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.

Structural studies

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

References

• KURATOMI K, FUKUNAGA K "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.
• Lane RS, Shapley A, Dekker EE "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.
• Nishihara H, Dekker EE "Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase". J. Biol. Chem. 247 5079–87.
• Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes