ArticleThe Journal of biological chemistry2014
Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 75 citations in OpenAlex.
- The carbohydrate-binding module of TrCel7A aids in navigating hemicellulose barriers in plant cell walls.The Journal of biological chemistry · 2026Article
- Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization.Biochemistry · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Investigation Into the Role of Reductants and Cosubstrates in Lytic Polysaccharide Monooxygenase Thermothielavioides terrestris AA9E Binding to Cellulose by Single-Molecule Imaging.Biotechnology and bioengineering · 2026Article
- Expansion of the known poly(aspartic acid) hydrolases through the identification of four new PahZ1 homologs.Protein engineering, design & selection : PEDS · 2025Article
- The membrane-targeting-sequence motif is required for exhibition of recessive resurrection in Escherichia coli RNase E.Nucleic acids research · 2025Article
- 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
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 2024Article
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Model of Processive Catalysis with Site Clustering and Blocking and Its Application to Cellulose Hydrolysis.The journal of physical chemistry. B · 2022Article
- Enzyme Synergy in Transient Clusters of Endo- and Exocellulase Enables a Multilayer Mode of Processive Depolymerization of Cellulose.ACS catalysis · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Article
- Role of Tryptophan 38 in Loading Substrate Chain into the Active-site Tunnel of Cellobiohydrolase I fromJournal of applied glycoscience · 2021Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Single-molecule imaging analysis reveals the mechanism of a high-catalytic-activity mutant of chitinase A fromThe Journal of biological chemistry · 2020Article
- Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.The Journal of biological chemistry · 2020Article
- Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose.Biotechnology for biofuels · 2020Article
- Removal ofBiotechnology for biofuels · 2020Article
- The dissociation mechanism of processive cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. They effectively break down crystalline cellulose and make up a major component in industrial enzyme mixtures used for deconstruction of lignocellulosic biomass. Identification of the rate-limiting step for cellobiohydrolases remains controversial, and recent reports have alternately suggested either association (on-rate) or dissociation (off-rate) as the overall bottleneck. Obviously, this uncertainty hampers both fundamental mechanistic understanding and rational design of enzymes with improved industrial applicability. To elucidate the role of on- and off-rates, respectively, on the overall kinetics, we have expressed a variant in which a tryptophan residue (Trp-38) in the middle of the active tunnel has been replaced with an alanine. This mutation weakens complex formation, and the population of substrate-bound W38A was only about half of the wild type. Nevertheless, the maximal, steady-state rate was twice as high for the variant enzyme. It is argued that these opposite effects on binding and activity can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process).
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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.