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Literature summary for 2.3.1.12 extracted from

  • Machicao, F.; Wieland, O.H.
    Subunit structure of dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex from bovine kidney (1980), Hoppe-Seyler's Z. Physiol. Chem., 361, 1093-1106.
    View publication on PubMed
Search for more literature for 2.3.1.12

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 molecular weight of proteolytic fragments Bos taurus
70000
-
 SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Bos taurus
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein 30 polypeptide chains with 2 lipoyl domains each Bos taurus

Purification (Commentary)

Purification (Comment) Organism
from pyruvate dehydrogenase complex Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activity of native enzyme and proteolytic fragments in various experiments Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
 Bos taurus S-acetyldihydrolipoamide + CoA
-
 ?

Subunits

Subunits Comment Organism
polymer 30 * 70000, SDS-PAGE, each polypeptide chains has 2 domains Bos taurus