ArticleThe Journal of biological chemistry2015
Probing substrate interactions in the active tunnel of a catalytically deficient cellobiohydrolase (Cel7).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 39 citations in OpenAlex.
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 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
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Alanine substitution in cellobiohydrolase provides new insights into substrate threading.Scientific reports · 2017Article
- Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases.PloS one · 2017Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 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
- Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.The Journal of biological chemistry · 2015Article
- Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity.The Journal of biological chemistry · 2015Article
- Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases.The Journal of biological chemistry · 2015Article
- Free Energy Diagram for the Heterogeneous Enzymatic Hydrolysis of Glycosidic Bonds in Cellulose.The Journal of biological chemistry · 2015Article
- 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
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolases break down cellulose sequentially by sliding along the crystal surface with a single cellulose strand threaded through the catalytic tunnel of the enzyme. This so-called processive mechanism relies on a complex pattern of enzyme-substrate interactions, which need to be addressed in molecular descriptions of processivity and its driving forces. Here, we have used titration calorimetry to study interactions of cellooligosaccharides (COS) and a catalytically deficient variant (E212Q) of the enzyme Cel7A from Trichoderma reesei. This enzyme has ∼10 glucopyranose subsites in the catalytic tunnel, and using COS ligands with a degree of polymerization (DP) from 2 to 8, different regions of the tunnel could be probed. For COS ligands with a DP of 2-3 the binding constants were around 10(5) m(-1), and for longer ligands (DP 5-8) this value was ∼10(7) m(-1). Within each of these groups we did not find increased affinity as the ligands got longer and potentially filled more subsites. On the contrary, we found a small but consistent affinity loss as DP rose from 6 to 8, particularly at the higher investigated temperatures. Other thermodynamic functions (ΔH, ΔS, and ΔCp) decreased monotonously with both temperature and DP. Combined interpretation of these thermodynamic results and previously published structural data allowed assessment of an affinity profile along the length axis of the active tunnel.
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