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Pyruvate synthase
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Pyruvate synthase : ウィキペディア英語版
Pyruvate synthase

In enzymology, a pyruvate synthase () 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 \rightleftharpoons 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+.
== Function ==

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

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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