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Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
Each polypeptide chain in the lipoate acetyltransferase (E2) core of the pyruvate dehydrogenase complex from Escherichia coli contains three repeating sequences in the N-terminal half of the molecule. The repeats are highly homologous in primary structure and each includes a lysine residue that is a...
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| Pubblicato in: | EMBO J |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group
1984
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC557515/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6430694/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1984.tb01969.x |
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