The
enzyme 4-hydroxy-2-oxoglutarate aldolase ()
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction
:4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
This enzyme belongs to the family of
lyase
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. ...
s, 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 Glyoxylate and dicarboxylate metabolism describes a variety of reactions involving glyoxylate or dicarboxylates. Glyoxylate is the conjugate base of glyoxylic acid, and within a buffered environment of known pH such as the cell cytoplasm these ter ...
.
Structural studies
As of late 2007, two
structures have been solved for this class of enzymes, with
PDB accession codes and .
References
*
*
*
* Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.
EC 4.1.3
Enzymes of known structure
{{4.1-enzyme-stub