4-hydroxy-2-oxoglutarate aldolase

The enzyme 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) catalyzes the chemical reaction

4-hydroxy-2-oxoglutarate pyruvate + glyoxylate
4-hydroxy-2-oxoglutarate aldolase
Identifiers
EC no.4.1.3.16
CAS no.9030-81-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.