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Literature summary for 1.8.1.4 extracted from

  • Reed, L.J.; Willms, C.R.
    Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli) (1966), Methods Enzymol., 9, 247-265.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
arsenite in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols Escherichia coli
Cd2+ in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
Escherichia coli lipoamide + NADH
-
?

Cofactor

Cofactor Comment Organism Structure
FAD 2 molecules of FAD per molecule of enzyme Escherichia coli
NAD+
-
Escherichia coli