Pyruvate synthase
| pyruvate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.7.1 | ||||||||
| CAS no. | 9082-51-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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
- ^ "Paul S. Hoffman : Research Description".
- ^ 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)
- 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)
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