2.3.1.12	physiological function	in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). K276 of hE2 is involved in the interaction with pyruvate dehydrogenase	686772	
2.3.1.12	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	702229	
2.3.1.12	physiological function	strain MM3 can grow on up to 250 microM pyrene in culture medium. With an initial cell density of 30000000 cells/ml, nearly 70% of 50 microM pyrene is degraded after 7 days of incubation, accompanied by distinct accumulation of dihydrolipoamide acetyltransferase	755757	
2.3.1.12	physiological function	structural comparison by cryo-electronmicroscopy of the human full-length and truncated dihydrolipoyl acetyltransferase cores reveal flexible linkers emanating from the edges of trimers of the internal catalytic domains. Using the secondary structure constraints revealed the 8 A cryo-electronmicroscopy and the prokaryotic truncated dihydrolipoyl acetyltransferase atomic structure as a template, a pseudo atomic model of human truncated dihydrolipoyl acetyltransferase is derived. The active sites are conserved between the truncated prokaryotic and human enzyme. Marked structural differences are apparent in the hairpin domain and in the N-terminal helix connected to the flexible linker	690088	
2.3.1.12	metabolism	the enzyme is a mitochondrial complement component 1, q subcomponent binding protein-binding protein	735426	
2.3.1.12	physiological function	uing an in vitro reconstituted pyruvate dehydrogenase complex densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence are provided that there are 40 copies of dihydrolipoyl transacetylase (E2p) and 20 copies of dihydrolipoamide dehydrogenase-binding protein (E3BP), in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled pyruvate dehydrogenase complex for dihydrolipoyl transacetylase: dihydrolipoamide dehydrogenase-binding protein: dihydrolipoamide dehydrogenase is 40:20:40:20	704473