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Literature summary for 1.8.1.4 extracted from

  • Richarme, G.
    Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli (1989), J. Bacteriol., 171, 6580-6585.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
dihydrolipoamide
-
Escherichia coli
0.15
-
NAD+
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
x * 46000, SDS-PAGE Escherichia coli
88000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the most important function of dehydrolipoamide dehydrogenase as a component of the pyruvate dehydrogenase and the 2-oxoglutarate dehydrogenase complex is the implication in the oxidative decarboxylation of pyruvate and 2-oxoglutarate ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
Escherichia coli lipoamide + NADH
-
?
additional information the most important function of dehydrolipoamide dehydrogenase as a component of the pyruvate dehydrogenase and the 2-oxoglutarate dehydrogenase complex is the implication in the oxidative decarboxylation of pyruvate and 2-oxoglutarate Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer x * 46000, SDS-PAGE Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli