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Literature summary extracted from

  • Fuller, C.C.; Reed, L.J.; Oliver, R.M.; Hackert, M.L.
    Crystallization of a dihydrolipoyl transacetylase - dihydrolipoyl dehydrogenase subcomplex and its implications regarding the subunit structure of the pyruvate dehydrogenase complex from Escherichia coli (1979), Biochem. Biophys. Res. Commun., 90, 431-438.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.12 E2-E3 subcomplex of pyruvate dehydrogenase, E2: EC 2.3.1.12, E3: EC 1.8.1.4, various crystallization conditions Escherichia coli

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 864000
-
 crystallization experiments Escherichia coli

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 Escherichia coli
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Escherichia coli
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.12 lipoprotein
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.3.1.12 polymer 24 identical subunits, data from crystallographic, biochemical and electron microscopic methods Escherichia coli