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Literature summary for 2.3.1.12 extracted from

  • Hanemaaijer, R.; de Kok, A.; Jolles, J.; Veeger, C.
    The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii (1987), Eur. J. Biochem., 169, 245-252.
    View publication on PubMed
Search for more literature for 2.3.1.12

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 Azotobacter vinelandii
63000
-
 sedimentation equilibrium Azotobacter vinelandii
83000
-
 SDS-PAGE Azotobacter vinelandii
530000
-
-
 Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
proteolytic fragments, isolation of lipoyl domain and catalytic domain Azotobacter vinelandii

Storage Stability

Storage Stability Organism
liquid nitrogen, 50 mM potassium phosphate buffer pH 7.0, 0.5 mM EDTA, 0.05 mM phenylmethylsulfonylfluoride Azotobacter vinelandii

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
polymer
-
 Azotobacter vinelandii