ArticleAngewandte Chemie (International ed. in English)2016
Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
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- Magnesium induced structural reorganization in the active site of adenylate kinase.Science advances · 2024Article
- Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development.ACS omega · 2024Review
- Elucidating Dynamics of Adenylate Kinase from Enzyme Opening to Ligand Release.Journal of chemical information and modeling · 2024Article
- Mechanistic Basis for a Connection between the Catalytic Step and Slow Opening Dynamics of Adenylate Kinase.Journal of chemical information and modeling · 2023Article
- Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
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- Serine protease dynamics revealed by NMR analysis of the thrombin-thrombomodulin complex.Scientific reports · 2021Article
- Reactions of aryl dimethylphosphinothioate esters with anionic oxygen nucleophiles: transition state structure in 70% water-30% ethanol.RSC advances · 2021Article
- Determining isoleucine side-chain rotamer-sampling in proteins fromChemical communications (Cambridge, England) · 2019Article
- Characterising side chains in large proteins by protonlessNature communications · 2019Article
- Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- AJournal of biomolecular NMR · 2017Article
- Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.Chemical communications (Cambridge, England) · 2017Article
- Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction.Angewandte Chemie (International ed. in English) · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
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 transition state analog (TSA) complex was utilized to evaluate the extent to which active site conformational entropy contributes to the transition state free energy. The catalytically essential arginine side-chain guanidino groups were found to be remarkably rigid in the TSA complex, indicating that the enzyme has evolved to restrict the conformational freedom along its reaction path over the energy landscape, which in turn allows the phosphoryl transfer to occur selectively by avoiding side reactions.
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