ArticleInternational journal of molecular sciences2021
Architecture Insight of Bifidobacterial α-L-Fucosidases.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Regulation of infant gut microbiota and metabolic pathways by human milk oligosaccharides: a multi-omics investigation.RSC advances · 2026Article
- FUT2-mediated intestinal fucosylation: a master regulator of host-microbiota symbiosis in health and disease.Frontiers in microbiology · 2026Review
- Recombinant Production and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2025Article
- Characterization and stabilization of GluLm and its application to deglycosylate dietary flavonoids and lignans.Applied microbiology and biotechnology · 2024Article
- The many functions of carbohydrate-active enzymes in family GH65: diversity and application.Applied microbiology and biotechnology · 2024Review
- Exploring the sequence-function space of microbial fucosidases.Communications chemistry · 2024Article
- Intestinal persistence of Bifidobacterium infantis is determined by interaction of host genetics and antibiotic exposure.The ISME journal · 2024Article
- Characterization and stabilization of the α-L-fucosidase set from Lacticaseibacillus rhamnosus INIA P603.Applied microbiology and biotechnology · 2022Article
- Genome analysis and 2'-fucosyllactose utilization characteristics of a new Akkermansia muciniphila strain isolated from mice feces.Molecular genetics and genomics : MGG · 2022Article
- How microbial glycosyl hydrolase activity in the gut mucosa initiates microbial cross-feeding.Glycobiology · 2022Review
- Assortment of Frontiers in Protein Science.International journal of molecular sciences · 2022Article
- Identification of α-L-fucosidase (ALFuc) of Blastocystis sp. subtypes ST1, ST2 and ST3.Revista do Instituto de Medicina Tropical de Sao Paulo · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Fucosylated carbohydrates and glycoproteins from human breast milk are essential for the development of the gut microbiota in early life because they are selectively metabolized by bifidobacteria. In this regard, α-L-fucosidases play a key role in this successful bifidobacterial colonization allowing the utilization of these substrates. Although a considerable number of α-L-fucosidases from bifidobacteria have been identified by computational analysis, only a few of them have been characterized. Hitherto, α-L-fucosidases are classified into three families: GH29, GH95, and GH151, based on their catalytic structure. However, bifidobacterial α-L-fucosidases belonging to a particular family show significant differences in their sequence. Because this fact could underlie distinct phylogenetic evolution, here extensive similarity searches and comparative analyses of the bifidobacterial α-L-fucosidases identified were carried out with the assistance of previous physicochemical studies available. This work reveals four and two paralogue bifidobacterial fucosidase groups within GH29 and GH95 families, respectively. Moreover,
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Registered trials
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