Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.12 additional information
-
 molecular weight of proteolytic fragments Escherichia coli
2.3.1.12 60100 64500 sedimentation equilibrium, depending on buffer Escherichia coli
2.3.1.12 78000
-
 SDS-PAGE Escherichia coli
2.3.1.12 1548000
-
 native enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.12 dihydrolipoamide + acetyl-CoA Escherichia coli
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Escherichia coli
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.12 lipoprotein
-
 Escherichia coli

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.12 dihydrolipoamide + acetyl-CoA
-
 Escherichia coli S-acetyldihydrolipoamide + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.12 polymer
-
 Escherichia coli