2-oxoglutarate decarboxylase
2-oxoglutarate decarboxylase | |||||||||
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Identifiers | |||||||||
EC number | 4.1.1.71 | ||||||||
CAS number | 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 / EGO | ||||||||
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In enzymology, a 2-oxoglutarate decarboxylase (EC 4.1.1.71) is an enzyme that catalyzes the chemical reaction
- 2-oxoglutarate succinate semialdehyde + CO2
Hence, this enzyme has one substrate, 2-oxoglutarate, and two products, succinate semialdehyde and 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
- 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.
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