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Literature summary extracted from

  • Klyachko, N.L.; Shchedrina, V.A.; Efimov, A.V.; Kazakov, S.V.; Gazaryan, I.G.; Kristal, B.S.; Brown, A.M.
    pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification (2005), J. Biol. Chem., 280, 16106-16114.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.4 52000
-
 2 * 52000, present at pH 5.8 and 7.5, active at pH 7.5 Sus scrofa
1.8.1.4 54000
-
 1 * 54000, only present and active at pH 5.8 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Sus scrofa P09623
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 Sephadex G-25 column gel filtration Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.4 heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Sus scrofa lipoamide + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.1.4 dimer 2 * 52000, present at pH 5.8 and 7.5, active at pH 7.5 Sus scrofa
1.8.1.4 monomer 1 * 54000, only present and active at pH 5.8 Sus scrofa
1.8.1.4 tetramer present at pH 5.8 and 7.5, active at pH 7.5 Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 LADH
-
 Sus scrofa
1.8.1.4 lipoamide dehydrogenase
-
 Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 5.8
-
 monomeric enzyme Sus scrofa
1.8.1.4 7.5
-
 tetrameric and dimeric enzyme Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
 Sus scrofa
1.8.1.4 NAD+
-
 Sus scrofa