Pyruvate synthase

In enzymology, a pyruvate synthase is an enzyme that catalyzes the chemical reaction


 * pyruvate + CoA + 2 oxidized ferredoxin $$\rightleftharpoons$$ acetyl-CoA + CO2 + 2 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 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. This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle (co2 fixation).

Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , and.