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Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli: Mechanism for rate enhancement in a multimeric structure

In the absence of CoA and presence of pyruvate, the lipoic acid residues covalently bound to the lipoate acetyltransferase core component (acetyl-CoA:dihydrolipoate S-acetyltransferase, EC 2.3.1.12) of the pyruvate dehydrogenase multienzyme complex of Escherichia coli become reductively acetylated....

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Détails bibliographiques
Auteurs principaux: Danson, Michael J., Fersht, Alan R., Perham, Richard N.
Format: Artigo
Langue:Inglês
Publié: 1978
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC392968/
https://ncbi.nlm.nih.gov/pubmed/214786
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