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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....
Kaydedildi:
| Asıl Yazarlar: | , , |
|---|---|
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
1978
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC392968/ https://ncbi.nlm.nih.gov/pubmed/214786 |
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