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Literature summary for 2.3.1.12 extracted from

  • Smolle, M.; Prior, A.E.; Brown, A.E.; Cooper, A.; Byron, O.; Lindsay, J.G.
    A new level of architectural complexity in the human pyruvate dehydrogenase complex (2006), J. Biol. Chem., 281, 19772-19780.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens P10515
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Subunits

Subunits Comment Organism
More evidence for a novel subunit organization in which dihydrolipoamide dehydrogenase E3 and E3BP form subcomplexes with a 1:2 stoichiometry implying the existence of a network of dihydrolipoamide dehydrogenase cross-bridges linking pairs of E3-binding proteins across the surface of the dihydrolipoamide acetyltransferase E2 core assembly. One of the E3-binding protein lipoyl domains docks into the dihydrolipoamide dehydrogenase E3 active site Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrolipoamide acetyltransferase
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Homo sapiens