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Literature summary for 1.2.1.104 extracted from
- Reconstitution of the Escherichia coli pyruvate dehydrogenase complex (1975), Proc. Natl. Acad. Sci. USA, 72, 3068-3072 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | dihydrolipoyl transacetylase subunit consists of 24 apparently identical polypeptide chains organized into a cube-like structure, and has the potential to bind 24 pyruvate dehydrogenase dimers in the absence of flavoprotein and 24 flavoprotein dimers in the absence of the pyruvate dehydrogenase subunit. The transacetylase can accommodate a total of only about 12 pyruvate dehydrogenase dimers and six flavoprotein dimers and this stoichiometry, which is the same as that of the native pyruvate dehydrogenase complex, produces maximum activity. Steric hindrance between the relatively bulky pyruvate dehydrogenase and flavoprotein molecules prevents the transacetylase from binding 24 molecules of each ligand | Escherichia coli |
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