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Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex
The Escherichia coli pyruvate dehydrogenase multienzyme complex contains multiple copies of three enzymatic components, E1p, E2p, and E3, that sequentially carry out distinct steps in the overall reaction converting pyruvate to acetyl-CoA. Efficient functioning requires the enzymatic components to a...
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| Autores principales: | , , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2014
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4208021/ https://ncbi.nlm.nih.gov/pubmed/25210042 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.592915 |
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