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Literature summary for 2.3.1.12 extracted from

  • Schwartz, E.R.; Reed, L.J.
    alpha-Keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia coli (1969), J. Biol. Chem., 244, 6074-6079.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-Acetylimidazole modifies tyrosyl residues and dissociates the enzyme into subunits Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
24 * 40000, linked by noncovalent bonds 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of pyruvate dehydrogenase complex, stoichiometry pyruvate dehydrogenase:transacetylase:flavoprotein is 1:0.35:0.4 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 * 40000, linked by noncovalent bonds Escherichia coli