ArticleFrontiers in microbiology2019
Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans.
Article in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Recombinant Production and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2025Article
- Comparative genomics ofMicrobial genomics · 2025Article
- Synthesis of fucosyllactose using α-L-fucosidases GH29 from infant gut microbial metagenome.Applied microbiology and biotechnology · 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
- Castration alters the cecal microbiota and inhibits growth in Holstein cattle.Journal of animal science · 2022Article
- Detection of Bacterial α-l-Fucosidases with anMolecules (Basel, Switzerland) · 2022Article
- Development of an Autochthonous Microbial Consortium for Enhanced Bioremediation of PAH-Contaminated Soil.International journal of molecular sciences · 2021Article
- Architecture Insight of Bifidobacterial α-L-Fucosidases.International journal of molecular sciences · 2021Article
- Metabolomics Insights in Early Childhood Caries.Journal of dental research · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-L-fucosidases (EC 3.2.1.51, FUC), belonging to the glycoside hydrolase family 29 (GH29), play important roles in several biological processes and are markers used for detecting hepatocellular carcinoma. In this study, a protein sequence similarity network (SSN) was generated and a subsequent evolutionary analysis was performed to understand the enzymes comprehensively. The SSN indicated that the proteins in the FUC family are mainly present in bacteria, fungi, metazoans, plants, as well as in archaea, but less abundantly. The sequences in bacteria were found to be more diverse than those in other taxonomic groups. The SSN and a phylogenetic tree both supported that the proteins in the FUC family can be classified into 3 subfamilies. FUCs in each subfamily are under the pressure of negative selection. The enzymes from metazoans, fungi, and plants separated into the three subfamilies and shared high similarity with the bacterial homologs. The multiple sequence alignment results indicated that the amino acid residues for binding α-L-fucosidase and catalysis are highly conserved in the 3 subfamilies; however, the evolutionary patterns were different, based on the coevolution analysis in the subfamily of metazoans and bacteria. Finally, gene duplication plays an important role for α-L-fucosidase evolution, not only in metazoans, but also in bacteria and fungi.
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