Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum - Wikidata - awgldk - TriplyDB

Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum

Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum

http://www.wikidata.org/entity/Q27655782

about

Biological analysis of the microbial metabolism of hetero-oligosaccharides in application to glycotechnology Crystal Structures of a Glycoside Hydrolase Family 20 Lacto-N-biosidase from Bifidobacterium bifidum Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima 1,3-1,4- -L-Fucosynthase That Specifically Introduces Lewis a/x Antigens into Type-1/2 Chains Genomic analysis of three Bifidobacterium species isolated from the calf gastrointestinal tract New structural and functional contexts of the Dx[DN]xDG linear motif: insights into evolution of calcium-binding proteins GH101 family of glycoside hydrolases: subfamily structure and evolutionary connections with other families.Mechanistic investigation of the endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae R6.A novel fluorescent assay for T-synthase activity.α-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to novel glycoside hydrolase family 129 is implicated in alternative mucin degradation pathway.Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism Bifidobacterial enzymes involved in the metabolism of human milk oligosaccharides.Bifidobacterium breve UCC2003 metabolises the human milk oligosaccharides lacto-N-tetraose and lacto-N-neo-tetraose through overlapping, yet distinct pathways.Mucin glycan foraging in the human gut microbiome.The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.Scalable syntheses of both enantiomers of DNJNAc and DGJNAc from glucuronolactone: the effect of N-alkylation on hexosaminidase inhibition.Gene-trait matching across the Bifidobacterium longum pan-genome reveals considerable diversity in carbohydrate catabolism among human infant strains.

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P2860

Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum

http://www.wikidata.org/entity/Q27655782

description

2009 nî lūn-bûn

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2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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Journal of Biochemistry

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Crystallographic and mutationa ...... se from Bifidobacterium longum

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P2093

Hidehiko Kumagai

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Hirofumi Shoun

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Hisashi Ashida

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Kenji Yamamoto

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Motomitsu Kitaoka

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Ryuichiro Suzuki

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Shinya Fushinobu

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Takane Katayama

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Takayoshi Wakagi

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P2860

Processing of X-ray diffraction data collected in oscillation mode

Structural and thermodynamic analyses of solute-binding Protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-N-biose I

The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design

Maximum-likelihood density modification

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

Clustal W and Clustal X version 2.0

ESPript: analysis of multiple sequence alignments in PostScript

Refinement of macromolecular structures by the maximum-likelihood method

Automated MAD and MIR structure solution

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389-98

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scholarly article

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4242830

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10.1093/JB/MVP086

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3

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146

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2009-09-01T00:00:00Z

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19502354

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