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Literature summary for 1.2.1.104 extracted from

  • Hiromasa, Y.; Fujisawa, T.; Aso, Y.; Roche, T.E.
    Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components (2004), J. Biol. Chem., 279, 6921-6933.
    View publication on PubMed
Search for more literature for 1.2.1.104

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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 Bos taurus 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus E1 is bound to E2, both components of the pyruvate dehydrogenase multienzyme complex PDC, via the E1-binding B domain of E2, enzyme component organization in the pyruvate dehydrogenase multienzyme complex, regulatory role, overview ?
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 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
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 E1 component of the pyruvate dehydrogenase multienzyme complex
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Source Tissue

Source Tissue Comment Organism Textmining
heart
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 Bos taurus
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kidney
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 Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information E1 is bound to E2, both components of the pyruvate dehydrogenase multienzyme complex PDC, via the E1-binding B domain of E2, enzyme component organization in the pyruvate dehydrogenase multienzyme complex, regulatory role, overview Bos taurus ?
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 ?

Subunits

Subunits Comment Organism
More enzyme component organization and binding structures in the pyruvate dehydrogenase multienzyme complex, core is formed by compoenents E2 and E3, regulatory role Bos taurus