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Literature summary for 1.1.99.39 extracted from

  • Toplak, M.; Brunner, J.; Schmidt, J.; Macheroux, P.
    Biochemical characterization of human D-2-hydroxyglutarate dehydrogenase and two disease related variants reveals the molecular cause of D-2-hydroxyglutaric aciduria (2019), Biochim. Biophys. Acta, 1867, 140255 .
    View publication on PubMed
Search for more literature for 1.1.99.39

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
I147S D-2-hydroxyglutaric aciduria disease-related variant. The cofactor binding site is compromised by the single amino acid replacement. The variant forms aggregates that are unable to bind the FAD cofactor Homo sapiens
V444A D-2-hydroxyglutaric aciduria disease-related variant. The cofactor binding site is compromised by the single amino acid replacement. The variant forms aggregates that are unable to bind the FAD cofactor Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-2-hydroxyglutarate + electron transfer flavoprotein Homo sapiens
-
 2-oxoglutarate + reduced electron transfer flavoprotein
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8N465
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-hydroxyglutarate + electron transfer flavoprotein
-
 Homo sapiens 2-oxoglutarate + reduced electron transfer flavoprotein
-
 ?

Synonyms

Synonyms Comment Organism
D2HGDH
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function the enzyme directly reduces recombinant human electron transferring flavoprotein (ETF), thus establishing a metabolic link between the oxidation of D-2-hydroxyglutarate and the mitochondrial electron transport chain Homo sapiens