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Literature summary for 1.8.1.4 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
Search for more literature for 1.8.1.4

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa P09623
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
LADH
-
 Sus scrofa
lipoamide dehydrogenase
-
 Sus scrofa

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Sus scrofa
NAD+
-
 Sus scrofa