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Literature summary for 2.3.1.12 extracted from

  • Hiromasa, Y.; Yan, X.; Roche, T.E.
    Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r (2008), Biochemistry, 47, 2312-2324.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase is expressed as a GST fusion protein Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
K+ association of the pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) dimers is enhanced by K+ Homo sapiens
phosphate phosphate has a pronounced effect in increasing ligand interference with pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Subunits

Subunits Comment Organism
dimer GST-L2, glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase exists as a dimer Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrolipoyl acetyltransferase glutathione-S-transferase fused to the inner lipoyl domain is used Homo sapiens

General Information

General Information Comment Organism
malfunction Nov3r a lipoyl group-binding site inhibitor (related trifluoro-2-hydroxy-2-menthylpropionate compound) prevents pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase) binding and dissect the effects of Nov3r binding at the lipoyl group binding site on PDHK2 binding of other ligands Homo sapiens