EC Number |
Title |
Organism |
---|
1.2.1.104 | Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution |
Escherichia coli |
1.2.1.104 | Activity of the mitochondrial pyruvate dehydrogenase complex in plants is stimulated in the presence of malate |
Hordeum vulgare |
1.2.1.104 | Activity of the mitochondrial pyruvate dehydrogenase complex in plants is stimulated in the presence of malate |
Pisum sativum |
1.2.1.104 | Altering the sensitivity of Escherichia coli pyruvate dehydrogenase complex to NADH inhibition by structure-guided design |
Escherichia coli |
1.2.1.104 | Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit |
Escherichia coli |
1.2.1.104 | Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex |
Neurospora crassa |
1.2.1.104 | Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex |
Neurospora crassa DSM 1257 |
1.2.1.104 | Biochemical nature of pyruvate dehydrogenase complex in the patient with primary lactic acidaemia |
Homo sapiens |
1.2.1.104 | Characterization and immunochemistry of pyruvate dehydrogenase complex of Ascaris muscle |
Ascaris suum |
1.2.1.104 | Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex |
Homo sapiens |