Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.
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Proteinaceous Molecules Mediating Bifidobacterium-Host InteractionsThe impact of the milk glycobiome on the neonate gut microbiotaCrystal Structures of a Glycoside Hydrolase Family 20 Lacto-N-biosidase from Bifidobacterium bifidumOligosaccharide binding proteins from Bifidobacterium longum subsp. infantis reveal a preference for host glycansThe predominance of type I oligosaccharides is a feature specific to human breast milkConsumption of human milk glycoconjugates by infant-associated bifidobacteria: mechanisms and implications.How glycan metabolism shapes the human gut microbiota.Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foragingMolecular dialogue between the human gut microbiota and the host: a Lactobacillus and Bifidobacterium perspective.Utilisation of mucin glycans by the human gut symbiont Ruminococcus gnavus is strain-dependentCarbohydrate metabolism in Bifidobacteria.Physiology of consumption of human milk oligosaccharides by infant gut-associated bifidobacteria.Insights from genomes of representatives of the human gut commensal Bifidobacterium bifidum.4-O-Acetyl-sialic acid (Neu4,5Ac2) in acidic milk oligosaccharides of the platypus (Ornithorhynchus anatinus) and its evolutionary significance.Backbone structures in human milk oligosaccharides: trans-glycosylation by metagenomic β-N-acetylhexosaminidases.α-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to novel glycoside hydrolase family 129 is implicated in alternative mucin degradation pathway.Gut Immunity and Type 1 Diabetes: a Mélange of Microbes, Diet, and Host Interactions?The Extracellular Wall-Bound β-N-Acetylglucosaminidase from Lactobacillus casei Is Involved in the Metabolism of the Human Milk Oligosaccharide Lacto-N-TrioseA molecular basis for bifidobacterial enrichment in the infant gastrointestinal tractBifidobacterial enzymes involved in the metabolism of human milk oligosaccharides.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 expressionEfficient and Regioselective Synthesis of β-GalNAc/GlcNAc-Lactose by a Bifunctional Transglycosylating β-N-Acetylhexosaminidase from Bifidobacterium bifidum.Variation in consumption of human milk oligosaccharides by infant gut-associated strains of Bifidobacterium breve.Bifidobacterium breve UCC2003 metabolises the human milk oligosaccharides lacto-N-tetraose and lacto-N-neo-tetraose through overlapping, yet distinct pathways.Protein-Linked Glycan Degradation in Infants Fed Human Milk.α-N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes α-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin.Bifidobacterial α-galactosidase with unique carbohydrate-binding module specifically acts on blood group B antigen.Glycoside hydrolase family 89 alpha-N-acetylglucosaminidase from Clostridium perfringens specifically acts on GlcNAc alpha1,4Gal beta1R at the non-reducing terminus of O-glycans in gastric mucin.Mucin glycan foraging in the human gut microbiome.Host-derived glycans serve as selected nutrients for the gut microbe: human milk oligosaccharides and bifidobacteria.The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.Sequential one-pot multienzyme (OPME) synthesis of lacto-N-neotetraose and its sialyl and fucosyl derivatives.Bifidobacterium bifidum Extracellular Sialidase Enhances Adhesion to the Mucosal Surface and Supports Carbohydrate Assimilation.An exo-alpha-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates.Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.Bifidobacterium longum subsp. infantis uses two different β-galactosidases for selectively degrading type-1 and type-2 human milk oligosaccharides.Cloning and expression of a β-galactosidase gene of Bacillus circulans.The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine.Sharing of human milk oligosaccharides degradants within bifidobacterial communities in faecal cultures supplemented with Bifidobacterium bifidumUtilization of Host-Derived Glycans by Intestinal and Species
P2860
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P2860
Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh-hant
name
Cooperation of β-galactosidase ...... harides with type 2 structure.
@en
Cooperation of β-galactosidase ...... harides with type 2 structure.
@nl
type
label
Cooperation of β-galactosidase ...... harides with type 2 structure.
@en
Cooperation of β-galactosidase ...... harides with type 2 structure.
@nl
prefLabel
Cooperation of β-galactosidase ...... harides with type 2 structure.
@en
Cooperation of β-galactosidase ...... harides with type 2 structure.
@nl
P2093
P2860
P356
P1433
P1476
Cooperation of β-galactosidase ...... harides with type 2 structure.
@en
P2093
Hisashi Ashida
Kenji Yamamoto
Masashi Kiyohara
Takane Katayama
Tomohiro Horimoto
P2860
P304
P356
10.1093/GLYCOB/CWQ101
P577
2010-06-24T00:00:00Z