ArticleThe Journal of biological chemistry2013
Crystal structures of a glycoside hydrolase family 20 lacto-N-biosidase from Bifidobacterium bifidum.
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 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 61 citations in OpenAlex.
- Structural insights into lacto-N-biose I recognition by a family 32 carbohydrate-binding module from Bifidobacterium bifidum.FEBS letters · 2026Article
- Article
- 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
- Crystal Structure of Glycoside Hydrolase Family 20 Lacto-Journal of applied glycoscience · 2025Article
- The Impact of Bioactive Molecules from Probiotics on Child Health: A Comprehensive Review.Nutrients · 2024Review
- Recent advances in enzymatic properties, preparation methods, and functions of glycoside hydrolase from Bifidobacterium: a review.World journal of microbiology & biotechnology · 2023Review
- Enzymatic Hydrolysis of Human Milk Oligosaccharides. The Molecular Mechanism ofACS catalysis · 2022Article
- FAD-dependentProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and evolution of the bifidobacterial carbohydrate metabolism proteins and enzymes.Biochemical Society transactions · 2021Review
- Transglycosylation Activity of EngineeredInternational journal of molecular sciences · 2021Article
- A Novel GH Family 20 β-N-acetylhexosaminidase With Both Chitosanase and Chitinase Activity FromFrontiers in molecular biosciences · 2021Article
- Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121.PloS one · 2020Article
- 1,6-α-L-Fucosidases fromJournal of applied glycoscience · 2020Article
- Conformations of the type-1 lacto-N-biose I unit in protein complex structures.Acta crystallographica. Section F, Structural biology communications · 2018Review
- Utilization of Host-Derived Glycans by IntestinalFrontiers in microbiology · 2018Review
- Efficient and Regioselective Synthesis of β-GalNAc/GlcNAc-Lactose by a Bifunctional Transglycosylating β-N-Acetylhexosaminidase from Bifidobacterium bifidum.Applied and environmental microbiology · 2016Article
- Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T.The Journal of biological chemistry · 2016Article
- Proteinaceous Molecules Mediating Bifidobacterium-Host Interactions.Frontiers in microbiology · 2016Review
- Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases.PloS one · 2015Article
- 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.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human milk oligosaccharides contain a large variety of oligosaccharides, of which lacto-N-biose I (Gal-β1,3-GlcNAc; LNB) predominates as a major core structure. A unique metabolic pathway specific for LNB has recently been identified in the human commensal bifidobacteria. Several strains of infant gut-associated bifidobacteria possess lacto-N-biosidase, a membrane-anchored extracellular enzyme, that liberates LNB from the nonreducing end of human milk oligosaccharides and plays a key role in the metabolic pathway of these compounds. Lacto-N-biosidase belongs to the glycoside hydrolase family 20, and its reaction proceeds via a substrate-assisted catalytic mechanism. Several crystal structures of GH20 β-N-acetylhexosaminidases, which release monosaccharide GlcNAc from its substrate, have been determined, but to date, a structure of lacto-N-biosidase is unknown. Here, we have determined the first three-dimensional structures of lacto-N-biosidase from Bifidobacterium bifidum JCM1254 in complex with LNB and LNB-thiazoline (Gal-β1,3-GlcNAc-thiazoline) at 1.8-Å resolution. Lacto-N-biosidase consists of three domains, and the C-terminal domain has a unique β-trefoil-like fold. Compared with other β-N-acetylhexosaminidases, lacto-N-biosidase has a wide substrate-binding pocket with a -2 subsite specific for β-1,3-linked Gal, and the residues responsible for Gal recognition were identified. The bound ligands are recognized by extensive hydrogen bonds at all of their hydroxyls consistent with the enzyme's strict substrate specificity for the LNB moiety. The GlcNAc sugar ring of LNB is in a distorted conformation near (4)E, whereas that of LNB-thiazoline is in a (4)C1 conformation. A possible conformational pathway for the lacto-N-biosidase reaction is discussed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.