ArticleProceedings of the National Academy of Sciences of the United States of America2014
α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Origami with small molecules: exploiting the C-F bond as a conformational tool.Beilstein journal of organic chemistry · 2025Review
- Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase.Communications biology · 2024Article
- CompleteJournal of the American Chemical Society · 2024Article
- Chemical features and machine learning assisted predictions of protein-ligand short hydrogen bonds.Scientific reports · 2023Article
- Chemical Features and Machine Learning Assisted Predictions of Protein-Ligand Short Hydrogen Bonds.Research square · 2023Article
- Essential Functional Interplay of the Catalytic Groups in Acid Phosphatase.ACS catalysis · 2022Article
- An Enzyme with High Catalytic Proficiency Utilizes Distal Site Substrate Binding Energy to Stabilize the Closed State but at the Expense of Substrate Inhibition.ACS catalysis · 2022Article
- Octahedral Trifluoromagnesate, an Anomalous Metal Fluoride Species, Stabilizes the Transition State in a Biological Motor.ACS catalysis · 2021Article
- Allomorphy as a mechanism of post-translational control of enzyme activity.Nature communications · 2020Article
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- Article
- Mechanistic Insights on Human Phosphoglucomutase Revealed by Transition Path Sampling and Molecular Dynamics Calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Observing enzyme ternary transition state analogue complexes byChemical science · 2017Article
- Article
- General Linker Diversification Approach to Bivalent Ligand Assembly: Generation of an Array of Ligands for the Cation-Independent Mannose 6-Phosphate Receptor.Organic letters · 2017Article
- Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.Topics in current chemistry (Cham) · 2017Review
- CheckMyMetal: a macromolecular metal-binding validation tool.Acta crystallographica. Section D, Structural biology · 2017Article
- (19)F NMR and DFT Analysis Reveal Structural and Electronic Transition State Features for RhoA-Catalyzed GTP Hydrolysis.Angewandte Chemie (International ed. in English) · 2016Article
- Synthesis, structure and reactivity of a terminal magnesium fluoride compound, [TpChemical science · 2016Article
- Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Journal of the American Chemical Society · 2015Article
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10 authors.
Funding
Abstract
β-Phosphoglucomutase (βPGM) catalyzes isomerization of β-D-glucose 1-phosphate (βG1P) into D-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a β-D-glucose 1,6-bisphosphate (βG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of βG1P deliver novel step 1 transition state analog (TSA) complexes for βPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the β-D-glucopyranose ring in the βG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by ∼ 30° between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only ∼ 5°, and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of βG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein.
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