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Literature summary for 2.3.1.168 extracted from

  • Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Chuang, D.T.
    Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex (2009), J. Biol. Chem., 284, 13086-13098.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed as recombinant protein in Escherichia coli Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Subunits

Subunits Comment Organism
More The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20. Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrolipoyl transacetylase enzyme is the E2 component of the human pyruvate dehydrogenase complex Homo sapiens
E2p E2p is a component of the human multienzyme pyruvate dehydrogenase complex Homo sapiens