ArticleThe Journal of biological chemistry2012
1,3-1,4-α-L-fucosynthase that specifically introduces Lewis a/x antigens into type-1/2 chains.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 93 citations in OpenAlex.
- Fucoidans: a new frontier in brown seaweed research and biotechnology.Cell surface (Amsterdam, Netherlands) · 2026Review
- Computationally guided enzyme engineering for regioselective synthesis of fucosylated human milk oligosaccharides.Applied microbiology and biotechnology · 2026Article
- Structural insights into a fucosidase involved in fucoidan degradation.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-Food chemistry. Molecular sciences · 2025Article
- Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.The FEBS journal · 2025Article
- Glycosphingolipids: from metabolism to chemoenzymatic total synthesis.Organic & biomolecular chemistry · 2024Review
- Recent advances of 3-fucosyllactose in health effects and production.Archives of microbiology · 2024Review
- 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
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- The dual role of fucosidases: tool or target.Biologia · 2023Review
- Preferential sugar utilization by bifidobacterial species.Microbiome research reports · 2023Article
- Cryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis.Structure (London, England : 1993) · 2022Article
- Diversification of a Fucosyllactose Transporter within the GenusApplied and environmental microbiology · 2022Article
- Structure and evolution of the bifidobacterial carbohydrate metabolism proteins and enzymes.Biochemical Society transactions · 2021Review
- Fucosidases from the human gut symbiont Ruminococcus gnavus.Cellular and molecular life sciences : CMLS · 2021Article
- Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.Nature communications · 2020Article
- Improved Transglycosylation by a Xyloglucan-Active α-l-Fucosidase fromJournal of fungi (Basel, Switzerland) · 2020Article
- Functional exploration of the GH29 fucosidase family.Glycobiology · 2020Article
- Human milk and mucosa-associated disaccharides impact on cultured infant fecal microbiota.Scientific reports · 2020Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-L-fucosyl residues attached at the non-reducing ends of glycoconjugates constitute histo-blood group antigens Lewis (Le) and ABO and play fundamental roles in various biological processes. Therefore, establishing a method for synthesizing the antigens is important for functional glycomics studies. However, regiospecific synthesis of glycosyl linkages, especially α-L-fucosyl linkages, is quite difficult to control both by chemists and enzymologists. Here, we generated an α-L-fucosynthase that specifically introduces Le(a) and Le(x) antigens into the type-1 and type-2 chains, respectively; i.e. the enzyme specifically accepts the disaccharide structures (Galβ1-3/4GlcNAc) at the non-reducing ends and attaches a Fuc residue via an α-(1,4/3)-linkage to the GlcNAc. X-ray crystallographic studies revealed the structural basis of this strict regio- and acceptor specificity, which includes the induced fit movement of the catalytically important residues, and the difference between the active site structures of 1,3-1,4-α-L-fucosidase (EC 3.2.1.111) and α-L-fucosidase (EC 3.2.1.51) in glycoside hydrolase family 29. The glycosynthase developed in this study should serve as a potentially powerful tool to specifically introduce the Le(a/x) epitopes onto labile glycoconjugates including glycoproteins. Mining glycosidases with strict specificity may represent the most efficient route to the specific synthesis of glycosidic bonds.
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