2-oxoglutarate decarboxylase
| 2-oxoglutarate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 2-oxoglutarate decarboxylase heterotetramer, Mycobacterium smegmatis | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.1.71 | ||||||||
| CAS no. | 37205-42-8 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme 2-oxoglutarate decarboxylase (EC 4.1.1.71) catalyzes the chemical reaction: 2-oxoglutarate succinate semialdehyde + CO2
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming). Other names in common use include oxoglutarate decarboxylase, alpha-ketoglutarate decarboxylase, alpha-ketoglutaric decarboxylase, oxoglutarate decarboxylase, pre-2-oxoglutarate decarboxylase, and 2-oxoglutarate carboxy-lyase. It employs one cofactor, thiamin diphosphate.
References
[edit]- Shigeoka S, Onishi T, Maeda K, Nakano Y, Kitaoka S (1986). "Occurrence of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in mitochondria of Euglena gracilis". FEBS Lett. 195: 43–47. doi:10.1016/0014-5793(86)80126-0.
