EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.105 | assembly of the complex from the individually expressed components in vitro | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.105 | 0.017 | - |
2-oxoglutarate | component E1, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 0.107 | - |
2-oxoadipate | component E1, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 0.15 | - |
2-oxoglutarate | recombinant enzyme complex, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 0.52 | - |
2-oxoadipate | recombinant enzyme complex, pH 7.5, 37°C | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.2.1.105 | mitochondrion | - |
Homo sapiens | 5739 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.105 | 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 | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.2.1.105 | 0.37 | - |
component E1, pH 7.5, 37°C | Homo sapiens |
1.2.1.105 | 5.63 | - |
recombinant enzyme complex, pH 7.5, 37°C | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.105 | 2-oxoadipate + CoA + NAD+ | - |
Homo sapiens | glutaryl-CoA + CO2 + NADH | - |
? | |
1.2.1.105 | 2-oxoglutarate + CoA + NAD+ | - |
Homo sapiens | succinyl-CoA + CO2 + NADH | - |
? |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.2.1.105 | 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 |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.105 | 1.1 | - |
2-oxoadipate | component E1, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 8.1 | - |
2-oxoadipate | recombinant enzyme complex, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 82 | - |
2-oxoglutarate | component E1, pH 7.5, 37°C | Homo sapiens | |
1.2.1.105 | 142 | - |
2-oxoglutarate | recombinant enzyme complex, pH 7.5, 37°C | Homo sapiens |