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Literature summary for 1.2.4.1 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

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent Escherichia coli