ArticleNature communications2024
Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.Protein science : a publication of the Protein Society · 2026Article
- A dual catalytic architecture promotes C-2 stereoinversion of CDP-glucose by the CDP-tyvelose 2-epimerase from Thermodesulfatator atlanticus.The Journal of biological chemistry · 2026Article
- Challenges in Mechanistic Investigation of a Flexible Aminocatalyst as Demonstrated through Enamine Formation.ChemistryOpen · 2025Article
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- Protein flexibility drives sugar rotation and high substrate promiscuity in a GDP-sugar 4-epimerase.Computational and structural biotechnology journal · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Understanding enzyme catalysis as connected to protein motions is a major challenge. Here, based on temperature kinetic studies combined with isotope effect measurements, we obtain energetic description of C-H activation in NAD-dependent UDP-glucuronic acid C4 epimerase. Approach from the ensemble-averaged ground state (GS) to the transition state-like reactive conformation (TSRC) involves, alongside uptake of heat (
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Registered trials
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