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Literature summary for 2.3.1.12 extracted from

  • Butterworth, P.J.; Tsai, S.; Eley, M.H.; Roche, T.E.; Reed, L.J.
    A kinetic study of dihydrolipoyl transacetylase from bovine kidney (1975), J. Biol. Chem., 250, 1921-1925.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,2-diselenolane-3-valeric acid competitive with respect to dihydrolipoamide and non-competitive with respect to acetyl-CoA Bos taurus
CoA competitive to acetyl-CoA, non-competitive to dihydrolipoamide Bos taurus
lipoamidase complete loss of activity after 3 h Bos taurus
palmitoyl-CoA competitive to acetyl-CoA, non-competitive to dihydrolipoamide Bos taurus
S-acetyldihydrolipoamide competitive to dihydrolipoamide, non-competitive to acetyl-CoA Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03 0.1 acetyl-CoA
-
Bos taurus
0.13 0.4 dihydrolipoamide
-
Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Bos taurus acetyl group is transferred from the S-acetyldihydrolipoyl moiety bound covalently to the transacetylase to CoA S-acetyldihydrolipoamide + CoA
-
r

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein
-
Bos taurus

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine reaction mechanism Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
Bos taurus S-acetyldihydrolipoamide + CoA
-
r
dihydrolipoamide + acetyl-CoA acetyl group is transferred from the S-acetyldihydrolipoyl moiety bound covalently to the transacetylase to CoA Bos taurus S-acetyldihydrolipoamide + CoA
-
r