ArticleThe Journal of biological chemistry2011
Probing carbohydrate product expulsion from a processive cellulase with multiple absolute binding free energy methods.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 77 citations in OpenAlex.
- There is an "I" in team: individual improvements in supercharged cellulase cocktail facilitates cooperative cellulose degradation.Biotechnology for biofuels and bioproducts · 2026Article
- 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
- A Case Study of the Glycoside Hydrolase Enzyme Mechanism Using an Automated QM-Cluster Model Building Toolkit.Frontiers in chemistry · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Dual Substrate Specificity of the Rutinosidase fromInternational journal of molecular sciences · 2020Article
- Article
- The dissociation mechanism of processive cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Alanine substitution in cellobiohydrolase provides new insights into substrate threading.Scientific reports · 2017Article
- Who's on base? Revealing the catalytic mechanism of inverting family 6 glycoside hydrolases.Chemical science · 2016Article
- Biochemical and Structural Characterizations of Two Dictyostelium Cellobiohydrolases from the Amoebozoa Kingdom Reveal a High Level of Conservation between Distant Phylogenetic Trees of Life.Applied and environmental microbiology · 2016Article
- Alleviating product inhibition in cellulase enzyme Cel7A.Biotechnology and bioengineering · 2016Article
- Subsite-specific contributions of different aromatic residues in the active site architecture of glycoside hydrolase family 12.Scientific reports · 2015Article
- Free Energy Diagram for the Heterogeneous Enzymatic Hydrolysis of Glycosidic Bonds in Cellulose.The Journal of biological chemistry · 2015Article
- Probing substrate interactions in the active tunnel of a catalytically deficient cellobiohydrolase (Cel7).The Journal of biological chemistry · 2015Article
- Genomics review of holocellulose deconstruction by aspergilli.Microbiology and molecular biology reviews : MMBR · 2014Review
- Deciphering the effect of the different N-glycosylation sites on the secretion, activity, and stability of cellobiohydrolase I from Trichoderma reesei.Applied and environmental microbiology · 2014Article
- Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F.Enzyme research · 2014Article
- Loop motions important to product expulsion in the Thermobifida fusca glycoside hydrolase family 6 cellobiohydrolase from structural and computational studies.The Journal of biological chemistry · 2013Article
- Product inhibition of cellulases studied with 14C-labeled cellulose substrates.Biotechnology for biofuels · 2013Article
- Structural characterization of a unique marine animal family 7 cellobiohydrolase suggests a mechanism of cellulase salt tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the enzymatic mechanism that cellulases employ to degrade cellulose is critical to efforts to efficiently utilize plant biomass as a sustainable energy resource. A key component of cellulase action on cellulose is product inhibition from monosaccharide and disaccharides in the product site of cellulase tunnel. The absolute binding free energy of cellobiose and glucose to the product site of the catalytic tunnel of the Family 7 cellobiohydrolase (Cel7A) of Trichoderma reesei (Hypocrea jecorina) was calculated using two different approaches: steered molecular dynamics (SMD) simulations and alchemical free energy perturbation molecular dynamics (FEP/MD) simulations. For the SMD approach, three methods based on Jarzynski's equality were used to construct the potential of mean force from multiple pulling trajectories. The calculated binding free energies, -14.4 kcal/mol using SMD and -11.2 kcal/mol using FEP/MD, are in good qualitative agreement. Analysis of the SMD pulling trajectories suggests that several protein residues (Arg-251, Asp-259, Asp-262, Trp-376, and Tyr-381) play key roles in cellobiose and glucose binding to the catalytic tunnel. Five mutations (R251A, D259A, D262A, W376A, and Y381A) were made computationally to measure the changes in free energy during the product expulsion process. The absolute binding free energies of cellobiose to the catalytic tunnel of these five mutants are -13.1, -6.0, -11.5, -7.5, and -8.8 kcal/mol, respectively. The results demonstrated that all of the mutants tested can lower the binding free energy of cellobiose, which provides potential applications in engineering the enzyme to accelerate the product expulsion process and improve the efficiency of biomass conversion.
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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.