ArticleThe Journal of biological chemistry2012
Product binding varies dramatically between processive and nonprocessive cellulase enzymes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- Biomass-Based Composites for Agricultural Applications.Polymers · 2025Review
- Impact of Synergy Partner Cel7B on Cel7A Binding Rates: Insights from Single-Molecule Data.The journal of physical chemistry. B · 2024Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Valorization of outer tunic of the marine filter feeder Ciona intestinalis towards the production of second-generation biofuel and prebiotic oligosaccharides.Biotechnology for biofuels · 2021Article
- Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungusThe Journal of biological chemistry · 2019Article
- Human Chitotriosidase Is an Endo-Processive Enzyme.PloS one · 2017Article
- Who's on base? Revealing the catalytic mechanism of inverting family 6 glycoside hydrolases.Chemical science · 2016Article
- Alleviating product inhibition in cellulase enzyme Cel7A.Biotechnology and bioengineering · 2016Article
- The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.The Journal of biological chemistry · 2015Article
- Article
- Cellobiohydrolase and endoglucanase respond differently to surfactants during the hydrolysis of cellulose.Biotechnology for biofuels · 2015Article
- 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
- Binding and movement of individual Cel7A cellobiohydrolases on crystalline cellulose surfaces revealed by single-molecule fluorescence imaging.The Journal of biological chemistry · 2013Article
- Computational investigation of the pH dependence of loop flexibility and catalytic function in glycoside hydrolases.The Journal of biological chemistry · 2013Article
- Structural, biochemical, and computational characterization of the glycoside hydrolase family 7 cellobiohydrolase of the tree-killing fungus Heterobasidion irregulare.The Journal of biological chemistry · 2013Article
- Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity.Biophysical journal · 2013Article
- Improving the performance of enzymes in hydrolysis of high solids paper pulp derived from MSW.Biotechnology for biofuels · 2013Article
- Endo-exo synergism in cellulose hydrolysis revisited.The Journal of biological chemistry · 2012Article
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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
Cellulases hydrolyze β-1,4 glycosidic linkages in cellulose, which are among the most prevalent and stable bonds in Nature. Cellulases comprise many glycoside hydrolase families and exist as processive or nonprocessive enzymes. Product inhibition negatively impacts cellulase action, but experimental measurements of product-binding constants vary significantly, and there is little consensus on the importance of this phenomenon. To provide molecular level insights into cellulase product inhibition, we examine the impact of product binding on processive and nonprocessive cellulases by calculating the binding free energy of cellobiose to the product sites of catalytic domains of processive and nonprocessive enzymes from glycoside hydrolase families 6 and 7. The results suggest that cellobiose binds to processive cellulases much more strongly than nonprocessive cellulases. We also predict that the presence of a cellodextrin bound in the reactant site of the catalytic domain, which is present during enzymatic catalysis, has no effect on product binding in nonprocessive cellulases, whereas it significantly increases product binding to processive cellulases. This difference in product binding correlates with hydrogen bonding between the substrate-side ligand and the cellobiose product in processive cellulase tunnels and the additional stabilization from the longer tunnel-forming loops. The hydrogen bonds between the substrate- and product-side ligands are disrupted by water in nonprocessive cellulase clefts, and the lack of long tunnel-forming loops results in lower affinity of the product ligand. These findings provide new insights into the large discrepancies reported for binding constants for cellulases and suggest that product inhibition will vary significantly based on the amount of productive binding for processive cellulases on cellulose.
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