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

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
2.3.1.12
-
 Escherichia coli
2.3.1.12
-
 Azotobacter vinelandii

Crystallization (Commentary)

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

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 additional information
-
 molecular weight of proteolytic fragments Azotobacter vinelandii
2.3.1.12 670000
-
 gel filtration Escherichia coli
2.3.1.12 670000
-
 gel filtration 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 Escherichia coli
-
 S-acetyldihydrolipoamide + CoA
-
 ?
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
-
-
-
2.3.1.12 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.12 fusion protein of 6 amino acids form beta-galactosidase, the apa-4 region and the catalytic domain of E2 Escherichia coli
2.3.1.12 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.12 47.1
-
 catalytic domain Escherichia coli
2.3.1.12 119
-
 catalytic domain Azotobacter vinelandii

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

Subunits

EC Number Subunits Comment Organism
2.3.1.12 polymer 24 subunits Escherichia coli
2.3.1.12 polymer 24 subunits Azotobacter vinelandii