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Literature summary for 2.3.1.12 extracted from

  • McCartney, R.G.; Sanderson, S.J.; Lindsay, J.G.
    Refolding and reconstitution studies on the transacetylase-protein X (E2/X) subcomplex of the mammalian pyruvate dehydrogenase complex: Evidence for specific binding of the dihydrolipoamide dehydrogenase component to sites on reassembled E2 (1997), Biochemistry, 36, 6819-6826.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
guanidine hydrochloride 50% inhibition at 0.3 M, complete inhibition at 0.7-1 M Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
82000
-
 3 * 82000, gel filtration, trimeric form occurs in solutions with 4 M guanidine hydrochloride Homo sapiens
200000
-
 at 1.8 - 2.8 M guanidine hydrochloride, complex dissociates at higher guanidine hydrochloride levels to a monomeric form with MW 82000 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Homo sapiens
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
treatment with guanidine hydrochloride and its subsequent removal results in refolding Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
 Homo sapiens S-acetyldihydrolipoamide + CoA
-
 ?

Subunits

Subunits Comment Organism
trimer 3 * 82000, gel filtration, trimeric form occurs in solutions with 4 M guanidine hydrochloride Homo sapiens