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Literature summary for 2.3.1.12 extracted from

  • Bleile, D.M.; Hackert, M.L.; Pettit, F.H.; Reed, L.J.
    Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart (1981), J. Biol. Chem., 256, 514-519.
    View publication on PubMed
Search for more literature for 2.3.1.12

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 molecular weight of proteolytic fragments Bos taurus
74000
-
 SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Bos taurus
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein
-
 Bos taurus

Purification (Commentary)

Purification (Comment) Organism
purification of tryptic fragments Bos taurus

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of pyruvate dehydrogenase complex Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
 Bos taurus S-acetyldihydrolipoamide + CoA
-
 ?

Subunits

Subunits Comment Organism
polymer domain structure of subunits: lipoyl domain MW 28000, subunit binding domain MW 26000, sedimentation equilibrium Bos taurus