2-oxoglutarate carboxylase
| 2-oxoglutarate carboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.4.1.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 2-oxoglutarate carboxylase (EC 6.4.1.7) is an enzyme that catalyzes the chemical reaction
- ATP + 2-oxoglutarate + HCO3- ADP + phosphate + oxalosuccinate
The 3 substrates of this enzyme are ATP, 2-oxoglutarate, and HCO3-, whereas its 3 products are ADP, phosphate, and oxalosuccinate.
This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. The systematic name of this enzyme class is '. Other names in common use include oxalosuccinate synthetase', carboxylating factor for ICDH (incorrect), CFI, and OGC.
References
- Aoshima M, Ishii M, Igarashi Y (2004). "A novel biotin protein required for reductive carboxylation of 2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus TK-6". Mol. Microbiol. 51 (3): 791–8. doi:10.1046/j.1365-2958.2003.03863.x. PMID 14731279.
- Aoshima M, Igarashi Y (2006). "A novel oxalosuccinate-forming enzyme involved in the reductive carboxylation of 2-oxoglutarate in Hydrogenobacter thermophilus TK-6". Mol. Microbiol. 62 (3): 748–59. doi:10.1111/j.1365-2958.2006.05399.x. PMID 17076668.
This article is issued from Wikipedia - version of the 5/12/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.