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Literature summary 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

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 Azotobacter vinelandii
2.3.1.12 63000
-
 sedimentation equilibrium Azotobacter vinelandii
2.3.1.12 83000
-
 SDS-PAGE Azotobacter vinelandii
2.3.1.12 530000
-
-
 Azotobacter vinelandii

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 Azotobacter vinelandii
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Azotobacter vinelandii
-
-
-

Purification (Commentary)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.3.1.12 polymer
-
 Azotobacter vinelandii