ArticleThe Journal of biological chemistry2012
Pre-steady-state kinetics for hydrolysis of insoluble cellulose by cellobiohydrolase Cel7A.
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 44 papers.
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44 citing papers in PubMed.
- Expansion of the known poly(aspartic acid) hydrolases through the identification of four new PahZ1 homologs.Protein engineering, design & selection : PEDS · 2025Article
- The Effect of Accessibility of Insoluble Substrate on the Overall Kinetics of Enzymatic Degradation.Biotechnology and bioengineering · 2025Article
- Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.BBA advances · 2025Review
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 2024Article
- Impact of Synergy Partner Cel7B on Cel7A Binding Rates: Insights from Single-Molecule Data.The journal of physical chemistry. B · 2024Article
- 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
- Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- 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
- Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungusThe Journal of biological chemistry · 2019Article
- Engineering enhanced cellobiohydrolase activity.Nature communications · 2018Article
- Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases fromBiotechnology for biofuels · 2018Article
- Developing fast enzyme recycling strategy through elucidating enzyme adsorption kinetics on alkali and acid pretreated corn stover.Biotechnology for biofuels · 2018Article
- Testing scientific models using Qualitative Reasoning: Application to cellulose hydrolysis.Scientific reports · 2017Article
- Molecular and biochemical characterization of recombinant cel12B, cel8C, and peh28 overexpressed inBiotechnology for biofuels · 2017Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 2016Article
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7 authors.
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Abstract
The transient kinetic behavior of enzyme reactions prior to the establishment of steady state is a major source of mechanistic information, yet this approach has not been utilized for cellulases acting on their natural substrate, insoluble cellulose. Here, we elucidate the pre-steady-state regime for the exo-acting cellulase Cel7A using amperometric biosensors and an explicit model for processive hydrolysis of cellulose. This analysis allows the identification of a pseudo-steady-state period and quantification of a processivity number as well as rate constants for the formation of a threaded enzyme complex, processive hydrolysis, and dissociation, respectively. These kinetic parameters elucidate limiting factors in the cellulolytic process. We concluded, for example, that Cel7A cleaves about four glycosidic bonds/s during processive hydrolysis. However, the results suggest that stalling the processive movement and low off-rates result in a specific activity at pseudo-steady state that is 10-25-fold lower. It follows that the dissociation of the enzyme-substrate complex (half-time of ~30 s) is rate-limiting for the investigated system. We suggest that this approach can be useful in attempts to unveil fundamental reasons for the distinctive variability in hydrolytic activity found in different cellulase-substrate systems.
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