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Literature summary for 2.3.1.12 extracted from

  • Bisswanger, H.; Henning, U.
    A new dihydrolipoamide transacetylase in Escherichia coli K12 (1973), Biochim. Biophys. Acta, 321, 143-148.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2
-
dihydrolipoamide
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
no component of pyruvate dehydrogenase complex, sucrose density gradient 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
-
K-12, wild-type and mutant strains
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
specific activity after growth on various carbon sources 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
dimer multimer formation is probably lost by loss of a small segment during genetic rearrangement Escherichia coli