EC Number |
General Information |
Reference |
---|
1.2.7.1 | physiological function |
first enzyme of pyruvate catabolism |
-, 288448 |
1.2.7.1 | physiological function |
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon |
-, 654391 |
1.2.7.1 | physiological function |
PFOR is translated after the second phase of the excystation process |
711368 |
1.2.7.1 | physiological function |
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming) |
-, 721449 |
1.2.7.1 | malfunction |
resistance to metronidazole is associated with enzyme down-regulation |
725220 |
1.2.7.1 | physiological function |
the enzyme is a surface-associated cell-binding protein that lacks enzyme activity and is involved in cytoadherence to host cells |
725907 |
1.2.7.1 | 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 |
-, 735589 |
1.2.7.1 | 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 |
-, 735819 |
1.2.7.1 | physiological function |
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 |
736364 |
1.2.7.1 | physiological function |
the enzyme is involved in proliferation, adhesion to host cells, and abscess formation, thereby influencing the pathogenicity of Trichomonas vaginalis |
740931 |