EC Number   |
Natural Substrates |
|---|
   1.2.1.104 | more |
E1 is bound to E2, both components of the pyruvate dehydrogenase multienzyme complex PDC, via the E1-binding B domain of E2, enzyme component organization in the pyruvate dehydrogenase multienzyme complex, regulatory role, overview |
| 1.2.1.104 | more |
pyruvate-supported mitochondrial respiration state 3 |
| 1.2.1.104 | more |
regulation of pyruvate dehydrogenase complex activity and citric acid cycle intermediates during high cardiac power generation, inhibition of fatty acid oxidation has a regulatory function, overview |
| 1.2.1.104 | more |
the PDH complex irreversibly decarboxylates pyruvate to acetylCoA (PDH activity) in a reaction that involves the participation of the three enzymes forming the PDH complex: AceE (pyruvate decarboxylase), AceF (dihydrolipoil acetyltransferase) and Lpd (dihydrolipoil dehydrogenase) |
| 1.2.1.104 | more |
the pyruvate dehydrogenase complex consists of multiple copies of several components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), E3-binding protein (BP), and specific kinases and phosphatases |
| 1.2.1.104 | pyruvate + CoA + NAD+ |
- |
| 1.2.1.104 | pyruvate + lipoamide |
- |
| 1.2.1.104 | pyruvate + lipoamide |
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by 2-ketobutyrate |
| 1.2.1.104 | pyruvate + lipoamide |
in overall reaction of pyruvate dehydrogenase complex, pyruvate can be replaced by hydroxypyruvate |
| 1.2.1.104 | pyruvate + lipoamide |
low reactivity with 2-ketovalerate |
