorB) + 1 * 25000 (subunit PorC) + 1 * 15000 (subunit PorD), SDS-PAGE
-
decamer
D3DJK0; D3DJJ8
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
decamer
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
2 * 21300, subunit PorG, 2 * 44300, subunit PorA, 2 * 32300, subunit PoB, 2 * 26100, subunit PorG, 2 * 8900, subunit PorE, calculated and SDS-PAGE
-
heterodimer
1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128
heterodimer
1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128
octamer
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
octamer
-
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
-
octamer
-
dimer of heterotetramers (alphabetagammadelta)2, 2 * 44000, alpha-subunit, 2 * 36000, beta-subunit, 2 * 20000, gamma subunit, 2 * 12000, delta-subunit, SDS-PAGE
tetramer
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
tetramer
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE
-
tetramer
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
tetramer
1 * 46000 + 1 * 35000 + 1 * 23000 + 1 * 13000, SDS-PAGE
additional information
D3DJK0; D3DJJ8
subunits PorA, PorB, PorG, and PorE are similar to the alpha, beta, gamma, and delta subunits of the four subunit-type 2-oxoacid oxidoreductases, respectively, and have conserved specific motifs. PorD has no specific motifs but is essential for the expression of the active enzyme. For recombinant enzyme, maximal activity is obtained when all five of the genes, porEDABG, are expressed. In the absence of porD, no active enzyme is produced
additional information
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
subunits PorA, PorB, PorG, and PorE are similar to the alpha, beta, gamma, and delta subunits of the four subunit-type 2-oxoacid oxidoreductases, respectively, and have conserved specific motifs. PorD has no specific motifs but is essential for the expression of the active enzyme. For recombinant enzyme, maximal activity is obtained when all five of the genes, porEDABG, are expressed. In the absence of porD, no active enzyme is produced
-
additional information
-
the enzyme is composed of two catalytic units of molecular mass 120000 Da. Each unit consists of four subunits, alpha/beta/gamma/delta, with masses of approximately 44000 Da, 36000 Da, 20000 Da, and 12000 Da, respectively, and contains at least two [4Fe-4S] clusters. The recombinantly expressed and reconstituted delta subunit is monomeric with a mass of 11879 Da
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native structure, those of lactyl-TPP and acetyl-TPP reaction intermediates, and with CoA bound. CoA binds to domain III and CoA binding and domain III movement drive electron transfer from the TPP, which is coordinated by domains I and IV, into the domain V [4Fe-4S] clusters
determination of reduction midpoint potentials from 10 to 85°C. The enzyme exhibits two voltammetric waves with peaks at -280 and -403 mV at room temperature, indicating multiple redox centers, and a single wave at -420 mV at 85°C. Ferredoxin displays a single linear temperature-dependent voltammetric wave at -280 mV at room temperature and -327 mV at 85°C
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
-
30 min, anoxic conditions, more than 80% residual activity after heating
80
85
-
the recombinantly expressed, purified and reconstituted delta subunit is stable for 2 h
90
80
half-life of pyruvate decarboxylase activity 2 h, of pyruvate ferredoxin oxidoreductase activity 3 h
90
-
60 min, in the presence of 2 M KCl, 50% loss of activity. In absence of salt 50% loss of activity after 50 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
following dialysis, the enzyme is very unstable in the absence of glycerol or ethylene glycol, thiamine diphosphate and MgCl2 also help to maintain activity
purified enzyme, stored for one year under liquid N2, no loss of activity if thawed anaerobically
-
the enzyme is extremely oxygen sensitive, losing 90% of its activity upon exposure to air for 1 h at 0°C
the operational stability of the enzyme in alginate hydrogels retains over 68% initial activity after 10 repeated cycles
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
oxygen-sensitive enzyme, the t1/2 for the enzyme activity in 50 mM Tris-HCl, pH 7.8 containing 2 mM sodium dithionite and 2 mM DTT is approximately 30 min
726840
the enzyme is efficiently protected when cells are exposed to air or H2O2
-
725463
the enzyme is extremely oxygen sensitive, losing 90% of its activity upon exposure to air for 1 h at 0°C
744835
the enzyme is inactivated by O2. Less than 50% of the original activity remains when the protein (0.23 mg/ml in 50 mM Tris/HCl pH 7.5) is exposed to air for 80 min at 25°C. Attempts to reactivate the enzyme by anoxic incubation in the presence of 2 mM dithiothreitol fail
-
288449
the enzyme is inactivated by oxygen, which makes it difficult to purify the enzyme under oxic conditions. The enzyme can be stabilized when 0.1% Triton X-100 is added to the purification buffers
-
288436
the enzyme is very sensitive to O2. Following incubation in air at 2°C for 40 min, about 60% of enzyme activity is lost. The half-life is 5.2 min when the purified enzyme is exposed to air in an ice bath. After inactivation of the purified enzyme by oxygen, activity is not restored byreplacing the oxygen with nitrogen and adding 0.01 mM dithionite no activity is lost after dialysis of extract in a basic buffer containing 20 mM potassium Tricine, pH 8.6, 5 mM MgCl2, 0.5 mM dithiothreitol, 0.1 mM thiamine diphosphate, and 10% glycerol
654391
when the recombinant enzyme (in 50 mM Tricine, pH 8.0) is exposed to air for 1 h on ice, a drastic loss of activity is observed
-
726231
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
736379
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
736379
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme
-20°C, under N2, after addition of 20% (v/v) glycerol to each fraction, the enzyme activity remains nearly constant for several weeks
-70°C, anaerobically in presence of CoASH, thiamine diphosphate anfd Mg2+, enzyme concentration below 0.02 mg/ml, stable for months
-
2°C, 2 weeks, anaerobic conditions, no loss of activity
4°C, storage results in a loss of 80% of the activity within 8 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DE52 column chromatography, DEAE-cellulose column chromatography, and Sephadex G25 gel filtration
-
Ni-NTA column chromatography
purifiaction using Q-sepharose, hydroxyapatite, blue sepharose and sephacryl
-
purified enzyme shos a brownish colour characteristic of iron-sulfur containing proteins
purified enzyme shows a brownish colour characteristic of iron-sulfur containing proteins
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
-
recombinantly expressed delta subunit is purified after reconstitution with iron and sulfide. The reconstituted delta-subunit is monomeric with a mass of 11879 Da as determined by mass spectrometry. The purified and reconstituted delta subunit contains 8 Fe mol/mol and remains intact when incubated at 85 °C for 2 h
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
metronidazole-resistant Giardia line 106-2ID10 has decreased PFOR activity
-
the operon organization for Pyrococcus furiosus pyruvate ferredoxin oxidoreductase POR and 2-oxoisovalerate ferredoxin oxidoreductase VOR is porG-vorDAB-porDAB, wherein the gamma subunit is shared by the two enzymes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biochemical assay for activity, low-potential electrons are introduced by photochemical reduction of EDTA/deazaflavin and the generated pyruvate is trapped by chemical derivatization with semicarbazide. The product of CO2 fixation can be detected as pyruvate semicarbazone by HPLC-MS
biofuel production
-
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
biotechnology
synthesis
biotechnology
-
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production
biotechnology
-
pyruvate:ferredoxin oxidoreductase PFR1 and [Fe-Fe]-hydrogenase HYDA1 of Chlamydomonas can be coupled for pyruvate-dependent H2 production
-
synthesis
-
engineering of Thermoanaerobacterium saccharolyticum to produce ethanol at high yield. Knockout of genes involved in organic acid formation (acetate kinase, phosphate acetyltransferase, and L-lactate dehydrogenase) results in a strain able to produce ethanol as the only detectable organic product and substantial changes in electron flow relative to the wild type. Ethanol formation in the engineered strain ALK2 utilizes pyruvate:ferredoxin oxidoreductase with electrons transferred from ferredoxin to NAD(P). The homoethanologenic phenotype is stable for more than 150 generations in continuous culture. The growth rate of strain ALK2 is similar to the wild-type strain, with a reduction in cell yield proportional to the decreased ATP availability resulting from acetate kinase inactivation. Glucose and xylose are coutilized and utilization of mannose and arabinose commences before glucose and xylose are exhausted. Using strain ALK2 in simultaneous hydrolysis and fermentation experiments at 50°C allows a 2.5fold reduction in cellulase loading compared with using Saccharomyces cerevisiae at 37°C. The maximum ethanol titer produced by strain ALK2 is 37 g/liter
synthesis
homologous protein production in Thermoacetobacter kivui by cloning and expression in Thermoacetobacter kivui. The encoded protein containing a genetically engineered His-tag is purified in only two steps to apparent homogeneity, and has the same properties as the native
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoon, K.S.; Ishii, M.; Kodama, T.; Igarashi, Y.
Purification and characterization of pyruvate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6
Arch. Microbiol.
167
275-279
1997
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
brenda
Blamey, J.M.; Adams, M.W.W.
Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
Biochim. Biophys. Acta
1161
19-27
1993
Pyrococcus furiosus
brenda
Kletzin, A.; Adams, M.W.W.
Molecular and phylogenetic chararcterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima
J. Bacteriol.
178
248-257
1996
Pyrococcus furiosus (Q51804 and Q51805 and Q51803 and Q51799), Pyrococcus furiosus, Thermotoga maritima (O05651 and Q56317 and O05650 and Q56316), Thermotoga maritima, Thermotoga maritima DSM 3109 (O05651 and Q56317 and O05650 and Q56316)
brenda
Townson, S.M.; Upcroft, J.A.; Upcroft, P.
Characterization and purification of pyruvate:ferredoxin oxidoreductase from Giardia duodenalis
Mol. Biochem. Parasitol.
79
183-193
1996
Giardia intestinalis, Giardia intestinalis BRIS/83/HEPU/106
brenda
Bock, A.K.; Kunow, J.; Glasemacher, J.; Schönheit, P.
Catalytic properties, molecular composition and sequence alignment of pyruvate:ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro)
Eur. J. Biochem.
237
35-44
1996
Methanosarcina barkeri (P80521 and P80522 and P80523 and P80524), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P80521 and P80522 and P80523 and P80524)
brenda
Kunow, J.; Linder, D.; Thauer, R.K.
Pyruvate:ferredoxin oxidoreductase from the sulfate-reducing Archaeoglobus fulgidus: molecular composition, catalytic properties, and sequence alignments
Arch. Microbiol.
163
21-28
1995
Archaeoglobus fulgidus
brenda
Lin, W.C.; Yang, Y.L.; Whitman, W.B.
The anabolic pyruvate oxidoreductase from Methanococcus maripaludis
Arch. Microbiol.
179
444-456
2003
Methanococcus maripaludis (Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3), Methanococcus maripaludis DSM Z 2067 (Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3)
brenda
Ikeda, T.; Ochiai, T.; Morita, S.; Nishiyama, A.; Yamada, E.; Arai, H.; Ishii, M.; Igarashi, Y.
Anabolic five subunit-type pyruvate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6
Biochem. Biophys. Res. Commun.
340
76-82
2006
Hydrogenobacter thermophilus (D3DJK0 and D3DJJ8), Hydrogenobacter thermophilus TK-6 / IAM 12695 (D3DJK0 and D3DJJ8)
brenda
Nishizawa, Y.; Yabuki, T.; Fukuda, E.; Wakagi, T.
Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1
FEBS Lett.
579
2319-2322
2005
Aeropyrum pernix (Q9YA13 and Q9YA11)
brenda
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
Arch. Microbiol.
163
112-118
1995
Archaeoglobus fulgidus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus, Archaeoglobus profundus DSM 5631
-
brenda
Labes, A.; Schoenheit, P.
Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Arch. Microbiol.
176
329-338
2001
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
brenda
Zhou, Z.H.; Adams, M.W.
Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions
Biochemistry
36
10892-10900
1997
Pyrococcus furiosus
brenda
Menon, A.L.; Hendrix, H.; Hutchins, A.; Verhagen, M.F.; Adams, M.W.
The delta-subunit of pyruvate ferredoxin oxidoreductase from Pyrococcus furiosus is a redox-active, iron-sulfur protein: evidence for an ancestral relationship with 8Fe-type ferredoxins
Biochemistry
37
12838-12846
1998
Pyrococcus furiosus
brenda
Ma, K.; Hutchins, A.; Sung, S.J.; Adams, M.W.
Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase
Proc. Natl. Acad. Sci. USA
94
9608-9613
1997
Pyrococcus furiosus
brenda
Leitsch, D.; Burgess, A.G.; Dunn, L.A.; Krauer, K.G.; Tan, K.; Duchene, M.; Upcroft, P.; Eckmann, L.; Upcroft, J.A.
Pyruvate:ferredoxin oxidoreductase and thioredoxin reductase are involved in 5-nitroimidazole activation while flavin metabolism is linked to 5-nitroimidazole resistance in Giardia lamblia
J. Antimicrob. Chemother.
66
1756-1765
2011
Giardia intestinalis
brenda
Pieulle, L.; Stocker, P.; Vinay, M.; Nouailler, M.; Vita, N.; Brasseur, G.; Garcin, E.; Sebban-Kreuzer, C.; Dolla, A.
Study of the thiol/disulfide redox systems of the anaerobe Desulfovibrio vulgaris points out pyruvate:ferredoxin oxidoreductase as a new target for thioredoxin 1
J. Biol. Chem.
286
7812-7821
2011
Desulfovibrio vulgaris
brenda
Noth, J.; Krawietz, D.; Hemschemeier, A.; Happe, T.
Pyruvate:ferredoxin oxidoreductase is coupled to light-independent hydrogen production in Chlamydomonas reinhardtii
J. Biol. Chem.
288
4368-4377
2013
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
brenda
Emelyanov, V.V.; Goldberg, A.V.
Fermentation enzymes of Giardia intestinalis, pyruvate:ferredoxin oxidoreductase and hydrogenase, do not localize to its mitosomes
Microbiology
157
1602-1611
2011
Giardia intestinalis (Q24982), Giardia intestinalis, Giardia intestinalis WB / CC 30957 (Q24982)
brenda
Meza-Cervantez, P.; Gonzalez-Robles, A.; Cardenas-Guerra, R.E.; Ortega-Lopez, J.; Saavedra, E.; Pineda, E.; Arroyo, R.
Pyruvate:ferredoxin oxidoreductase (PFO) is a surface-associated cell-binding protein in Trichomonas vaginalis and is involved in trichomonal adherence to host cells
Microbiology
157
3469-3482
2011
Trichomonas vaginalis
brenda
van Lis, R.; Baffert, C.; Coute, Y.; Nitschke, W.; Atteia, A.
Chlamydomonas reinhardtii chloroplasts contain a homodimeric pyruvate:ferredoxin oxidoreductase that functions with FDX1
Plant Physiol.
161
57-71
2013
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
brenda
Eram, M.S.; Oduaran, E.; Ma, K..
The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis
Archaea
2014
349379
2014
Thermococcus guaymasensis (W8CQR1 and W8CQB2 and W8CQB1 and W8CR61), Thermococcus guaymasensis, Thermococcus guaymasensis DSM 11113 (W8CQR1 and W8CQB2 and W8CQB1 and W8CR61)
brenda
Bock, A.K.; Schönheit, P.; Teixeira, M.
The iron-sulfur centers of the pyruvate:ferredoxin oxidoreductase from Methanosarcina barkeri (Fusaro)
FEBS Lett.
414
209-212
1997
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
brenda
Wang, Q.; Wang, Q.; Tong, W.; Bai, X.; Chen, Z.; Zhao, J.; Zhang, J.; Liu, S.
Regulation of enzyme activity of alcohol dehydrogenase through its interactions with pyruvate-ferredoxin oxidoreductase in Thermoanaerobacter tengcongensis
Biochem. Biophys. Res. Commun.
417
1018-1023
2012
Caldanaerobacter subterraneus subsp. tengcongensis (Q8RCI3), Caldanaerobacter subterraneus subsp. tengcongensis, Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 (Q8RCI3)
brenda
Blamey, J.M.; Adams, M.W.
Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium, Thermotoga maritima
Biochemistry
33
1000-1007
1994
Thermotoga maritima
brenda
Smith, E.T.; Blamey, J.M.; Adams, M.W.
Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon, Pyrococcus furiosus, and the hyperthermophilic bacterium, Thermotoga maritima, have different catalytic mechanisms
Biochemistry
33
1008-1016
1994
Thermotoga maritima (O05651 and Q56317 and O05650 and Q56316), Thermotoga maritima, Pyrococcus furiosus (Q51804 and Q51805 and Q51803 and Q51799), Pyrococcus furiosus, Thermotoga maritima DSM 3109 (O05651 and Q56317 and O05650 and Q56316)
brenda
Forget, P.
Purification and characterization of a heat stable ferredoxin isolated from Clostridium thermocellum
Biochimie
64
1009-1014
1983
Acetivibrio thermocellus
brenda
Zhou, J.; Olson, D.; Lanahan, A.; Tian, L.; Murphy, S.; Lo, J.; Lynd, L.
Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SL-YS485
Biotechnol. Biofuels
8
138
2015
Thermoanaerobacterium saccharolyticum (I3VRD9), Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum JW/SL-YS485 (I3VRD9), Thermoanaerobacterium saccharolyticum JW/SL-YS485
brenda
Nohara, K.; Orita, I.; Nakamura, S.; Imanaka, T.; Fukui, T.
Genetic examination and mass balance analysis of pyruvate/amino acid oxidation pathways in the hyperthermophilic archaeon Thermococcus kodakarensis
J. Bacteriol.
196
3831-3839
2014
Thermococcus kodakarensis (Q5JIJ8 and Q5JIJ7 and Q5JIJ6), Thermococcus kodakarensis
brenda
Imai, T.; Taguchi, K.; Ogawara, Y.; Ohmori, D.; Yamakura, F.; Ikezawa, H.; Urushiyama, A.
Characterization and cloning of an extremely thermostable, Pyrococcus furiosus-type 4Fe ferredoxin from Thermococcus profundus
J. Biochem.
130
649-655
2001
Thermococcus profundus (Q9HHD4), Thermococcus profundus
brenda
Eram, M.S.; Wong, A.; Oduaran, E.; Ma, K.
Molecular and biochemical characterization of bifunctional pyruvate decarboxylases and pyruvate ferredoxin oxidoreductases from Thermotoga maritima and Thermotoga hypogea
J. Biochem.
158
459-466
2015
Pseudothermotoga hypogea (V9NGI4 and V9NFX1 and V9NGQ2 and V9NHA1), Pseudothermotoga hypogea, Thermotoga maritima (Q56317 and 05650 and Q56316 and O05651), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q56317 and 05650 and Q56316 and O05651)
brenda
Smith, E.T.; Odom, L.D.; Awramko, J.A.; Chiong, M.; Blamey, J.
Direct electrochemical characterization of hyperthermophilic Thermococcus celer metalloenzymes involved in hydrogen production from pyruvate
J. Biol. Inorg. Chem.
6
227-231
2001
Thermococcus celer
brenda
Shaw, A.J.; Podkaminer, K.K.; Desai, S.G.; Bardsley, J.S.; Rogers, S.R.; Thorne, P.G.; Hogsett, D.A.; Lynd, L.R.
Metabolic engineering of a thermophilic bacterium to produce ethanol at high yield
Proc. Natl. Acad. Sci. USA
105
13769-13774
2008
Thermoanaerobacterium saccharolyticum
brenda
Takenaka, M.; Yoon, K.S.; Matsumoto, T.; Ogo, S.
Acetyl-CoA production by encapsulated pyruvate ferredoxin oxidoreductase in alginate hydrogels
Biores. Technol.
227
279-285
2017
Citrobacter sp.
brenda
Saranyah, K.; Kalva, S.; Mukund, N.; Singh, S.K.; Saleena, L.M.
Homology modeling and in silico site directed mutagenesis of pyruvate ferredoxin oxidoreductase from Clostridium thermocellum
Comb. Chem. High Throughput Screen.
18
975-989
2015
Acetivibrio thermocellus
brenda
Song, H.O.
Influence of 120 kDa pyruvate:ferredoxin oxidoreductase on pathogenicity of Trichomonas vaginalis
Korean J. Parasitol.
54
71-74
2016
Trichomonas vaginalis
brenda
Kushkevych, I.V.
Kinetic properties of pyruvate ferredoxin oxidoreductase of intestinal sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9
Pol. J. Microbiol.
64
107-114
2015
Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger, Desulfovibrio piger Vib-7
brenda
Bock, A.; Kunow, J.; Glasemacher, J.; Schönheit, P.
Catalytic properties, molecular composition and sequence alignments of pyruvate ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro)
Eur. J. Biochem.
237
35-44
1996
Methanosarcina barkeri (P80521 and P80522 and P80523 and P80524), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P80521 and P80522 and P80523 and P80524)
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
Patil, Y.; Junghare, M.; Müller, N.
Fermentation of glycerol by Anaerobium acetethylicum and its potential use in biofuel production
Microb. Biotechnol.
10
203-217
2017
Anaerobium acetethylicum
brenda
Warren, C.A.; van Opstal, E.; Ballard, T.E.; Kennedy, A.; Wang, X.; Riggins, M.; Olekhnovich, I.; Warthan, M.; Kolling, G.L.; Guerrant, R.L.; Macdonald, T.L.; Hoffman, P.S.
Amixicile, a novel inhibitor of pyruvate ferredoxin oxidoreductase, shows efficacy against Clostridium difficile in a mouse infection model
Antimicrob. Agents Chemother.
56
4103-4111
2012
Clostridioides difficile, Clostridioides difficile ATCC 43255
brenda
Witt, A.; Pozzi, R.; Diesch, S.; Haedicke, O.; Grammel, H.
New light on ancient enzymes - in vitro CO2 fixation by pyruvate synthase of Desulfovibrio africanus and Sulfolobus acidocaldarius
FEBS J.
286
4494-4508
2019
Desulfocurvibacter africanus (P94692), Desulfocurvibacter africanus
brenda
Katsyv, A.; Schoelmerich, M.C.; Basen, M.; Mueller, V.
The pyruvate ferredoxin oxidoreductase of the thermophilic acetogen, Thermoanaerobacter kivui
FEBS open bio
11
1332-1342
2021
Thermoanaerobacter kivui (A0A097APA2), Thermoanaerobacter kivui
brenda
Nisa, K.; Ashraf, S.; Siddiqui, M.; Taj, N.; Habib-Ur-Rehma, H.; Bano, A.; Rashid, N.
Purification and characterization of a thermostable pyruvate ferredoxin oxidoreductase/pyruvate decarboxylase from Thermococcus kodakaraensis
Pak. J. Zool.
52
1149-1156
2020
Thermococcus kodakarensis
-
brenda
Chen, P.Y.; Aman, H.; Can, M.; Ragsdale, S.W.; Drennan, C.L.
Binding site for coenzyme A revealed in the structure of pyruvate ferredoxin oxidoreductase from Moorella thermoacetica
Proc. Natl. Acad. Sci. USA
115
3846-3851
2018
Moorella thermoacetica (Q2RMD6)
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.7.1)
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