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Literature summary for 1.2.1.105 extracted from

  • Nemeria, N.S.; Gerfen, G.; Yang, L.; Zhang, X.; Jordan, F.
    Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the L-lysine, L-hydroxylysine and L-tryptophan degradation pathways from studies in vitro (2018), Biochim. Biophys. Acta Bioenerg., 1859, 932-939 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
assembly of the complex from the individually expressed components in vitro Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 2-oxoglutarate component E1, pH 7.5, 37°C Homo sapiens
0.107
-
 2-oxoadipate component E1, pH 7.5, 37°C Homo sapiens
0.15
-
 2-oxoglutarate recombinant enzyme complex, pH 7.5, 37°C Homo sapiens
0.52
-
 2-oxoadipate recombinant enzyme complex, pH 7.5, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens A0A024R713 and A0A024R6C9 A0A024R713 i.e dihydrolipoyl dehydrogenase component E3, cf. EC 1.8.1.4, A0A024R6C9 i.e. dihydrolipoyllysine-residue succinyltransferase component E2, cf. EC 2.3.1.61
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.37
-
 component E1, pH 7.5, 37°C Homo sapiens
5.63
-
 recombinant enzyme complex, pH 7.5, 37°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoadipate + CoA + NAD+
-
 Homo sapiens glutaryl-CoA + CO2 + NADH
-
 ?
2-oxoglutarate + CoA + NAD+
-
 Homo sapiens succinyl-CoA + CO2 + NADH
-
 ?

General Information

General Information Comment Organism
physiological function functional and regulatory crosstalk between the 2-oxoglutarate dehydrogenase complex, and a 2-oxoadipate dehydrogenase complex from the final degradation pathway of L-lysine, L-hydroxylysine and L-tryptophan. The two complexes share the same dihydrolipoyl succinyltransferase (E2) and dihydrolipoyl dehydrogenase (E3) components but display different substrate preferences and different binding modes. Similarly to E1o, the E1a also forms the thiamine diphosphate-enamine radical from 2-oxoadipate in the oxidative half reaction. Both complexes produced superoxide/H2O2 from O2 in the reductive half reaction Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1
-
 2-oxoadipate component E1, pH 7.5, 37°C Homo sapiens
8.1
-
 2-oxoadipate recombinant enzyme complex, pH 7.5, 37°C Homo sapiens
82
-
 2-oxoglutarate component E1, pH 7.5, 37°C Homo sapiens
142
-
 2-oxoglutarate recombinant enzyme complex, pH 7.5, 37°C Homo sapiens