EC Number   |
Subunits |
Reference |
|---|
   1.2.1.104 | monomer |
1 * 100000, SDS-PAGE |
348977 |
| 1.2.1.104 | More |
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 | More |
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 | More |
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 | More |
identification of key amino acid residues responsible for enzyme component assembly to the multienzyme complex, overview |
654615 |
| 1.2.1.104 | More |
lipoamide dehydrogenase and two unknown polypeptides bind tightly to complex |
758742 |
| 1.2.1.104 | More |
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 | More |
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 | More |
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 | More |
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 |
