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Updated: Jul 4, 2026

One-step Metabolomics: Carbohydrates, Organic and Amino Acids Quantified in a Single Procedure
Published on: June 25, 2010
[L-2-hydroxyglutaric aciduria, an error of metabolism]
1Laboratoire de Chimie physiologique, de Duve Institute et U.C.L.
Abstract:
The neurometabolic disorder L-2-hydroxyglutaric aciduria was recently shown to be due to a defect in L-2-hydroxyglutarate dehydrogenase. This FAD-linked enzyme catalyses the irreversible conversion of L-2-hydroxyglutarate to alpha-ketoglutarate. The formation of L-2-hydroxyglutarate results from a side-activity of mitochondrial L-malate dehydrogenase, the enzyme which normally catalyses the interconversion of oxaloacetate and L-malate, but which also catalyses the NADH-dependent conversion of alpha-ketoglutarate to L-2-hydroxyglutarate. Though very slow, this activity accounts for the in vivo formation of L-2-hydroxyglutarate. As the latter compound is most likely toxic, L-2-hydroxyglutarate dehydrogenase catalyses a metabolite repair reaction.
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