2-hydroxy-3-oxoadipate synthase (EC 2.2.1.5) is an enzyme that catalyzes the following chemical reaction:
| 2-hydroxy-3-oxoadipate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.2.1.5 | ||||||||
| CAS no. | 9054-72-2 | ||||||||
| 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 two substrates of this enzyme are α-ketoglutaric acid and glyoxylic acid. Its products are 2-hydroxy-3-oxoadipic acid and carbon dioxide.[1][2] The product can spontaneously decarboxylate to give 5-hydroxy-4-oxo-pentanoic acid:[3]
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). Other names in common use include 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating), alpha-ketoglutaric-glyoxylic carboligase, and oxoglutarate: glyoxylate carboligase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, thiamin diphosphate.[4]
References
edit- ↑ Schlossberg MA, Richert DA, Bloom RJ, Westerfeld WW (1968). "Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of alpha-ketoglutarate: glyoxylate carboligase". Biochemistry. 7 (1): 333–7. doi:10.1021/bi00841a042. PMID 4320439.
- ↑ Stewart PR, Quayle JR (1967). "The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria". Biochem. J. 102 (3): 885–897. doi:10.1042/bj1020885. PMC 1270340. PMID 16742506.
- ↑ Schlossberg MA, Bloom RJ, Richert DA, Westerfeld WW (1970). "Carboligase activity of alpha-ketoglutarate dehydrogenase". Biochemistry. 9 (5): 1148–53. doi:10.1021/bi00807a015. PMID 5418712.
- ↑ Enzyme 2.2.1.5 at KEGG Pathway Database.
