Untangling the Reaction Mechanism of the Polysaccharide Lyase PL42 Using QM/MM Metadynamics Simulations
through umbrella sampling, aligning reasonably with experimental data. Beyond confirming the proposed experimental mechanism, the results demonstrate that PL42 catalyzes β-elimination via a histidine-based catalytic system distinct from those of PL7 and PL38. Additionally, they expand the emerging conformational framework linking polysaccharide lyase mechanisms through their product-ring geometries.
Authors
- Shinya Fushinobu (ORCID: https://orcid.org/0000-0003-1346-6435)
- Santiago Alonso‐Gil (ORCID: https://orcid.org/0000-0001-7596-8161)
- Tatsuya Kondo (ORCID: https://orcid.org/0000-0002-7232-8238)
- Pedro A. Sánchez-Murcia
Institutions
- Medical University of Graz (AT)
- Institut Laue-Langevin (FR)
- BioTechMed-Graz (AT)
- Osaka Metropolitan University (JP)
- The University of Tokyo (JP)
Publication Details
- Journal
- Journal of Chemical Information and Modeling
- Published
- 2026-04-17
- DOI
- https://doi.org/10.1021/acs.jcim.6c00945
- Primary Topic
- Polysaccharides Composition and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Medizinische Universität Graz
- Bundesministerium für Bildung, Wissenschaft und Forschung
- Japan Society for the Promotion of Science