Pyruvate synthase

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pyruvate synthase
EC number
CAS number 9082-51-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a pyruvate synthase (EC is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).

The relevant equilibrium catalysed by PFOR is:

pyruvate + CoA + oxidized ferredoxin acetyl-CoA + CO2 + reduced ferredoxin + 2 H+

The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 4 products are acetyl-CoA, CO2, reduced ferredoxin, and H+.


This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle (CO2 fixation).

Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters. This process links glycolysis to the Wood–Ljungdahl pathway.


This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use include:

  • pyruvate oxidoreductase,
  • pyruvate synthetase,
  • pyruvate:ferredoxin oxidoreductase, and
  • pyruvic-ferredoxin oxidoreductase.



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