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Literature summary for 1.2.1.105 extracted from

  • Kanzaki, T.; Hayakawa, T.; Hamada, M.; Fukuyoshi, Y.; Koike, M.
    Mammalian alpha-keto acid dehydrogenase complexes. IV. Substrate specificities and kinetic properties of the pig heart pyruvate and 2-oxoglutarate dehydrogenase complexes (1969), J. Biol. Chem., 244, 1183-1187.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-oxo-3-methylpentanoate 2-oxoglutarate dehydrogenase complex Sus scrofa
2-oxoglutarate 2-oxoglutarate dehydrogenase complex Sus scrofa
2-Oxoisohexanoate 2-oxoglutarate dehydrogenase complex Sus scrofa
2-oxoisopentanoate 2-oxoglutarate dehydrogenase complex Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + lipoamide
-
Sus scrofa S-succinyldihydrolipoamide + CO2
-
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