ArticleJournal of the American Chemical Society2020
Rational Design of Mechanism-Based Inhibitors and Activity-Based Probes for the Identification of Retaining α-l-Arabinofuranosidases.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Targeting Conformational Flexibility of a Reactive Intermediate to Enhance Selectivity of a GABA Aminotransferase Inactivator.Journal of the American Chemical Society · 2026Article
- Synthesis and Application of Bioactive N-Functionalized Aziridines.Angewandte Chemie (International ed. in English) · 2025Review
- Discovery of an Aziridine-Based Inhibitor That Targets Cysteine Desulfurase Type II SufS via High-Throughput X‑ray Crystallography.ACS medicinal chemistry letters · 2025Article
- Activity-based probes for dynamic characterisation of polysaccharide-degrading enzymes.The Biochemical journal · 2025Review
- Activity-Based Profiling of Retaining Glycosidases in Disease Diagnosis and Their Application in Drug Discovery.Handbook of experimental pharmacology · 2025Review
- Integration of Experimental and Computational Methods to Characterize Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- From Mechanism-Based Retaining Glycosidase Inhibitors to Activity-Based Glycosidase Profiling.Journal of the American Chemical Society · 2024Review
- A Multiplexing Activity-Based Protein-Profiling Platform for Dissection of a Native Bacterial Xyloglucan-Degrading System.ACS central science · 2023Article
- β-l-ACS chemical biology · 2023Article
- Identification of fungal lignocellulose-degrading biocatalysts secreted by Phanerochaete chrysosporium via activity-based protein profiling.Communications biology · 2022Article
- A conserved enzyme of smut fungi facilitates cell-to-cell extension in the plant bundle sheath.Nature communications · 2022Article
- Cloning, expression and characterization of a glycoside hydrolase family 51 α-l-arabinofuranosidase from3 Biotech · 2022Article
- Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases.The journal of physical chemistry. B · 2022Review
- Synthesis of broad-specificity activity-based probes forOrganic & biomolecular chemistry · 2022Article
- Activity-based protein profiling reveals dynamic substrate-specific cellulase secretion by saprotrophic basidiomycetes.Biotechnology for biofuels and bioproducts · 2022Article
- Design, Synthesis and Structural Analysis of Glucocerebrosidase Imaging Agents.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Modulation of the Activity and Regioselectivity of a Glycosidase: Development of a Convenient Tool for the Synthesis of Specific Disaccharides.Molecules (Basel, Switzerland) · 2021Article
- Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on α-1,6 Mannanases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Complete Genome Sequence of Pedobacter sp. PAMC26386 and Their Low Temperature Application in Arabinose-containing Polysaccharides Degradation.Current microbiology · 2021Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 4 countries.
Funding
Abstract
Identifying and characterizing the enzymes responsible for an observed activity within a complex eukaryotic catabolic system remains one of the most significant challenges in the study of biomass-degrading systems. The debranching of both complex hemicellulosic and pectinaceous polysaccharides requires the production of α-l-arabinofuranosidases among a wide variety of coexpressed carbohydrate-active enzymes. To selectively detect and identify α-l-arabinofuranosidases produced by fungi grown on complex biomass, potential covalent inhibitors and probes which mimic α-l-arabinofuranosides were sought. The conformational free energy landscapes of free α-l-arabinofuranose and several rationally designed covalent α-l-arabinofuranosidase inhibitors were analyzed. A synthetic route to these inhibitors was subsequently developed based on a key Wittig-Still rearrangement. Through a combination of kinetic measurements, intact mass spectrometry, and structural experiments, the designed inhibitors were shown to efficiently label the catalytic nucleophiles of retaining GH51 and GH54 α-l-arabinofuranosidases. Activity-based probes elaborated from an inhibitor with an aziridine warhead were applied to the identification and characterization of α-l-arabinofuranosidases within the secretome of
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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.