ArticleThe Journal of biological chemistry2016
Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 43 citations in OpenAlex.
- Slowdown of Enzymatic Cellulose Conversion Emerges from Cellulase Mode of Action.ACS catalysis · 2026Article
- Analysis of the phosphorylome of trichoderma reesei cultivated on sugarcane bagasse suggests post-translational regulation of the secreted glycosyl hydrolase Cel7A.Biotechnology reports (Amsterdam, Netherlands) · 2021Article
- 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
- In-depth characterization of Trichoderma reesei cellobiohydrolase TrCel7A produced in Nicotiana benthamiana reveals limitations of cellulase production in plants by host-specific post-translational modifications.Plant biotechnology journal · 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
- The dissociation mechanism of processive cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Modeling the activity burst in the initial phase of cellulose hydrolysis by the processive cellobiohydrolase Cel7A.Biotechnology and bioengineering · 2019Article
- Engineering enhanced cellobiohydrolase activity.Nature communications · 2018Article
- Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.Biotechnology for biofuels · 2018Article
- Article
- Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases fromBiotechnology for biofuels · 2018Article
- Human Chitotriosidase Is an Endo-Processive Enzyme.PloS one · 2017Article
- Molecular origins of reduced activity and binding commitment of processive cellulases and associated carbohydrate-binding proteins to cellulose III.The Journal of biological chemistryArticle
- 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
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural polysaccharides like cellulose and chitin are abundant and their enzymatic degradation to soluble sugars is an important route in green chemistry. Processive glycoside hydrolases (GHs), like cellobiohydrolase Cel7A of Trichoderma reesei (TrCel7A) are key components of efficient enzyme systems. TrCel7A consists of a catalytic domain (CD) and a smaller carbohydrate-binding module (CBM) connected through the glycosylated linker peptide. A tunnel-shaped active site rests in the CD and contains 10 glucose unit binding sites. The active site of TrCel7A is lined with four Trp residues with two of them, Trp-40 and Trp-38, in the substrate binding sites near the tunnel entrance. Although addressed in numerous studies the elucidation of the role of CBM and active site aromatics has been obscured by a complex multistep mechanism of processive GHs. Here we studied the role of the CBM-linker and Trp-38 of TrCel7A with respect to binding affinity, on- and off-rates, processivity, and synergism with endoglucanase. The CBM-linker increased the on-rate and substrate affinity of the enzyme. The Trp-38 to Ala substitution resulted in increased off-rates and decreased processivity. The effect of the Trp-38 to Ala substitution on on-rates was strongly dependent on the presence of the CBM-linker. This compensation between CBM-linker and Trp-38 indicates synergism between CBM-linker and CD in feeding the cellulose chain into the active site. The inter-domain synergism was pre-requisite for the efficient degradation of cellulose in the presence of endoglucanase.
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