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Literature summary for 1.2.1.105 extracted from

  • Zhou, J.; Yang, L.; Ozohanics, O.; Zhang, X.; Wang, J.; Ambrus, A.; Arjunan, P.; Brukh, R.; Nemeria, N.S.; Furey, W.; Jordan, F.
    A multipronged approach unravels unprecedented protein-protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complex (2018), J. Biol. Chem., 293, 19213-19227 .
    View publication on PubMedView publication on EuropePMC
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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
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General Information

General Information Comment Organism
physiological function protein-protein interactions in the dehydrogenase complex. Fluorescence studies suggest a strong interaction for the E1-E2 subcomplex, but a much weaker interaction in the E1-E3 subcomplex, and fail to identify any interaction in the E2-E3 subcomplex. Hydrogen-deuterium exchange MS studies show interactions in the E1-E2 and E1-E3. The N-terminal region of E1, peptides 18YVEEM22 and 27ENPKSVHKSWDIF39 constitute the binding region responsible for the assembly of the E1 with both the E2 and E3 components into OGDH. A E2 region comprising residues from both a linker region and from the catalytic domain is critical for interacting with E1 Homo sapiens