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Conformational gating mechanism for processive catalysis of β(1,3)-glucans
Abstract Processive catalysis is a fundamental molecular mechanism to build and dismantle complex biopolymers such as nucleic acids, proteins and carbohydrates, underpinning a myriad of biotechnological applications. Here, we uncover a processive mechanism for the breakdown of β(1,3)-glucans, a widespread carbohydrate class. This mechanism involves a dynamic active site, which adopts a tunnel-like conformation upon substrate binding.
Publisher Correction: A metagenomic ‘dark matter’ enzyme catalyses oxidative cellulose conversion - Nature
Correction to: Nature https://doi.org/10.1038/s41586-024-08553-z Published online 12 February 2025 In the version of the article initially published, in Fig. 2d, the y-axis label was a duplicate of Fig. 2c, and has now been amened to read “Bound enzyme (μmol of CelOCE per g Avicel)”, while there was an extra hydrogen in the middle chemical structure of Fig. 4b, as seen in Fig. 1. The figures have now been corrected in the HTML and PDF versions of the article.
A metagenomic ‘dark matter’ enzyme catalyses oxidative cellulose conversion - Nature
Abstract The breakdown of cellulose is one of the most important reactions in nature1,2 and is central to biomass conversion to fuels and chemicals3. However, the microfibrillar organization of cellulose and its complex interactions with other components of the plant cell wall poses a major challenge for enzymatic conversion4.
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