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Literature summary extracted from

  • Mailloux, R.J.; Gardiner, D.; OBrien, M.
    2-Oxoglutarate dehydrogenase is a more significant source of O2(-)/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue (2016), Free Radic. Biol. Med., 97, 501-512.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.4.2 mitochondrion
-
 Sus scrofa 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.4.2 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Sus scrofa
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.2 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.4.2 heart
-
 Sus scrofa
-
1.2.4.2 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.2 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Sus scrofa [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.4.2 2-oxoglutarate dehydrogenase
-
 Sus scrofa
1.2.4.2 OGDH
-
 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.2 FAD
-
 Sus scrofa
1.2.4.2 thiamine diphosphate
-
 Sus scrofa

General Information

EC Number General Information Comment Organism
1.2.4.2 physiological function the enzyme is a potent source of reactive oxygen species in liver and cardiac tissue Sus scrofa