ArticleAngewandte Chemie (International ed. in English)2020
Dynamics of Ligand Binding to a Rigid Glycosidase*.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 10 citations in OpenAlex.
- Recent Advances of Azobenzene-Based Photoresponsive Molecular Switches for Protein-Targeted Photopharmacology.Molecules (Basel, Switzerland) · 2026Review
- Activity-Enhancing Mutations in an LmrR-Based Artificial Metalloenzyme Destabilize the Protein Scaffold and Alter its Conformational Plasticity.Chembiochem : a European journal of chemical biology · 2025Article
- Molecular insights of acarbose metabolization catalyzed by acarbose-preferred glucosidase.Nature communications · 2025Article
- Terminal spin labeling of xylotriose strongly affects interactions in the active site of xylanase BcX.Journal of biomolecular NMR · 2025Article
- Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-Food chemistry. Molecular sciences · 2025Article
- Dielectric Spectroscopy Studies of Conformational Relaxation Dynamics in Molecular Glass-Forming Liquids.International journal of molecular sciences · 2023Review
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics.Antimicrobial agents and chemotherapy · 2021Article
- Tuning the Transglycosylation Reaction of a GH11 Xylanase by a Delicate Enhancement of its Thumb Flexibility.Chembiochem : a European journal of chemical biology · 2021Article
- Dynamics of Ligand Binding to a Rigid Glycosidase*.Angewandte Chemie (International ed. in English) · 2020Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The single-domain GH11 glycosidase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose, which is one of the most abundant renewable biomaterials in nature. We demonstrate that BCX in solution undergoes minimal structural changes during turnover. NMR spectroscopy results show that the rigid protein matrix provides a frame for fast substrate binding in multiple conformations, accompanied by slow conversion, which is attributed to an enzyme-induced substrate distortion. A model is proposed in which the rigid enzyme takes advantage of substrate flexibility to induce a conformation that facilitates the acyl formation step of the hydrolysis reaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.