L-2-hydroxyglutarate dehydrogenase


In enzymology, L-2-hydroxyglutarate dehydrogenase is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are -2-hydroxyglutaric acid and an electron acceptor. Its products are α-ketoglutaric acid and the corresponding reduced acceptor. Enzymes which preferentially catalyze the conversion of the stereoisomer of 2-oxoglutarate also exist in both mammals and plants and are named D-2-hydroxyglutarate dehydrogenase. L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; L-2-hydroxyglutarate dehydrogenase is an example of a metabolite repair enzyme that oxidizes L-2-hydroxyglutarate back to 2-oxoglutarate.

Nomenclature

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is -2-hydroxyglutarate:acceptor 2-oxidoreductase. Other names in common use include:
  • -2-hydroxyglutarate: 2-oxidoreductase
  • alpha-hydroxyglutarate dehydrogenase
  • alpha-hydroxyglutarate dehydrogenase
  • alpha-hydroxyglutarate oxidoreductase
  • alpha-ketoglutarate reductase
  • hydroxyglutaric dehydrogenase
  • L-alpha-hydroxyglutarate dehydrogenase
  • L-alpha-hydroxyglutarate:NAD 2-oxidoreductase

Clinical significance

Deficiency in this enzyme in humans or in the model plant Arabidopsis thaliana leads to accumulation of L-2-hydroxyglutarate. In humans this results in the fatal neurometabolic disorder 2-Hydroxyglutaric aciduria whereas plants seem to be unaffected by elevated cellular concentrations of this compound