ArticleThe Journal of biological chemistry2013
Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Effect of Probiotics on the Gut-Mammary Pathway: Implications on Infant Microbiota Transfer and Development.Current nutrition reports · 2026Review
- Genomic characterization ofApplied and environmental microbiology · 2026Article
- Gastrointestinal Journey of Human Milk Oligosaccharides: From Breastfeeding Origins to Functional Roles in Adults.Microorganisms · 2025Review
- Human milk oligosaccharide metabolism and antibiotic resistance in early gut colonizers: insights from bifidobacteria and lactobacilli in the maternal-infant microbiome.Gut microbes · 2025Article
- Article
- Integrative genomic reconstruction reveals heterogeneity in carbohydrate utilization across human gut bifidobacteria.Nature microbiology · 2025Article
- Integrative genomic reconstruction reveals heterogeneity in carbohydrate utilization across human gut bifidobacteria.bioRxiv : the preprint server for biology · 2025Article
- Discovery of Lacto-N-Biosidases and a Novel N-Acetyllactosaminidase Activity in the CAZy Family GH20: Functional Diversity and Structural Insights.Chembiochem : a European journal of chemical biology · 2025Article
- 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
- GH136-encoding gene (perB) is involved in gut colonization and persistence by Bifidobacterium bifidum PRL2010.Microbial biotechnology · 2024Article
- Review
- Gut Microbiota and Its Role in Anti-aging Phenomenon: Evidence-Based Review.Applied biochemistry and biotechnology · 2023Review
- Molecular strategies for the utilisation of human milk oligosaccharides by infant gut-associated bacteria.FEMS microbiology reviews · 2023Review
- Study of the biosynthesis and functionality of polyphosphate in Bifidobacterium longum KABP042.Scientific reports · 2023Article
- A bacterial sulfoglycosidase highlights mucin O-glycan breakdown in the gut ecosystem.Nature chemical biology · 2023Article
- Fungal β-glucan-facilitated cross-feeding activities between Bacteroides and Bifidobacterium species.Communications biology · 2023Article
- Preferential sugar utilization by bifidobacterial species.Microbiome research reports · 2023Article
- Substrate recognition mode of a glycoside hydrolase family 42 β-galactosidase fromMicrobiome research reports · 2023Article
- Characterization and Identification of Probiotic Features in Lacticaseibacillus Paracasei Using a Comparative Genomic Analysis Approach.Probiotics and antimicrobial proteins · 2022Article
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12 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Infant gut-associated bifidobacteria possess species-specific enzymatic sets to assimilate human milk oligosaccharides, and lacto-N-biosidase (LNBase) is a key enzyme that degrades lacto-N-tetraose (Galβ1-3GlcNAcβ1-3Galβ1-4Glc), the main component of human milk oligosaccharides, to lacto-N-biose I (Galβ1-3GlcNAc) and lactose. We have previously identified LNBase activity in Bifidobacterium bifidum and some strains of Bifidobacterium longum subsp. longum (B. longum). Subsequently, we isolated a glycoside hydrolase family 20 (GH20) LNBase from B. bifidum; however, the genome of the LNBase(+) strain of B. longum contains no GH20 LNBase homolog. Here, we reveal that locus tags BLLJ_1505 and BLLJ_1506 constitute LNBase from B. longum JCM1217. The gene products, designated LnbX and LnbY, respectively, showed no sequence similarity to previously characterized proteins. The purified enzyme, which consisted of LnbX only, hydrolyzed via a retaining mechanism the GlcNAcβ1-3Gal linkage in lacto-N-tetraose, lacto-N-fucopentaose I (Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4Glc), and sialyllacto-N-tetraose a (Neu5Acα2-3Galβ1-3GlcNAcβ1-3Galβ1-4Gal); the latter two are not hydrolyzed by GH20 LNBase. Among the chromogenic substrates examined, the enzyme acted on p-nitrophenyl (pNP)-β-lacto-N-bioside I (Galβ1-3GlcNAcβ-pNP) and GalNAcβ1-3GlcNAcβ-pNP. GalNAcβ1-3GlcNAcβ linkage has been found in O-mannosyl glycans of α-dystroglycan. Therefore, the enzyme may serve as a new tool for examining glycan structures. In vitro refolding experiments revealed that LnbY and metal ions (Ca(2+) and Mg(2+)) are required for proper folding of LnbX. The LnbX and LnbY homologs have been found only in B. bifidum, B. longum, and a few gut microbes, suggesting that the proteins have evolved in specialized niches.
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