ArticleThe journal of physical chemistry. B2009
A kinetic model for the enzymatic action of cellulase.
Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 71 citations in OpenAlex.
- An absorbance method for analysis of enzymatic degradation kinetics of poly(ethylene terephthalate) films.Scientific reports · 2021Article
- Effects of the linker region on the structure and function of modular GH5 cellulases.Scientific reports · 2016Article
- An Electrochemical Impedance Spectroscopy System for Monitoring Pineapple Waste Saccharification.Sensors (Basel, Switzerland) · 2016Article
- Article
- Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Direct amplification of new cellulase genes from woodland soil purified DNA.Molecular biology reports · 2013Article
- Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity.Biophysical journal · 2013Article
- Article
- A cellular automaton model of crystalline cellulose hydrolysis by cellulases.Biotechnology for biofuels · 2011Article
- The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein.Biophysical journal · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We develop a mechanochemical model for the dynamics of cellulase, a two-domain enzyme connected by a peptide linker, as it extracts and hydrolyzes a cellulose polymer from a crystalline substrate. We consider two random walkers, representing the catalytic domain (CD) and the carbohydrate binding module (CBM), whose rates for stepping are biased by the coupling through the linker and the energy required to lift the cellulose polymer from the crystalline surface. Our results show that the linker length and stiffness play a critical role in the cooperative action of the CD and CBM domains and that, for a given linker length, the steady-state hydrolysis shows a maximum at some intermediate linker stiffness. The maximum hydrolysis rate corresponds to a transition of the linker from a compressed to an extended conformation, where the system exhibits maximum fluctuation, as measured by the variance of the separation distance between the two domains and the dispersion around the mean hydrolysis speed. In the range of experimentally known values of the parameters of our model, improving the intrinsic hydrolytic activity of the CD leads to a proportional increase in the overall hydrolysis rate.
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