+ 2 reduced
ferredoxin
2-oxoglutarate synthase
| 2-oxoglutarate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.7.3 | ||||||||
| CAS no. | 37251-05-1 | ||||||||
| 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, 2-oxoglutarate synthase (EC 1.2.7.3) is an enzyme that catalyzes the chemical reaction
The substrates of this enzyme are succinyl-CoA, reduced ferredoxin, carbon dioxide and two protons. Its products are 2-oxoglutaric acid, coenzyme A, and oxidized ferredoxin. This reaction is part of the reverse Krebs cycle, as a means of carbon fixation.[1][2][3]
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 2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating). Other names in common use include 2-ketoglutarate ferredoxin oxidoreductase, 2-oxoglutarate:ferredoxin oxidoreductase, KGOR, 2-oxoglutarate ferredoxin oxidoreductase, and 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating). In the direction from 2-oxoglutaric acid to succinyl-CoA the enzyme is part of the citric acid cycle.[4][5][6]
References
- ^ Enzyme 1.2.7.3 at KEGG Pathway Database.
- ^ Buchanan BB, Evans MC (1965). "The synthesis of alpha-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium". Proc. Natl. Acad. Sci. U.S.A. 54 (4): 1212–8. Bibcode:1965PNAS...54.1212B. doi:10.1073/pnas.54.4.1212. PMC 219840. PMID 4286833.
- ^ Gehring U, Arnon DI (1972). "Purification and properties of -ketoglutarate synthase from a photosynthetic bacterium". J. Biol. Chem. 247 (21): 6963–9. doi:10.1016/S0021-9258(19)44680-2. PMID 4628267.
- ^ Dorner E, Boll M (2002). "Properties of 2-Oxoglutarate:Ferredoxin Oxidoreductase from Thauera aromatica and Its Role in Enzymatic Reduction of the Aromatic Ring". J. Bacteriol. 184 (14): 3975–83. doi:10.1128/JB.184.14.3975-3983.2002. PMC 135165. PMID 12081970.
- ^ Mai X, Adams MW (1996). "Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis". J. Bacteriol. 178 (20): 5890–6. doi:10.1128/jb.178.20.5890-5896.1996. PMC 178443. PMID 8830683.
- ^ Schut GJ, Menon AL, Adams MW (2001). "2-keto acid oxidoreductases from Pyrococcus furiosus and Thennococcus litoralis". Hyperthermophilic enzymes Part B. Methods in Enzymology. Vol. 331. pp. 144–58. doi:10.1016/S0076-6879(01)31053-4. ISBN 978-0-12-182232-3. PMID 11265457.