Jump to content

Pyruvate synthase

From Wikipedia, the free encyclopedia
This is an old revision of this page, as edited by Rjwilmsi (talk | contribs) at 10:38, 13 April 2012 (References: Journal cites (journal names):, using AWB (8060)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
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
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the chemical reaction

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).

Structural 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.

References

  • Evans MC, Buchanan BB (1965). "Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium". Proc. Natl. Acad. Sci. U.S.A. 53 (6): 1420–5. doi:10.1073/pnas.53.6.1420. PMC 219872. PMID 5217644.
  • Gehring U, Arnon DI (1972). "Purification and properties of -ketoglutarate synthase from a photosynthetic bacterium". J. Biol. Chem. 247 (21): 6963–9. PMID 4628267.
  • Uyeda K, Rabinowitz JC (1971). "Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme". J. Biol. Chem. 246 (10): 3111–9. PMID 5574389.
  • Uyeda K, Rabinowitz JC (1971). "Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism". J. Biol. Chem. 246 (10): 3120–5. PMID 4324891.
  • Charon MH, Volbeda A, Chabriere E, Pieulle L, Fontecilla-Camps JC (1999). "Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase". Curr. Opin. Struct. Biol. 9 (6): 663–9. doi:10.1016/S0959-440X(99)00027-5. PMID 10607667.{{cite journal}}: CS1 maint: multiple names: authors list (link)