Carbohydrate-Active Enzymes and Glycoside Hydrolase Functionality

Carbohydrate-active enzymes (CAZymes) encompass a broad spectrum of catalysts responsible for the assembly, modification and degradation of oligo- and polysaccharides. Among these, glycoside hydrolases (GHs) play a pivotal role by cleaving glycosidic bonds through proton-donor and nucleophile residues in their active sites. GHs are organised into families based on sequence and structural similarity, each family often displaying multiple substrate specificities and reaction mechanisms, including hydrolysis, transglycosylation and lyase activity. Advances in high-resolution crystallography, sequence-based classification and automated annotation pipelines have revealed the complexity of GH subfamilies, the modular architecture conferred by non-catalytic carbohydrate-binding modules (CBMs) and the diversity of catalytic subsites that dictate chain length, linkage specificity and product profile. Understanding CAZyme functionality at molecular and systems levels underpins applications in biomass conversion, human health, glycoengineering and the design of novel biocatalysts for sustainable bioprocessing.

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Carbohydrate-Active Enzymes and Glycoside Hydrolase Functionality publication trend

The graph below shows the total number of articles in carbohydrate-active enzymes and glycoside hydrolase functionality across all publications each year (not limited to Nature Index journals).

Technical terms

Carbohydrate-active enzymes (CAZymes): A collective term for enzymes that synthesise, modify or break down carbohydrate polymers and oligosaccharides.

Glycoside hydrolases (GHs): Enzymes within CAZymes that hydrolyse glycosidic bonds by general acid–base and nucleophilic catalysis.

CAZy database: An online, expert-curated classification linking CAZyme sequences to families, subfamilies, specificities and structures.

Glycoside hydrolase family 31 (GH31): A large and taxonomically diverse GH family encompassing hydrolases, transglycosidases and lyases with α-glucosidic activities.

Sequence similarity network: A computational framework that groups protein sequences into subfamilies based on pairwise similarity scores to predict functional relationships.

Carbohydrate-binding module (CBM): Non-catalytic protein domains that target CAZymes to specific carbohydrate substrates, enhancing catalytic efficiency.

Conserved unique peptide patterns (CUPP): A motif-based annotation approach using family-specific peptides to assign CAZyme subgroups and predict enzyme functions.

References

1. The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Research (2013).
2. SACCHARIS: an automated pipeline to streamline discovery of carbohydrate active enzyme activities within polyspecific families and de novo sequence datasets. Biotechnology for Biofuels and Bioproducts (2018).
3. Peptide-based functional annotation of carbohydrate-active enzymes by conserved unique peptide patterns (CUPP). Biotechnology for Biofuels and Bioproducts (2019).
4. A subfamily classification to choreograph the diverse activities within glycoside hydrolase family 31. Journal of Biological Chemistry (2023).
5. Structural basis of the strict specificity of a bacterial GH31 α-1,3-glucosidase for nigerooligosaccharides. Journal of Biological Chemistry (2022).