1.2.1.104 ? x * 100000, SDS-PAGE 348986 1.2.1.104 ? x * 40000-41000 + x * 37000 348964 1.2.1.104 ? x * 92500, SDS-PAGE 348962 1.2.1.104 dimer 2 * 100000, SDS-PAGE 348948 1.2.1.104 dimer 2 * 94000, SDS-PAGE 348939 1.2.1.104 dimer 2 * 95000-96500, SDS-PAGE with and without urea 348966 1.2.1.104 dimer 2 * 99474, calculation from nucleotide sequence 348982 1.2.1.104 dimer alpha2,beta2, 2 * 38000 + 2 * 56000, SDS-PAGE, N-terminal amino acid sequencing 348988 1.2.1.104 dimer alpha2,beta2, 2 * 43000 + 2 * 40000, SDS-PAGE, immunoblotting 348989 1.2.1.104 heterotetramer x-ray crystallography 690088 1.2.1.104 monomer 1 * 100000, SDS-PAGE 348977 1.2.1.104 additional information analysis of architecture of enzyme subunits in pyruvate dehydrogenase complex. Complex contains 30 enzyme heterotetramers plus dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase multimers 674601 1.2.1.104 additional information analysis of pyruvate dehydrogenase core complex consisting of dihydrolipoyl acetyltransferase and dihydrolipoyl dehydrogenase enzymes and comparison with structure of enzyme complex with dihydrolipoyl acetyltransferase 674743 1.2.1.104 additional information enzyme component organization and binding structures in the pyruvate dehydrogenase multienzyme complex, core is formed by compoenents E2 and E3, regulatory role 656269 1.2.1.104 additional information identification of key amino acid residues responsible for enzyme component assembly to the multienzyme complex, overview 654615 1.2.1.104 additional information lipoamide dehydrogenase and two unknown polypeptides bind tightly to complex 758742 1.2.1.104 additional information PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength -, 760048 1.2.1.104 additional information the affinity of PDH2 for the PDH-binding domain of E2 of pyruvate dehydrogenase complex differs only modestly from that of PDH1, surface plasma resonance studies 674778 1.2.1.104 additional information the complex consists of four subunits, i.e. E1alpha (44 kDa), E1beta (35 kDa), E2 (73 kDa), and E3 (60 kDa), SDS-PAGE 759422 1.2.1.104 additional information the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3 -, 760048 1.2.1.104 multimer x * 100000, pyruvate dehydrogenase, x * 87000, dihydrolipoamide transacetylase (acetyl-CoA:dihydrolipoamide S-acetyltransferase, EC 2.3.1.12), and x * 56000, dihydrolipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) components, respectively, SDS-PAGE 758852 1.2.1.104 multimer x * 160000, x * 57600, x * 55600, x * 52500, x * 37100, SDS-PAGE 758867 1.2.1.104 multimer x * 39800, x * 41700, 53700, and 57500, i.e. pyruvate decarboxylase subunits (E1), lipoate acetyltransferase (E2), and lipoamide dehydrogenase (E3), respectively, SDS-PAGE 758928 1.2.1.104 multimer x * 57000, x * 54000, x * 42000 and x * 36000, respectively, SDS-PAGE. The empirical unit must be repeated at least 50 times to make up the assembled complex 758743 1.2.1.104 multimer x * 68000, lipoate acetyltransferase, x * 54800, lipoamide dehydrogenase, x *41900, alpha-pyruvate dehydrogenase, x * 45000, beta-pyruvate dehydrogenase subunit, plus x * 45000, component X, SDS-PAGE 759746 1.2.1.104 multimer x * 70000, E2 subunit, x * 55000, E3 subunit, SDS-PAGE 758755 1.2.1.104 multimer x * 78000, i.e. dihydrolipoamide transacetylase (E2) subunit, x * 60000, x * 58000, i.e. dihydrolipoamide dehydrogenase (E3) subunit, x * 55000, x * 43000 and x * 41000, i.e. alpha-subunits of pyruvate dehydrogenase, and x * 37000, i.e. beta-subunit of pyruvate dehydrogenase (E1), respectively, SDS-PAGE 758744 1.2.1.104 multimer x *42000 and x * 37000, alpha- and beta-subunits of pyruvate dehydrogenase, respectively, x * 76000, lipoate acetyltransferase, and x * 56000, lipoamide dehydrogenase. Two unknown polypeptides of 46000 and 41000 are additionally detected 758742 1.2.1.104 oligomer - 348910 1.2.1.104 oligomer 60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex 348910, 94881 1.2.1.104 oligomer quaternary structure of pyruvate dehydrogenase complex 348933 1.2.1.104 oligomer x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE -, 759204 1.2.1.104 tetramer - 348945, 348988, 94881 1.2.1.104 tetramer alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE 348985 1.2.1.104 tetramer alpha2,beta2, 2 * 41000 + 2 * 35000, SDS-PAGE 348941 1.2.1.104 tetramer alpha2,beta2, 2 * 41000 + 2 * 36000 348910 1.2.1.104 tetramer alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence 348986 1.2.1.104 tetramer alpha2,beta2, 2 * 42000 + 2 * 37000, SDS-PAGE 348912 1.2.1.104 tetramer alpha2,beta2, 2 * 42000 + 2 * 38000, SDS-PAGE 348926 1.2.1.104 tetramer alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE 348947, 348959