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Information on EC 1.2.7.1 - pyruvate synthase and Organism(s) Pyrococcus furiosus and UniProt Accession Q51799
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1.2.7.1 pyruvate synthaseIUBMB Comments
Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
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Word Map
- 1.2.7.1
- ferredoxins
- acetyl-coa
- clostridium
- hydrogenase
- metronidazole
- hydrogenosomal
- trichomonas
- vaginalis
- thiamin
- histolytica
- entamoeba
- giardia
- desulfovibrio
- pasteurianum
-
low-potential
- duodenalis
-
trichomoniasis
- 2-oxoacids
- flavodoxins
-
adp-forming
- nitazoxanide
- formate-lyase
-
wood-ljungdahl
-
2-oxoacid:ferredoxin
-
5-nitroimidazole
-
acetogenic
-
metronidazole-resistant
- africanus
-
tritrichomonas
-
hydrogen-producing
-
foramen
-
amitochondriate
- synthesis
-
ferredoxin-type
- indolepyruvate
- biofuel production
- analysis
- biotechnology
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
pyruvate:ferredoxin oxidoreductase, pyruvate ferredoxin oxidoreductase, pyruvate-ferredoxin oxidoreductase, pyruvate synthase, pfo a, ap120, pfora, pfor1, nifj1, pyruvate:ferredoxin oxidoreductase a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketobutyrate synthase
-
-
-
-
2-oxobutyrate-ferredoxin oxidoreductase
-
-
-
-
alpha-ketobutyrate synthase
-
-
-
-
alpha-ketobutyrate-ferredoxin oxidoreductase
-
-
-
-
POR
synthase, 2-oxobutyrate
-
-
-
-
POR
-
bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + oxidized methyl viologen
acetyl-CoA + CO2 + reduced methyl viologen
-
-
-
-
?
pyruvate + H2O + oxidized methyl viologen
acetyl-CoA + reduced methyl viologen + H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
the enzyme catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor)
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
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-
?
additional information
?
-
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no activity with 2-oxoglutarate, phenyl pyruvate or indole pyruvate
-
-
?
additional information
?
-
the addition of pyruvate to oxidized POR produces an isotropic signal centered at g = 2.01, assigned to a (hydroxyethy1)thiamine pyrophosphate radical intermediate. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite
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-
?
additional information
?
-
-
the addition of pyruvate to oxidized POR produces an isotropic signal centered at g = 2.01, assigned to a (hydroxyethy1)thiamine pyrophosphate radical intermediate. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
the enzyme catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain
[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
protein contains at least two [4Fe-4S] ferredoxin-type clusters
[4Fe-4S]-center
the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
the enzyme contains at least two [4Fe-4S] clusters. The purified and reconstituted delta subunit contains 8 Fe mol/mol
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
-
the recombinantly expressed, purified and reconstituted delta subunit is stable for 2 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, stored for one year under liquid N2, no loss of activity if thawed anaerobically
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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)
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
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
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
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)
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
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