Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction

States along the phosphoryl transfer reaction catalyzed by the nucleoside monophosphate kinase UmpK were captured and changes in the conformational heterogeneity of conserved active site arginine side‐chains were quantified by NMR spin‐relaxation methods. In addition to apo and ligand‐bound UmpK, a...

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Detalles Bibliográficos
Autores principales: Zeymer, Cathleen, Werbeck, Nicolas D., Zimmermann, Sabine, Reinstein, Jochen, Hansen, D. Flemming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5026167/
https://www.ncbi.nlm.nih.gov/pubmed/27534930
http://dx.doi.org/10.1002/anie.201606238

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5026167/
https://www.ncbi.nlm.nih.gov/pubmed/27534930
http://dx.doi.org/10.1002/anie.201606238

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