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Literature summary for 2.3.1.12 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)

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
864000
-
crystallization experiments Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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