ArticleThe Journal of biological chemistry2020
Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Flavoaffinins, Elusive Cellulose-Binding Natural Products from an Anaerobic Bacterium.Journal of the American Chemical Society · 2026Article
- The energetic landscape of CH-π interactions in protein-carbohydrate binding.Chemical science · 2025Article
- Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.BBA advances · 2025Review
- Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non-productive binding: insights from crystal structures and MD simulation.The FEBS journal · 2023Article
- Enzyme Synergy in Transient Clusters of Endo- and Exocellulase Enables a Multilayer Mode of Processive Depolymerization of Cellulose.ACS catalysis · 2022Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolases effectively degrade cellulose and are of biotechnological interest because they can convert lignocellulosic biomass to fermentable sugars. Here, we implemented a fluorescence-based method for real-time measurements of complexation and decomplexation of the processive cellulase Cel7A and its insoluble substrate, cellulose. The method enabled detailed kinetic and thermodynamic analyses of ligand binding in a heterogeneous system. We studied WT Cel7A and several variants in which one or two of four highly conserved Trp residues in the binding tunnel had been replaced with Ala. WT Cel7A had on/off-rate constants of 1 × 10
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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.