Journal of Biological Chemistry, ISSN 0021-9258, 02/2008, Volume 283, Issue 8, pp. 4469 - 4479
Endo-beta-N-acetylglucosaminidase from Mucor hiemalis(Endo-M), a family 85 glycoside hydrolase, acts on the beta 1,4 linkage of N,N'-diacetylchitobiose moiety...
COMPLEX | OLIGOSACCHARIDES | ENZYME | CHEMOENZYMATIC SYNTHESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUBSTRATE-ASSISTED CATALYSIS | MOLECULAR-CLONING | GLYCOSYLATION | GLYCOPEPTIDES | Glycoproteins - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Mucor - enzymology | Mucor - genetics | Mutagenesis, Site-Directed | Viral Proteins - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Binding Sites - genetics | Mutation, Missense | Disaccharides - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Substrate Specificity - genetics | Anti-HIV Agents - chemistry | HIV-1 - chemistry | Catalysis | Kinetics | Carbohydrate Conformation | Glycoproteins - chemistry | Amino Acid Substitution
COMPLEX | OLIGOSACCHARIDES | ENZYME | CHEMOENZYMATIC SYNTHESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUBSTRATE-ASSISTED CATALYSIS | MOLECULAR-CLONING | GLYCOSYLATION | GLYCOPEPTIDES | Glycoproteins - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Mucor - enzymology | Mucor - genetics | Mutagenesis, Site-Directed | Viral Proteins - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Binding Sites - genetics | Mutation, Missense | Disaccharides - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Substrate Specificity - genetics | Anti-HIV Agents - chemistry | HIV-1 - chemistry | Catalysis | Kinetics | Carbohydrate Conformation | Glycoproteins - chemistry | Amino Acid Substitution
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 14, pp. 11272 - 11281
Endo-beta-N-acetylglucosaminidase from Streptococcus pneumoniae (Endo-D) is an endoglycosidase capable of hydrolyzing the Fc N-glycan of intact IgG antibodies...
SUBSTRATE-SPECIFICITY | PRIMARY SEQUENCE | STRUCTURAL BASIS | CHEMOENZYMATIC SYNTHESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GLYCOPROTEINS | MOLECULAR-CLONING | ASPARAGINE-LINKED OLIGOSACCHARIDES | FLAVOBACTERIUM-MENINGOSEPTICUM | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Fucose - metabolism | Ligases - genetics | Mutant Proteins - genetics | Molecular Sequence Data | Mutant Proteins - metabolism | Glycosylation | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Hydrolysis | Immunoglobulin G - genetics | Mutant Proteins - chemistry | Cloning, Molecular | Protein Engineering | Kinetics | Streptococcus pneumoniae - enzymology | Immunoglobulin G - metabolism | Transglycosylation | Glycosynthase | Glycoside Hydrolases | Enzyme Catalysis | Oligosaccharide | Glycoprotein | Glycobiology and Extracellular Matrices | Glycoconjugate
SUBSTRATE-SPECIFICITY | PRIMARY SEQUENCE | STRUCTURAL BASIS | CHEMOENZYMATIC SYNTHESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GLYCOPROTEINS | MOLECULAR-CLONING | ASPARAGINE-LINKED OLIGOSACCHARIDES | FLAVOBACTERIUM-MENINGOSEPTICUM | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Fucose - metabolism | Ligases - genetics | Mutant Proteins - genetics | Molecular Sequence Data | Mutant Proteins - metabolism | Glycosylation | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Hydrolysis | Immunoglobulin G - genetics | Mutant Proteins - chemistry | Cloning, Molecular | Protein Engineering | Kinetics | Streptococcus pneumoniae - enzymology | Immunoglobulin G - metabolism | Transglycosylation | Glycosynthase | Glycoside Hydrolases | Enzyme Catalysis | Oligosaccharide | Glycoprotein | Glycobiology and Extracellular Matrices | Glycoconjugate
Journal Article
ChemBioChem, ISSN 1439-4227, 01/2018, Volume 19, Issue 2, pp. 136 - 141
To demonstrate the structural specificity of the glycosyl donor for the transglycosylation reaction by using endo‐β‐N‐acetylglucosaminidase from Mucor hiemalis...
carbohydrates | enzymes | glycosylation | chemical modification | structural specificity | CHEMISTRY, MEDICINAL | OLIGOSACCHARIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOPROTEINS | ENZYME | CHEMOENZYMATIC SYNTHESIS | SUBSTRATE | PURIFICATION | MICROBIAL ENDOGLYCOSIDASE | GLYCOPEPTIDES | OXAZOLINE DONORS | Mucor - enzymology | Oxazoles - metabolism | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Oligosaccharides - chemistry | Protein Conformation | Glycosylation | Molecular Structure | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Oligosaccharides - biosynthesis | Oxazoles - chemistry
carbohydrates | enzymes | glycosylation | chemical modification | structural specificity | CHEMISTRY, MEDICINAL | OLIGOSACCHARIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOPROTEINS | ENZYME | CHEMOENZYMATIC SYNTHESIS | SUBSTRATE | PURIFICATION | MICROBIAL ENDOGLYCOSIDASE | GLYCOPEPTIDES | OXAZOLINE DONORS | Mucor - enzymology | Oxazoles - metabolism | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Oligosaccharides - chemistry | Protein Conformation | Glycosylation | Molecular Structure | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Oligosaccharides - biosynthesis | Oxazoles - chemistry
Journal Article
Glycobiology, ISSN 0959-6658, 06/2013, Volume 23, Issue 6, pp. 736 - 744
In four yeast strains, Ogataea minuta, Candida parapolymorpha, Pichia anomala and Zygosaccharomyces rouxii, we identified endo-beta-N-acetylglucosaminidase...
Endo-Om | transglycosylation | Ogataea minuta | Endo-β-N-acetylglucosaminidase | yeast | RETICULUM-ASSOCIATED DEGRADATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SACCHAROMYCES-CEREVISIAE | POLYMANNOSE OLIGOSACCHARIDES | FREE OLIGOSACCHARIDES | CAENORHABDITIS-ELEGANS | Endo-beta-N-acetylglucosaminidase | ENDOPLASMIC-RETICULUM | MOLECULAR-CLONING | CYTOSOL | EXPRESSION | Fungal Proteins - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Fungal Proteins - biosynthesis | Ribonucleases - chemistry | Humans | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - biosynthesis | Molecular Sequence Data | Glycosylation | Fungal Proteins - genetics | Phylogeny | Saccharomycetales - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Sequence Analysis, DNA | Hydrolysis | Sequence Homology, Amino Acid | Base Sequence | Oligosaccharides - chemistry | Cloning, Molecular | Transferrin - chemistry | Protein Processing, Post-Translational
Endo-Om | transglycosylation | Ogataea minuta | Endo-β-N-acetylglucosaminidase | yeast | RETICULUM-ASSOCIATED DEGRADATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SACCHAROMYCES-CEREVISIAE | POLYMANNOSE OLIGOSACCHARIDES | FREE OLIGOSACCHARIDES | CAENORHABDITIS-ELEGANS | Endo-beta-N-acetylglucosaminidase | ENDOPLASMIC-RETICULUM | MOLECULAR-CLONING | CYTOSOL | EXPRESSION | Fungal Proteins - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Fungal Proteins - biosynthesis | Ribonucleases - chemistry | Humans | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - biosynthesis | Molecular Sequence Data | Glycosylation | Fungal Proteins - genetics | Phylogeny | Saccharomycetales - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Sequence Analysis, DNA | Hydrolysis | Sequence Homology, Amino Acid | Base Sequence | Oligosaccharides - chemistry | Cloning, Molecular | Transferrin - chemistry | Protein Processing, Post-Translational
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2017, Volume 12, Issue 8, p. e0183589
A plant transient expression system, with eukaryotic post-translational modification machinery, offers superior efficiency, scalability, safety, and lower cost...
ANTIBODIES | TRANSMISSION-BLOCKING IMMUNITY | TRANSIENT EXPRESSION | PRECURSOR | PLASMODIUM-FALCIPARUM | MULTIDISCIPLINARY SCIENCES | VACCINE CANDIDATE PFS48/45 | PURIFICATION | ANTIGENS | GLYCOSYLATION | EPITOPES | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Streptomyces - metabolism | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Tobacco - metabolism | Cloning, Molecular | Glycosylation | Plant Proteins - biosynthesis | Recombinant Proteins - biosynthesis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Glucosamine | Peptides | Agricultural biotechnology | Antibodies | Amino acids | Plants (organisms) | Vaccines | Machinery | Proteins | Polysaccharides | Post-translation | Bacteria | N-glycosidase | Recombinant | Enzymes | Antigens | Deglycosylation | Immunoglobulins | N-Acetylglucosaminidase | Malaria | Glycoproteins | N-Acetyl-D-glucosamine | Oligosaccharides | Biological activity | N-linked glycans | Asparagine | Monoclonal antibodies | In vivo methods and tests | Production capacity | Aberration | Conformation
ANTIBODIES | TRANSMISSION-BLOCKING IMMUNITY | TRANSIENT EXPRESSION | PRECURSOR | PLASMODIUM-FALCIPARUM | MULTIDISCIPLINARY SCIENCES | VACCINE CANDIDATE PFS48/45 | PURIFICATION | ANTIGENS | GLYCOSYLATION | EPITOPES | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Streptomyces - metabolism | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Tobacco - metabolism | Cloning, Molecular | Glycosylation | Plant Proteins - biosynthesis | Recombinant Proteins - biosynthesis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Glucosamine | Peptides | Agricultural biotechnology | Antibodies | Amino acids | Plants (organisms) | Vaccines | Machinery | Proteins | Polysaccharides | Post-translation | Bacteria | N-glycosidase | Recombinant | Enzymes | Antigens | Deglycosylation | Immunoglobulins | N-Acetylglucosaminidase | Malaria | Glycoproteins | N-Acetyl-D-glucosamine | Oligosaccharides | Biological activity | N-linked glycans | Asparagine | Monoclonal antibodies | In vivo methods and tests | Production capacity | Aberration | Conformation
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 02/2018, Volume 125, Issue 2, pp. 168 - 174
Endo-β- -acetylglucosaminidase from the methylotrophic yeast (Endo-Om) is a glycoside hydrolase family 85 enzyme that has dual catalytic activity in the...
Endo-Om | N-glycan | Ogataea minuta | Glycosidase family 85 | Endo-β-N-acetylglucosaminidase | SPECIFICITY | CRYSTAL-STRUCTURE | FOOD SCIENCE & TECHNOLOGY | ASPARAGINE-LINKED OLIGOSACCHARIDES | SWISS-MODEL | ENZYME | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SUBSTRATE | Endo-beta-N-acetylglucosaminidase | MOLECULAR-CLONING | GLYCOPEPTIDES | EXPRESSION | TRANSGLYCOSYLATION | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mutagenesis, Site-Directed | Tryptophan - genetics | Models, Molecular | Oligosaccharides - metabolism | Saccharomycetales - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Tryptophan - metabolism | Hydrolysis | Mannose - metabolism | Saccharomycetales - genetics | Conserved Sequence | Index Medicus
Endo-Om | N-glycan | Ogataea minuta | Glycosidase family 85 | Endo-β-N-acetylglucosaminidase | SPECIFICITY | CRYSTAL-STRUCTURE | FOOD SCIENCE & TECHNOLOGY | ASPARAGINE-LINKED OLIGOSACCHARIDES | SWISS-MODEL | ENZYME | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SUBSTRATE | Endo-beta-N-acetylglucosaminidase | MOLECULAR-CLONING | GLYCOPEPTIDES | EXPRESSION | TRANSGLYCOSYLATION | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mutagenesis, Site-Directed | Tryptophan - genetics | Models, Molecular | Oligosaccharides - metabolism | Saccharomycetales - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Tryptophan - metabolism | Hydrolysis | Mannose - metabolism | Saccharomycetales - genetics | Conserved Sequence | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2009, Volume 4, Issue 3, pp. e4658 - e4658
Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently,...
REFINEMENT | ENHANCED TRANSGLYCOSYLATION | TRANSGLYCOSYLATION ACTIVITY | CHEMOENZYMATIC SYNTHESIS | MULTIDISCIPLINARY SCIENCES | PURIFICATION | GLYCOSYNTHASES | OLIGOSACCHARIDE SYNTHESIS | GLYCOPROTEINS | COMPLEX OLIGOSACCHARIDES | GLYCOPEPTIDES | Carbohydrate Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mutagenesis, Site-Directed | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Protein Conformation | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Enzymes | Carbohydrates | Residues | Automation | N-Acetylglucosaminidase | Laboratories | Thiazoline | Chemical reactions | Biochemistry | Biology | Biophysics | Hydrogen bonding | Proteins | Chemical bonds | Life sciences | Catalysis | Glycopeptides | Bonding | Arthrobacter | Glycoside hydrolase | Index Medicus
REFINEMENT | ENHANCED TRANSGLYCOSYLATION | TRANSGLYCOSYLATION ACTIVITY | CHEMOENZYMATIC SYNTHESIS | MULTIDISCIPLINARY SCIENCES | PURIFICATION | GLYCOSYNTHASES | OLIGOSACCHARIDE SYNTHESIS | GLYCOPROTEINS | COMPLEX OLIGOSACCHARIDES | GLYCOPEPTIDES | Carbohydrate Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mutagenesis, Site-Directed | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Protein Conformation | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Enzymes | Carbohydrates | Residues | Automation | N-Acetylglucosaminidase | Laboratories | Thiazoline | Chemical reactions | Biochemistry | Biology | Biophysics | Hydrogen bonding | Proteins | Chemical bonds | Life sciences | Catalysis | Glycopeptides | Bonding | Arthrobacter | Glycoside hydrolase | Index Medicus
Journal Article
Chemical Society reviews, ISSN 0306-0012, 08/2017, Volume 46, Issue 16, pp. 5128 - 5146
The endo-β-N-acetylglucosaminidases (ENGases) are an enzyme class (EC 3.2.1.96) produced by a range of organisms, ranging from bacteria, through fungi, to...
Glycoproteins - biosynthesis | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycopeptides - biosynthesis | Glycopeptides - chemistry | Models, Molecular | Carbohydrate Conformation | Glycoproteins - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry
Glycoproteins - biosynthesis | Biocatalysis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycopeptides - biosynthesis | Glycopeptides - chemistry | Models, Molecular | Carbohydrate Conformation | Glycoproteins - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry
Journal Article
FEMS Microbiology Letters, ISSN 0378-1097, 12/2011, Volume 325, Issue 2, pp. 123 - 129
Abstract It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans...
glycoprotein | Enterococcus faecalis V583 | endo‐β‐N‐acetylglucosaminidase | N‐linked glycan | Endo-β-N-acetylglucosaminidase | Glycoprotein | N-linked glycan | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - chemistry | Glycoproteins - metabolism | Molecular Sequence Data | Acetylglucosamine | Ribonucleases | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Polysaccharides - metabolism | Mannose - metabolism | Sequence Alignment | Bacterial Proteins - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Kinetics | Enterococcus faecalis - enzymology | Proteins | Enzymes | Polysaccharides | N-linked glycans | N-Acetylglucosaminidase | Nomenclature | Mannose | Glycoproteins | Glycan
glycoprotein | Enterococcus faecalis V583 | endo‐β‐N‐acetylglucosaminidase | N‐linked glycan | Endo-β-N-acetylglucosaminidase | Glycoprotein | N-linked glycan | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - chemistry | Glycoproteins - metabolism | Molecular Sequence Data | Acetylglucosamine | Ribonucleases | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Polysaccharides - metabolism | Mannose - metabolism | Sequence Alignment | Bacterial Proteins - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Kinetics | Enterococcus faecalis - enzymology | Proteins | Enzymes | Polysaccharides | N-linked glycans | N-Acetylglucosaminidase | Nomenclature | Mannose | Glycoproteins | Glycan
Journal Article
Biotechnology Progress, ISSN 8756-7938, 01/2017, Volume 33, Issue 1, pp. 104 - 112
Glycans play important biological roles in cell‐to‐cell interactions, protection against pathogens, as well as in proper protein folding and stability, and are...
N‐glycans | nutrition | glycosidases | immobilization | N-glycans | THERMAL-DENATURATION | FOOD SCIENCE & TECHNOLOGY | CROSS-LINKING | ORIENTED IMMOBILIZATION | ASPERGILLUS-ORYZAE | ENZYME IMMOBILIZATION | BETA-N-ACETYLGLUCOSAMINIDASE | HUMAN-MILK | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ALGINATE GEL BEADS | SUPPORT MATERIALS | ALPHA-AMYLASE | Bifidobacterium longum - enzymology | Enzymes, Immobilized - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycoside Hydrolases - chemistry | Polysaccharides - chemistry | Glycosylation | Glycoside Hydrolases - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Protein Folding | Mannose - chemistry | Enzymes | Polysaccharides
N‐glycans | nutrition | glycosidases | immobilization | N-glycans | THERMAL-DENATURATION | FOOD SCIENCE & TECHNOLOGY | CROSS-LINKING | ORIENTED IMMOBILIZATION | ASPERGILLUS-ORYZAE | ENZYME IMMOBILIZATION | BETA-N-ACETYLGLUCOSAMINIDASE | HUMAN-MILK | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ALGINATE GEL BEADS | SUPPORT MATERIALS | ALPHA-AMYLASE | Bifidobacterium longum - enzymology | Enzymes, Immobilized - chemistry | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycoside Hydrolases - chemistry | Polysaccharides - chemistry | Glycosylation | Glycoside Hydrolases - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Protein Folding | Mannose - chemistry | Enzymes | Polysaccharides
Journal Article
The Journal of Organic Chemistry, ISSN 0022-3263, 11/2012, Volume 77, Issue 21, pp. 9437 - 9446
The complex-type N-linked octasaccharide oxazoline having LacNAc as the nonreducing end sugar was efficiently synthesized using the benzyl-protected LacNAc,...
N-LINKED GLYCOPEPTIDES | OLIGOSACCHARIDES | SOLID-PHASE SYNTHESIS | O-ACYL ISOPEPTIDE | DISEASE | ASSISTED THIOESTERIFICATION | EFFICIENT SYNTHESIS | CHEMISTRY, ORGANIC | CHEMICAL-SYNTHESIS | GLYCAN | SPHINGOLIPID ACTIVATOR PROTEIN | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycoproteins - metabolism | Glycopeptides - chemistry | Molecular Sequence Data | Glycosylation | Saposins - chemical synthesis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Glycopeptides - metabolism | Saposins - metabolism | Saposins - chemistry | Carbohydrates - chemistry | Acetylglucosaminidase - metabolism | Acetylglucosaminidase - chemistry | Hydrophobic and Hydrophilic Interactions | Glycoproteins - chemistry | Carrier Proteins | Glycoproteins - chemical synthesis | Peptides | Analysis | Glycoproteins | Research | Chemical properties | Chemical synthesis | Structure | Protein binding
N-LINKED GLYCOPEPTIDES | OLIGOSACCHARIDES | SOLID-PHASE SYNTHESIS | O-ACYL ISOPEPTIDE | DISEASE | ASSISTED THIOESTERIFICATION | EFFICIENT SYNTHESIS | CHEMISTRY, ORGANIC | CHEMICAL-SYNTHESIS | GLYCAN | SPHINGOLIPID ACTIVATOR PROTEIN | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Glycoproteins - metabolism | Glycopeptides - chemistry | Molecular Sequence Data | Glycosylation | Saposins - chemical synthesis | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Glycopeptides - metabolism | Saposins - metabolism | Saposins - chemistry | Carbohydrates - chemistry | Acetylglucosaminidase - metabolism | Acetylglucosaminidase - chemistry | Hydrophobic and Hydrophilic Interactions | Glycoproteins - chemistry | Carrier Proteins | Glycoproteins - chemical synthesis | Peptides | Analysis | Glycoproteins | Research | Chemical properties | Chemical synthesis | Structure | Protein binding
Journal Article
Carbohydrate Research, ISSN 0008-6215, 09/2014, Volume 396, pp. 62 - 69
Heterogeneity of glycan structures in native glycoconjugates always hampers precise studies on carbohydrate-involved biological functions. To construct...
Egg yolk | Man3GlcNAc oxazoline | Chemoenzymatic transglycosylation | Sialylglycopeptide | Biocatalysis | Egg Yolk - chemistry | Desiccation | Bacterial Proteins - chemistry | Glycosylation | Chromatography, High Pressure Liquid | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Oligosaccharides - chemical synthesis | Oxazoles - chemical synthesis | Sialoglycoproteins - isolation & purification | Sialoglycoproteins - chemistry | Egg Proteins - chemistry | Egg Proteins - isolation & purification
Egg yolk | Man3GlcNAc oxazoline | Chemoenzymatic transglycosylation | Sialylglycopeptide | Biocatalysis | Egg Yolk - chemistry | Desiccation | Bacterial Proteins - chemistry | Glycosylation | Chromatography, High Pressure Liquid | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Oligosaccharides - chemical synthesis | Oxazoles - chemical synthesis | Sialoglycoproteins - isolation & purification | Sialoglycoproteins - chemistry | Egg Proteins - chemistry | Egg Proteins - isolation & purification
Journal Article
Glycobiology, ISSN 0959-6658, 12/2009, Volume 20, Issue 4, pp. 420 - 432
Endo-beta-N-acetylglucosaminidases are thought to be key enzymes in the catabolism of asparagine-linked oligosaccharides. However, little is known about the...
Transglycosylation | Asparagine-linked oligosaccharide | Basidiomycetes | Endo-β-N-acetylglucosaminidases FV | Flammulina velutipes | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GLYCANS | GLYCOPROTEINS | COMPLEX OLIGOSACCHARIDES | CARBOHYDRATE | endo-beta-N-acetylglucosaminidases FV | AUG INITIATOR CODON | ARTHROBACTER-PROTOPHORMIAE | basidiomycetes | asparagine-linked oligosaccharide | transglycosylation | SODIUM DODECYL-SULFATE | TRANSGLYCOSYLATION ACTIVITY | STREPTOMYCES-GRISEUS | Glycoproteins - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mannose - genetics | DNA, Complementary - genetics | Glycoproteins - metabolism | Flammulina - enzymology | Binding Sites - genetics | Oligosaccharides - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Substrate Specificity - genetics | Glycopeptides - metabolism | Mannose - metabolism | Escherichia coli - genetics | Asparagine - metabolism | Base Sequence | Oligosaccharides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Glycopeptides - genetics | DNA, Complementary - metabolism | Asparagine - genetics | Oligosaccharides - genetics
Transglycosylation | Asparagine-linked oligosaccharide | Basidiomycetes | Endo-β-N-acetylglucosaminidases FV | Flammulina velutipes | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GLYCANS | GLYCOPROTEINS | COMPLEX OLIGOSACCHARIDES | CARBOHYDRATE | endo-beta-N-acetylglucosaminidases FV | AUG INITIATOR CODON | ARTHROBACTER-PROTOPHORMIAE | basidiomycetes | asparagine-linked oligosaccharide | transglycosylation | SODIUM DODECYL-SULFATE | TRANSGLYCOSYLATION ACTIVITY | STREPTOMYCES-GRISEUS | Glycoproteins - genetics | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics | Amino Acid Sequence | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Mannose - genetics | DNA, Complementary - genetics | Glycoproteins - metabolism | Flammulina - enzymology | Binding Sites - genetics | Oligosaccharides - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Substrate Specificity - genetics | Glycopeptides - metabolism | Mannose - metabolism | Escherichia coli - genetics | Asparagine - metabolism | Base Sequence | Oligosaccharides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Glycopeptides - genetics | DNA, Complementary - metabolism | Asparagine - genetics | Oligosaccharides - genetics
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1788, pp. 225 - 241
Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is a unique and well developed tool for probing the protein content of...
Peptide identification for imaging mass spectrometry | Proteomics | Imaging mass spectrometry | Peptide N-glycosidase F | MALDI imaging mass spectrometry | Formalin-fixed | Paraffin-embedded tissue imaging | Tryptic peptide imaging | Paraffin Embedding - methods | Animals | Formaldehyde - chemistry | Humans | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Tissue Fixation - methods | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Trypsin - chemistry | Peptides - analysis | Polysaccharides - analysis
Peptide identification for imaging mass spectrometry | Proteomics | Imaging mass spectrometry | Peptide N-glycosidase F | MALDI imaging mass spectrometry | Formalin-fixed | Paraffin-embedded tissue imaging | Tryptic peptide imaging | Paraffin Embedding - methods | Animals | Formaldehyde - chemistry | Humans | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Tissue Fixation - methods | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Trypsin - chemistry | Peptides - analysis | Polysaccharides - analysis
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2002, Volume 99, Issue 15, pp. 9691 - 9696
Formation of oligosaccharides occurs both in the cytosol and in the lumen of the endoplasmic reticulum (ER). Luminal oligosaccharides are transported into the...
Proteins | COS cells | Enzymes | Biological Sciences | Databases | Amino acids | Oligosaccharides | Eukaryotic cells | Cytosol | Chromatography | Oviducts | D-GLUCOSAMINIDASE | SUBSTRATE-SPECIFICITY | FREE POLYMANNOSE OLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | PURIFICATION | HEPG2 CELLS | ENDOPLASMIC-RETICULUM | HEN OVIDUCT | GLYCOPROTEIN-BIOSYNTHESIS | GLYCANASE | PEPTIDE | Recombinant Proteins - metabolism | Amino Acid Sequence | Arabidopsis - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Oviducts - enzymology | Drosophila | Humans | Cercopithecus aethiops | Molecular Sequence Data | Oligosaccharides - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Organ Specificity | Arabidopsis - genetics | Sequence Homology, Amino Acid | Cytosol - enzymology | Sequence Alignment | Animals | Transfection | Peptide Mapping | Chickens | Female | COS Cells | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - isolation & purification
Proteins | COS cells | Enzymes | Biological Sciences | Databases | Amino acids | Oligosaccharides | Eukaryotic cells | Cytosol | Chromatography | Oviducts | D-GLUCOSAMINIDASE | SUBSTRATE-SPECIFICITY | FREE POLYMANNOSE OLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | PURIFICATION | HEPG2 CELLS | ENDOPLASMIC-RETICULUM | HEN OVIDUCT | GLYCOPROTEIN-BIOSYNTHESIS | GLYCANASE | PEPTIDE | Recombinant Proteins - metabolism | Amino Acid Sequence | Arabidopsis - enzymology | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism | Oviducts - enzymology | Drosophila | Humans | Cercopithecus aethiops | Molecular Sequence Data | Oligosaccharides - metabolism | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry | Organ Specificity | Arabidopsis - genetics | Sequence Homology, Amino Acid | Cytosol - enzymology | Sequence Alignment | Animals | Transfection | Peptide Mapping | Chickens | Female | COS Cells | Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - isolation & purification
Journal Article