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Results 1 - 6 of 6
EC Number General Information Commentary Reference
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12malfunction 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
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12metabolism the enzyme is a mitochondrial complement component 1, q subcomponent binding protein-binding protein 735426
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12physiological 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
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12physiological 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
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12physiological 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
Show all pathways known for 2.3.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.12physiological 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
Results 1 - 6 of 6