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Literature summary extracted from

  • Kale, S.; Ulas, G.; Song, J.; Brudvig, G.W.; Furey, W.; Jordan, F.
    Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex (2008), Proc. Natl. Acad. Sci. USA, 105, 1158-1163.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.2.4.1 E410K CC-bond formation is dramatically slowed down (10-fold compared with E1ec) in E401K, the loop dynamics apparently greatly influences covalent addition of substrate to the enzyme-bound thiamine diphosphate Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.4.1 100000
-
 2 * 100000, SDS-PAGE Escherichia coli
1.2.4.1 200000
-
 SDS-PAGE Escherichia coli

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.1 pyruvate + CoA + oxidized 2,6-dichlorophenolindophenol
-
 Escherichia coli acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.4.1 homodimer 2 * 100000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.2.4.1 E1 component of pyruvate dehydrogenase multienzyme complex
-
 Escherichia coli
1.2.4.1 E1ec
-
 Escherichia coli

Cofactor

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