In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate (TPP) but relies on lipoate as the electron acceptor.

Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters.

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.

Other names in common use include: PFOR adopts a dimeric structure, while each monomeric subunit is composed of one or multiple chain(s) of polypeptides.

[2] An PFOR reaction starts with the nucleophilic attack of C2 of TPP on the 2-oxo carbon of pyruvate, which forms a lactyl-TPP adduct.