ArticleNature communications2020
Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- Calcium enhances hydrolytic and transfucosylation activities in α-L-fucosidase from Thermotoga maritima through catalytic loop stabilization: an MD simulation study.Applied microbiology and biotechnology · 2026Article
- Generating 3D models of complex carbohydrates with GLYCAM-Web.Nature methods · 2026Article
- Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.Microbial biotechnology · 2026Article
- Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease.Nature communications · 2025Article
- Integrative Analysis of Fucosylated Tetra Glycoforms in Hepatocellular Carcinoma: A NanoLC-PRM-MS/MS and Machine Learning Approach.Journal of proteome research · 2025Article
- Structural insights into a fucosidase involved in fucoidan degradation.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.The FEBS journal · 2025Article
- A Robust α-l-Fucosidase fromACS chemical biology · 2024Article
- Exploring the sequence-function space of microbial fucosidases.Communications chemistry · 2024Article
- Synthesis of fucosyllactose using α-L-fucosidases GH29 from infant gut microbial metagenome.Applied microbiology and biotechnology · 2024Article
- Improved Enzymatic Production of the Fucosylated Human Milk Oligosaccharide LNFP II with GH29B α-1,3/4-l-Fucosidases.Journal of agricultural and food chemistry · 2024Article
- α-L-Fucosidases from an Alpaca Faeces Metagenome: Characterisation of Hydrolytic and Transfucosylation Potential.International journal of molecular sciences · 2024Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- Sialidases and fucosidases of Akkermansia muciniphila are crucial for growth on mucin and nutrient sharing with mucus-associated gut bacteria.Nature communications · 2023Article
- Mass Spectrometry-Based Methods to Determine the Substrate Specificities and Kinetics of N-Linked Glycan Hydrolysis by Endo-β-N-Acetylglucosaminidases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis.Structure (London, England : 1993) · 2022Article
- Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates.Microbiology spectrum · 2022Article
- Sculpting therapeutic monoclonal antibody N-glycans using endoglycosidases.Current opinion in structural biology · 2022Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Fucosylation is important for the function of many proteins with biotechnical and medical applications. Alpha-fucosidases comprise a large enzyme family that recognizes fucosylated substrates with diverse α-linkages on these proteins. Lactobacillus casei produces an α-fucosidase, called AlfC, with specificity towards α(1,6)-fucose, the only linkage found in human N-glycan core fucosylation. AlfC and certain point mutants thereof have been used to add and remove fucose from monoclonal antibody N-glycans, with significant impacts on their effector functions. Despite the potential uses for AlfC, little is known about its mechanism. Here, we present crystal structures of AlfC, combined with mutational and kinetic analyses, hydrogen-deuterium exchange mass spectrometry, molecular dynamic simulations, and transfucosylation experiments to define the molecular mechanisms of the activities of AlfC and its transfucosidase mutants. Our results indicate that AlfC creates an aromatic subsite adjacent to the active site that specifically accommodates GlcNAc in α(1,6)-linkages, suggest that enzymatic activity is controlled by distinct open and closed conformations of an active-site loop, with certain mutations shifting the equilibrium towards open conformations to promote transfucosylation over hydrolysis, and provide a potentially generalizable framework for the rational creation of AlfC transfucosidase mutants.
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Registered trials
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