We are analyzing https://link.springer.com/article/10.1007/s10545-007-0487-0.

Title:
l-2-Hydroxyglutaric aciduria, a defect of metabolite repair | Journal of Inherited Metabolic Disease
Description:
l-2-hydroxyglutaric aciduria is a metabolic disorder in which l-2-hydroxyglutarate accumulates as a result of a deficiency in FAD-linked l-2-hydroxyglutarate dehydrogenase, a mitochondrial enzyme converting l-2-hydroxyglutarate to α-ketoglutarate. The origin of the l-2-hydroxyglutarate, which accumulates in this disorder, is presently unknown. The oxidation–reduction potential of the 2-hydroxyglutarate/α-ketoglutarate couple is such that l-2-hydroxyglutarate could potentially be produced through the reduction of α-ketoglutarate by a NAD- or NADP-linked oxidoreductase. In fractions of rat liver cytosolic extracts that had been chromatographed on an anion exchanger we detected an enzyme reducing α-ketoglutarate in the presence of NADH. This enzyme co-purified with cytosolic l-malate dehydrogenase (cMDH) upon further chromatography on Blue Sepharose. Mitochondrial fractions also contained an NADH-linked, ‘α-ketoglutarate reductase’ which similarly co-purified with mitochondrial l-malate dehydrogenase (mMDH). Purified mMDH catalysed the reduction of α-ketoglutarate to l-2-hydroxyglutarate with a catalytic efficiency that was about 107-fold lower than that observed with oxaloacetate. For the cytosolic enzyme, this ratio amounted to 108, indicating that this enzyme is more specific. Both cMDH and mMDH are highly active in tissues and α-ketoglutarate is much more abundant than oxaloacetate and more concentrated in mitochondria than in the cytosol. As a result of this, the weak activity of mMDH on α-ketoglutarate is sufficient to account for the amount of l-2-hydroxyglutarate that is excreted by patients deficient in FAD-linked l-2-hydroxyglutarate dehydrogenase. The latter enzyme appears, therefore, to be responsible for a ‘metabolite repair’ phenomenon and to belong to the expanding class of ‘house-cleaning’ enzymes.
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28 years and 1 months (reg. 1997-05-29).

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Topics {✒️}

fad-linked l-2-hydroxyglutarate dehydrogenase mitochondrial l-malate dehydrogenase month download article/chapter +-dependent malate dehydrogenase cytosolic l-malate dehydrogenase inherited metabolic disease blue sepharose free nicotinamide–adenine dinucleotide severe neurodegenerative disease 2-hydroxyglutarate/α-ketoglutarate couple o-methyltransferase-deficient mice veiga-da-cunha alpha-hydroxyglutaric acid synthetase enzyme reducing α-ketoglutarate inherited neurometabolic disease cerebral metabolic state fructosamine-3-kinase deficient mice full article pdf l-2-hydroxyacid dehydrogenase mitochondrial metabolism l-2-hydroxyglutaric aciduria privacy choices/manage cookies malate–aspartate shuttle 2-hydroxyglutaric acid present l-2-hydroxyglutarate accumulates l-2-hydroxyglutaric acidemia l-2-hydroxyglutaric acidaemia malic dehydrogenase homogeneous lactic dehydrogenase α-hydroxyglutaric acid declared references related subjects malic enzyme nadp-linked oxidoreductase malate dehydrogenase �α-ketoglutarate reductase human mitochondrial nad rat skeletal muscle rat-liver tissue european economic area compound heterozygous mutation isolated subcellular membranes intracellular distribution patterns intracellular deglycation pathway complete compression ischemia methionine sulfoxide reductases fatal progressive epilepsy l-2-hydroxyglutarate protein–dye binding increased protein glycation

Questions {❓}

Duran M, Kamerling JP, Bakker HD, van Gennip AH, Wadman SK (1980) l-2-Hydroxyglutaric aciduria: an inborn error of metabolism?

Schema {🗺️}

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         Hydroxyglutarate
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         Dependent Malic Enzyme
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         Human Genetics
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         Internal Medicine
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