ReviewEssays in biochemistry2023
Structure and function of microbial α-l-fucosidases: a mini review.
Review in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Senescence-associated loss of intestinal α1,2-fucose disrupts a modifiable host-microbiome homeostasis axis in people with HIV.bioRxiv : the preprint server for biology · 2026Article
- Optimisation of selection for methane mitigation by integrating production traits with ruminal microbiome-driven breeding in beef cattle.Genetics, selection, evolution : GSE · 2026Article
- Impact of 1,2-α-L-fucosidase on pig enteric methane production and growth performance.Animal microbiome · 2026Article
- Efficient mucin O-glycan degradation by specific mucin degrading intestinal bacteria: towards understanding enzyme-glycan interactions.Glycobiology · 2026Article
- Ligand-modified multifunctional liposome-based targeted delivery platform: a multimodal cancer combination therapy strategy.Theranostics · 2026Review
- Multi-omics and field experiments reveal the mechanism of Pseudomonas palleroniana P6 promoting the growth and polyphyllins accumulation in Paris polyphylla.BMC plant biology · 2025Article
- Recombinant Production and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2025Article
- An l-fucose-responsive transcription factor cross-regulates the expression of a diverse array of carbohydrate-active enzymes in Trichoderma reesei.PLoS genetics · 2025Article
- Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.The FEBS journal · 2025Article
- Mechanisms of recalcitrant fucoidan breakdown in marine Planctomycetota.Nature communications · 2024Article
- Pangenome comparison ofmSystems · 2024Article
- Exploring the sequence-function space of microbial fucosidases.Communications chemistry · 2024Article
- Genome Analysis of Multiple Polysaccharide-Degrading Bacterium Microbulbifer thermotolerans HB226069: Determination of Alginate Lyase Activity.Marine biotechnology (New York, N.Y.) · 2024Article
- Synthesis of fucosyllactose using α-L-fucosidases GH29 from infant gut microbial metagenome.Applied microbiology and biotechnology · 2024Article
- Mechanism of 2'-fucosyllactose degradation by human-associatedJournal of bacteriology · 2024Article
- Simulated digestions of free oligosaccharides and mucin-type O-glycans reveal a potential role for Clostridium perfringens.Scientific reports · 2024Article
- Immunomodulating Enzymes fromMicroorganisms · 2024Review
- α-L-Fucosidases from an Alpaca Faeces Metagenome: Characterisation of Hydrolytic and Transfucosylation Potential.International journal of molecular sciences · 2024Article
- Pangenome comparison ofbioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Fucose is a monosaccharide commonly found in mammalian, insect, microbial and plant glycans. The removal of terminal α-l-fucosyl residues from oligosaccharides and glycoconjugates is catalysed by α-l-fucosidases. To date, glycoside hydrolases (GHs) with exo-fucosidase activity on α-l-fucosylated substrates (EC 3.2.1.51, EC 3.2.1.-) have been reported in the GH29, GH95, GH139, GH141 and GH151 families of the Carbohydrate Active Enzymes (CAZy) database. Microbes generally encode several fucosidases in their genomes, often from more than one GH family, reflecting the high diversity of naturally occuring fucosylated structures they encounter. Functionally characterised microbial α-l-fucosidases have been shown to act on a range of substrates with α-1,2, α-1,3, α-1,4 or α-1,6 fucosylated linkages depending on the GH family and microorganism. Fucosidases show a modular organisation with catalytic domains of GH29 and GH151 displaying a (β/α)8-barrel fold while GH95 and GH141 show a (α/α)6 barrel and parallel β-helix fold, respectively. A number of crystal structures have been solved in complex with ligands, providing structural basis for their substrate specificity. Fucosidases can also be used in transglycosylation reactions to synthesise oligosaccharides. This mini review provides an overview of the enzymatic and structural properties of microbial α-l-fucosidases and some insights into their biological function and biotechnological applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.