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Literature summary for 2.3.1.12 extracted from

  • Henney, H.R.; Willms, C.R.; Muramatsu, T.; Mukherjee, B.B.; Reed, L.J.
    alpha-Keto acid dehydrogenase complexes. VII. Isolation and partial characterization of the polypeptide chains in the dihydrolipoyl transacetylase of Escherichia coli (1967), J. Biol. Chem., 242, 898-901.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
24 * 36000, linked by noncovalent bonds Escherichia coli
1000000
-
sedimentation equilibrium centrifugation 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 1 molecule lipoic acid per polypeptide chain Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
-
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 * 36000, linked by noncovalent bonds Escherichia coli