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Literature summary for 2.3.1.12 extracted from
- Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex (2009), J. Biol. Chem., 284, 13086-13098.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoyl transacetylase | is part of the human pyruvate dehydrogenase complex | Homo sapiens |
| E2p | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological 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 | Homo sapiens |
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