Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases

Michelle Teune, Plínio S. Vieira, Thorben Döhler, Gottfried J. Palm, Theresa Dutschei, Daniel Bartosik, Leona Berndt, Gabriela F. Persinoti, Sandra Maaß, Dörte Becher, Thomas Schweder, Mário T. Murakami (), Michael Lammers () and Uwe T. Bornscheuer ()
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Michelle Teune: University Greifswald
Plínio S. Vieira: Brazilian Center for Research in Energy and Materials (CNPEM)
Thorben Döhler: University Greifswald
Gottfried J. Palm: University of Greifswald
Theresa Dutschei: University Greifswald
Daniel Bartosik: University of Greifswald
Leona Berndt: University of Greifswald
Gabriela F. Persinoti: Brazilian Center for Research in Energy and Materials (CNPEM)
Sandra Maaß: University of Greifswald
Dörte Becher: University of Greifswald
Thomas Schweder: University of Greifswald
Mário T. Murakami: Brazilian Center for Research in Energy and Materials (CNPEM)
Michael Lammers: University of Greifswald
Uwe T. Bornscheuer: University Greifswald

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract Carbohydrate esterases modify polysaccharides by removing different ester moieties thereby affecting their physicochemical properties and their accessibility by glycoside hydrolases. We determined the full-length structures of two members (Fl8CE20_II and PpCE20_II) from the carbohydrate esterase family 20 (CE20) by X-ray crystallography that feature an ancillary domain, inserted into the catalytic SGNH-hydrolase domain. Detailed structural analysis identifies a so far undescribed catalytic triad architecture which lacks the typical aspartate for polarization of the histidine but instead reveals a precisely coordinated water molecule mediating contact between the His and Asp. This coordinated water in the Ser-His-(H2O-Asp/Asn) motif, as further confirmed by mutational studies and by determination of kinetic constants, is crucial for catalytic activity. We therefore term this active site architecture a water-mediated catalytic triad.

Date: 2025
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DOI: 10.1038/s41467-025-62387-5

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