1.2.7.1: pyruvate synthase
This is an abbreviated version!
For detailed information about pyruvate synthase, go to the full flat file.
Word Map on EC 1.2.7.1
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1.2.7.1
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ferredoxins
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acetyl-coa
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clostridium
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hydrogenase
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metronidazole
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hydrogenosomal
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trichomonas
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vaginalis
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thiamin
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histolytica
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entamoeba
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giardia
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desulfovibrio
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pasteurianum
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low-potential
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duodenalis
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trichomoniasis
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2-oxoacids
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flavodoxins
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adp-forming
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nitazoxanide
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formate-lyase
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wood-ljungdahl
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2-oxoacid:ferredoxin
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5-nitroimidazole
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acetogenic
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metronidazole-resistant
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africanus
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tritrichomonas
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hydrogen-producing
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foramen
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amitochondriate
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synthesis
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ferredoxin-type
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indolepyruvate
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biofuel production
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analysis
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biotechnology
- 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
Synonyms
2-ketobutyrate synthase, 2-oxobutyrate (methylviologen), 2-oxobutyrate synthase (benzylviologen), 2-oxobutyrate-ferredoxin oxidoreductase, alpha-ketobutyrate synthase, alpha-ketobutyrate-ferredoxin oxidoreductase, AP120, Ape2126/2128, bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase, EC 1.2.7.2, Moth_0064, NifJ1, OFOR, PFO, PFO A, PFOR, Pfor1, PforA, PFR, PFR1, POR, PorEDABG, pyruvate ferredoxin oxidoreductase, pyruvate-ferredoxin oxidoreductase, pyruvate:Fd oxidoreductase, pyruvate:ferredoxin oxidoreductase, pyruvate:ferredoxin oxidoreductase A, synthase, 2-oxobutyrate, TKV_c04340, Tsac_0046, TTE0445
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General Information
General Information on EC 1.2.7.1 - pyruvate synthase
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malfunction
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resistance to metronidazole is associated with enzyme down-regulation
metabolism
physiological function
the enzyme is involved in catabolism of pyruvate
metabolism
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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
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PFOR is translated after the second phase of the excystation process
physiological function
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Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
physiological function
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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
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the enzyme is involved in proliferation, adhesion to host cells, and abscess formation, thereby influencing the pathogenicity of Trichomonas vaginalis
physiological function
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Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
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physiological function
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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
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physiological function
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in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
-
physiological function
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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
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