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Literature summary for 1.8.1.4 extracted from

  • Smith, L.D.; Bungard, S.J.; Danson, M.J.; Hough, D.W.
    Dihydrolipoamide dehydrogenase from the Thermoacidophilic archaebacterium Thermoplasma acidophilum (1987), Biochem. Soc. Trans., 15, 1097.
No PubMed abstract available
Search for more literature for 1.8.1.4

Inhibitors

Inhibitors Comment Organism Structure
p-Aminophenyldichloroarsine inactivated only in presence of NADH and dihydrolipoamide, no significant loss of activity in absence of NADH and dihydrolipoamide Thermoplasma acidophilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.52
-
 NAD+
-
 Thermoplasma acidophilum
0.83
-
 dihydrolipoamide
-
 Thermoplasma acidophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
118000
-
 gel filtration Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermoplasma acidophilum the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.012
-
-
 Thermoplasma acidophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+ alternate oxidation and reduction of an intrachain disulfide bond Thermoplasma acidophilum lipoamide + NADH
-
 ?
additional information the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system Thermoplasma acidophilum ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Thermoplasma acidophilum