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Literature summary extracted from

  • Millar, A.H.; Leaver, C.J.; Hill, S.A.
    Characterization of the dihydrolipoamide acetyltransferase of the mitochondrial pyruvate dehydrogenase complex from potato and comparisons with similar enzymes in diverse plant species (1999), Eur. J. Biochem., 264, 973-981.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.12 additional information
-
molecular weight of proteolytic fragments Solanum tuberosum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.12 dihydrolipoamide + acetyl-CoA Solanum tuberosum
-
S-acetyldihydrolipoamide + CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Solanum tuberosum
-
potato
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.12
-
Solanum tuberosum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.12 dihydrolipoamide + acetyl-CoA
-
Solanum tuberosum S-acetyldihydrolipoamide + CoA
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.12 More treatment with NaCl results in 2 fractions with E2 activity, MW 55000 and MW 78000, SDS-PAGE, gel filtration Solanum tuberosum
2.3.1.12 polymer stoichiometry of pyruvate dehydrogenase complexes Solanum tuberosum