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Literature summary for 2.3.1.12 extracted from

  • Bleile, D.M.; Munk, P.; Oliver, R.M.; Reed, L.J.
    Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli (1979), Proc. Natl. Acad. Sci. USA, 76, 4385-4389.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
molecular weight of proteolytic fragments Escherichia coli
60100 64500 sedimentation equilibrium, depending on buffer Escherichia coli
78000
-
SDS-PAGE Escherichia coli
1548000
-
native enzyme 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

Purification (Commentary)

Purification (Comment) Organism
pyruvate dehydrogenase complex and tryptic fragments of E2 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
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
-
Escherichia coli