4-hydroxy-2-oxoglutarate aldolase
| 4-hydroxy-2-oxoglutarate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.16 | ||||||||
| CAS no. | 9030-81-3 | ||||||||
| 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 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) catalyzes the chemical reaction
- 4-hydroxy-2-oxoglutarate pyruvate + glyoxylate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming). Other names in common use include 2-oxo-4-hydroxyglutarate aldolase, hydroxyketoglutaric aldolase, 4-hydroxy-2-ketoglutaric aldolase, 2-keto-4-hydroxyglutaric aldolase, 4-hydroxy-2-ketoglutarate aldolase, 2-keto-4-hydroxyglutarate aldolase, 2-oxo-4-hydroxyglutaric aldolase, DL-4-hydroxy-2-ketoglutarate aldolase, hydroxyketoglutarate aldolase, 2-keto-4-hydroxybutyrate aldolase, and 4-hydroxy-2-oxoglutarate glyoxylate-lyase. This enzyme participates in arginine and proline metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WAU and 2C0A.
References
- KURATOMI K, FUKUNAGA K (1963). "The metabolism of γ-hydroxyglutamate in rat liver I. Enzymic synthesis of γ-hydroxy-α-ketoglutarate from pyruvate and glyoxylate". Biochim. Biophys. Acta. 78 (4): 617–28. doi:10.1016/0006-3002(63)91027-8. PMID 14089442.
- Lane RS, Shapley A, Dekker EE (1971). "2-keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserine". Biochemistry. 10 (8): 1353–64. doi:10.1021/bi00784a013. PMID 5580656.
- Nishihara H, Dekker EE (1972). "Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase". J. Biol. Chem. 247 (16): 5079–87. PMID 4560498.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.
