Structural and Functional Dissection of GH161 β-Glucan Phosphorylases: Molecular Specificities and Dynamics of Catalysis of Dimeric GH-Q Enzymes

In the CAZy classification of carbohydrate-active enzymes, the GH-Q clan regroups three distantly related glycoside hydrolase (GH) families: GH94, GH149, and GH161. These families contain glycoside phosphorylases (GPs) that mainly use α–d-glucose-1-phosphate as a glucosyl donor. In the present study, we investigated the structure–function relationships within family GH161, which exhibits β-1,3-glucan phosphorylase activity. Using cryo-electron microscopy (cryo-EM), we determined the dimeric structure of a GH161 enzyme. Comparison between the unliganded form, the acceptor-bound form, and finally a catalytically active complex revealed conformational changes during catalysis that involve coordinated rearrangements within the active site, including loops held by the adjacent protomer. These structural insights, combined with biochemical characterization, deepen our understanding of the molecular determinants driving catalysis in GH-Q enzymes.

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Journal
ACS Catalysis
Published
2025-11-12
DOI
https://doi.org/10.1021/acscatal.5c05191
Primary Topic
Enzyme Production and Characterization
Type
article
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article

Structural and Functional Dissection of GH161 β-Glucan Phosphorylases: Molecular Specificities and Dynamics of Catalysis of Dimeric GH-Q Enzymes

David Ropartz, Claire Moulis, Nicolas Terrapon, Ramteen Shayan et al.
ACS Catalysis
Enzyme Production and Characterization
article

Structural and Functional Dissection of GH161 β-Glucan Phosphorylases: Molecular Specificities and Dynamics of Catalysis of Dimeric GH-Q Enzymes

David Ropartz, Claire Moulis, Nicolas Terrapon, Ramteen Shayan, Vincent Lombard, Gianluca Cioci, Régis Fauré, Simon Ladevèze, Gabrielle Potocki-Véronèse, Ao Li, Bernard Henrissat, Neil R. Cooper, Magali Remaud‐Siméon
article en

Abstract

In the CAZy classification of carbohydrate-active enzymes, the GH-Q clan regroups three distantly related glycoside hydrolase (GH) families: GH94, GH149, and GH161. These families contain glycoside phosphorylases (GPs) that mainly use α–d-glucose-1-phosphate as a glucosyl donor. In the present study, we investigated the structure–function relationships within family GH161, which exhibits β-1,3-glucan phosphorylase activity. Using cryo-electron microscopy (cryo-EM), we determined the dimeric structure of a GH161 enzyme. Comparison between the unliganded form, the acceptor-bound form, and finally a catalytically active complex revealed conformational changes during catalysis that involve coordinated rearrangements within the active site, including loops held by the adjacent protomer. These structural insights, combined with biochemical characterization, deepen our understanding of the molecular determinants driving catalysis in GH-Q enzymes.

ACS CatalysisVol. 15(22)
Centre National de la Recherche Scientifique (FR), Université Fédérale de Toulouse Midi-Pyrénées (FR), Aix-Marseille Université (FR), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Biopolymères Interactions Assemblages (FR), Technical University of Denmark (DK)
Openalex Percentile: Top 64%
Enzyme Production and Characterization
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