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Literature summary extracted from

  • Chandrasekhar, K.; Wang, J.; Arjunan, P.; Sax, M.; Park, Y.H.; Nemeria, N.S.; Kumaran, S.; Song, J.; Jordan, F.; Furey, W.
    Insight to the interaction of the dihydrolipoamide acetyltransferase (E2) core with the peripheral components in the Escherichia coli pyruvate dehydrogenase complex via multifaceted structural approaches (2013), J. Biol. Chem., 288, 15402-15417.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.4.1
-
 Escherichia coli
2.3.1.12 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.12 K191E the mutant shows 50% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 K191R the mutant shows 79% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R129A the mutant shows 34% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R129E the mutant shows 3.0% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R129K the mutant shows 77% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R130A the mutant shows wild type activity Escherichia coli
2.3.1.12 R130E the mutant shows 57% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R150A the mutant shows 8.0% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R150E the mutant shows 2.4% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R150K the mutant shows 5.0% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R153E the mutant shows 60% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R153K the mutant shows 83% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R161A the mutant shows 65% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R161E the mutant shows 84% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R202E the mutant shows 10% activity compared to the wild type enzyme Escherichia coli
2.3.1.12 R202K the mutant shows 86% activity compared to the wild type enzyme Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.4.1 99474
-
 x * 99474, calculated from amino acid sequence Escherichia coli
2.3.1.12 65959
-
 x * 65959, calculated from amino acid sequence Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.12 acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine Escherichia coli
-
 CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.1 Escherichia coli
-
-
-
2.3.1.12 Escherichia coli P06959
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.1
-
 Escherichia coli
2.3.1.12 nickel affinity column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.1 pyruvate + pyruvate dehydrogenase complex subunit E2p
-
 Escherichia coli ?
-
 ?
2.3.1.12 acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
-
 Escherichia coli CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.4.1 ? x * 99474, calculated from amino acid sequence Escherichia coli
2.3.1.12 ? x * 65959, calculated from amino acid sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.2.4.1 E1p
-
 Escherichia coli
1.2.4.1 thiamin diphosphate-dependent pyruvate dehydrogenase
-
 Escherichia coli
2.3.1.12 dihydrolipoamide acetyltransferase
-
 Escherichia coli
2.3.1.12 pyruvate dehydrogenase complex component E2
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.1 thiamine diphosphate dependent on Escherichia coli