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Pyruvate synthase

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pyruvate synthase
Identifiers
EC no.1.2.7.1
CAS no.9082-51-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase. 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.

The relevant equilibrium catalysed by PFOR is:

pyruvate + CoA + 2 oxidized ferredoxin 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).

Crystallographic studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1B0P, 1KEK, 2C3M, 2C3O, 2C3P, 2C3U, 2C3Y, 2C42, 2PDA, and 2RAA.

Inhibitors

Amixicile is a potent inhibitor of pyruvate ferredoxin oxidoreductase and is in pre-clinincal studies to treat infections of Helicobacter pylori and Clostridium difficile.[1][2]

References

  1. ^ "Paul S. Hoffman : Research Description".
  2. ^ Warren; et al. "Amixicile: A novel inhibitor of pyruvate: ferredoxin oxidoreductase shows efficacy against Clostridium difficile in a mouse infection model. Antimicrob. Agents Chemother. 56:1403-1411". doi:10.1128/AAC.00360-12. {{cite journal}}: Cite journal requires |journal= (help); Explicit use of et al. in: |author= (help)