4-hydroxy-2-oxoglutarate aldolase

From Wikipedia, the free encyclopedia

In enzymology, a 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) is an enzyme that catalyzes the chemical reaction

4-hydroxy-2-oxoglutarate $\rightleftharpoons$ pyruvate + glyoxylate

Hence, this enzyme has one substrate, 4-hydroxy-2-oxoglutarate, and two products, pyruvate and 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WAU and 2C0A.

[edit] References

IUBMB entry for 4.1.3.16
BRENDA references for 4.1.3.16 (Recommended.)
PubMed references for 4.1.3.16
PubMed Central references for 4.1.3.16
Google Scholar references for 4.1.3.16
KURATOMI K, FUKUNAGA K (1963). "THE METABOLISM OF GAMMA-HYDROXYGLUTAMATE IN RAT LIVER. I. ENZYMIC SYNTHESIS OF GAMMA-HYDROXY-ALPHA-KETOGLUTARATE FROM PYRUVATE AND GLYOXYLATE". Biochim. Biophys. Acta. 78: 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: 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: 5079–87. PMID 4560498.
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.