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Literature summary for 2.3.1.12 extracted from

  • Schulze, E.; Westphal, A.H.; Obmolova, G.; Mattevi, A.; Hol, W.G.; de Kok, A.
    The catalytic domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli. Expression, purification, properties and preliminary X-ray analysis (1991), Eur. J. Biochem., 201, 561-568.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli
-
Azotobacter vinelandii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Azotobacter vinelandii

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
additional information
-
molecular weight of proteolytic fragments Azotobacter vinelandii
670000
-
gel filtration Escherichia coli
670000
-
gel filtration Azotobacter vinelandii

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
-
?
dihydrolipoamide + acetyl-CoA Azotobacter vinelandii
-
S-acetyldihydrolipoamide + CoA
-
?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
fusion protein of 6 amino acids form beta-galactosidase, the apa-4 region and the catalytic domain of E2 Escherichia coli
fusion protein of 6 amino acids form beta-galactosidase, the papa-4 region and the catalytic domain of E2 Azotobacter vinelandii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
47.1
-
catalytic domain Escherichia coli
119
-
catalytic domain Azotobacter vinelandii

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
polymer 24 subunits Escherichia coli
polymer 24 subunits Azotobacter vinelandii