Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q96HY7 and Q02218 | Q96HY7 i.e. E1 component of the 2-oxoadipate dehydrogenase complex, Q02218 i.e. E1 component of the 2-oxoglutarate dehydrogenase complex, cf. EC 1.2.4.2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine | - |
Homo sapiens | [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2 | - |
? | |
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine | - |
Homo sapiens | [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DHTKD1 | - |
Homo sapiens |
E1a | - |
Homo sapiens |
OGDH | cf. EC 1.2.4.2 | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the 2-oxoadipate dehydrogenase E1a uses the dihydrolipoyl succinyltransferase (E2o) and the dihydrolipoyl dehydrogenase (E3) components of the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex (OGDHc) for its activity. 2-Oxoglutarate and 2-oxoadipate can be oxidized by E1a, E1a displays an approximately 49fold preference in catalytic efficiency for 2-oxoadipate over 2-oxoglutarate. E1a forms the thiamidiphosphate-enamine radical from 2-oxoadipate in the oxidative half reaction, and may produce superoxide and H2O2 from decarboxylation of 2-oxoadipate in the forward physiological direction. Once assembled to complex with the same E2o and E3 components, the E1o and E1a display strikingly different regulation: both succinyl-CoA and glutaryl-CoA significantly reduced the E1o activity, but not the activity of E1a | Homo sapiens |