ArticleJournal of bacteriology2004
Molecular cloning and characterization of Bifidobacterium bifidum 1,2-alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95).
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.
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Who cites it
125 citing papers in PubMed, 260 citations in OpenAlex.
- Ratio-Dependent Regulation of Butyrate Production by 2'-Fucosyllactose and Fructooligosaccharides in aMicroorganisms · 2026Article
- bifidoAnnotator: fine-grained annotation of bifidobacterial glycoside hydrolases for human milk glycan utilization.Microbial genomics · 2026Article
- Expanding the Toolbox for Inducible Protein Expression With Automation-enabled Generation of Glycomimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Article
- Human milk oligosaccharide metabolism and antibiotic resistance in early gut colonizers: insights from bifidobacteria and lactobacilli in the maternal-infant microbiome.Gut microbes · 2025Article
- Gut mucin fucosylation dictates the entry of botulinum toxin complexes.Nature communications · 2025Article
- Emergent roles of infant gut microbes during the utilization of human milk oligosaccharides.NPJ biofilms and microbiomes · 2025Article
- Gut mucin fucosylation dictates the entry of botulinum toxin complexes.bioRxiv : the preprint server for biology · 2025Article
- Article
- An l-fucose-responsive transcription factor cross-regulates the expression of a diverse array of carbohydrate-active enzymes in Trichoderma reesei.PLoS genetics · 2025Article
- HMOs Induce Butyrate Production ofMicroorganisms · 2025Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Probiotic Bifidobacterium bifidum strains desialylate MUC13 and increase intestinal epithelial barrier function.Scientific reports · 2025Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Variation in the Conservation of Species-Specific Gene Sets for HMO Degradation and Its Effects on HMO Utilization in Bifidobacteria.Nutrients · 2024Article
- Linking human milk oligosaccharide metabolism and early life gut microbiota: bifidobacteria and beyond.Microbiology and molecular biology reviews : MMBR · 2024Review
- Molecular strategies for the utilisation of human milk oligosaccharides by infant gut-associated bacteria.FEMS microbiology reviews · 2023Review
- Comparison of the relative impacts of acute consumption of an inulin-enriched diet, milk kefir or a commercial probiotic product on the human gut microbiome and metabolome.NPJ science of food · 2023Article
- Mucin glycans and their degradation by gut microbiota.Glycoconjugate journal · 2023Review
- The Enzymatic Hydrolysis of Human Milk Oligosaccharides and Prebiotic Sugars from LAB Isolated from Breast Milk.Microorganisms · 2023Article
65 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the alpha-(1-->2) linkage of 2'-fucosyllactose, and a gene encoding 1,2-alpha-l-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted molecular mass of 205 kDa and containing a signal peptide and a membrane anchor at the N and C termini, respectively. A domain responsible for fucosidase activity (the Fuc domain; amino acid residues 577 to 1474) was localized by deletion analysis and then purified as a hexahistidine-tagged protein. The recombinant Fuc domain specifically hydrolyzed the terminal alpha-(1-->2)-fucosidic linkages of various oligosaccharides and a sugar chain of a glycoprotein. The stereochemical course of the hydrolysis of 2'-fucosyllactose was determined to be inversion by using (1)H nuclear magnetic resonance. The primary structure of the Fuc domain exhibited no similarity to those of any glycoside hydrolases (GHs) but showed high similarity to those of several hypothetical proteins in a database. Thus, it was revealed that the AfcA protein constitutes a novel inverting GH family (GH family 95).
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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.