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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseAsparagineAmidohydrolasesCarbohydrate SequenceSulfotransferasesMolecular Sequence DataPeptidesGlucosamineAmino Acid SequenceAspartate-Ammonia LigaseFlavobacteriumGlycosylationOligosaccharidesCarbohydrate ConformationGlycopeptidesDisaccharidesPeptide FragmentsN-Acetylmuramoyl-L-alanine AmidaseGlycosylphosphatidylinositolsHeparitin SulfateChromatography, High Pressure LiquidPolysaccharidesModels, MolecularMutagenesis, Site-DirectedBinding SitesProtein ConformationStructure-Activity RelationshipProtein Structure, SecondaryBase SequenceAspartic AcidKineticsAmino AcidsSequence Homology, Amino AcidHeparinSubstrate SpecificityEscherichia coliMutationRecombinant ProteinsProtein Structure, TertiaryProtein BindingCloning, MolecularAsparaginaseAcetyl Coenzyme APenicillin AmidaseAmino Acid SubstitutionCircular DichroismCrystallography, X-RayProtein Processing, Post-TranslationalOligopeptidesHydrogen-Ion ConcentrationCell LineMass SpectrometryMagnetic Resonance SpectroscopyCatalysisGlutamineTrypsinAmidesAntimicrobial Cationic PeptidesHexosyltransferasesMolecular WeightBacterial ProteinsElectrophoresis, Polyacrylamide GelHydrogen BondingProtein FoldingSequence AlignmentPeptides, CyclicCattleHydrolysisCarbohydratesMembrane ProteinsCatalytic DomainPeptide LibraryGlycoproteinsAspartate-tRNA LigaseDNA, ComplementaryPolyisoprenyl Phosphate SugarsPolyisoprenyl Phosphate OligosaccharidesDNA PrimersCysteinePeptide MappingAmide SynthasesRNA, Transfer, AsnInterleukin-1betaRecombinant Fusion ProteinsTransfectionAmino Acid MotifsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseProtein PrecursorsNuclear Magnetic Resonance, BiomolecularEpitopesLigasesHistidineTransferasesMollusk VenomsTunicamycinAmphibian ProteinsRhodococcusCell Membranebeta 2-MicroglobulinThermodynamics

EnzymaticProteinsMannoseOccurCommonAlphaOligosaccharideGlycoproteinsEnzymeGlycopeptidesActivity

Enzymatic1

• Any of the enzymatically catalyzed modifications of the individual AMINO ACIDS of PROTEINS, and enzymatic cleavage or crosslinking of peptide chains that occur pre-translationally (on the amino acid component of AMINO ACYL TRNA), co-translationally (during the process of GENETIC TRANSLATION), or after translation is completed (POST-TRANSLATIONAL PROTEIN PROCESSING). (lookformedical.com)

Proteins2

• In most instances, proteins of interest are denatured and treated with PNGase F. Following this, they are either subjected to gel electrophoresis, in which protein migration changes due to the deglycosylation by PNGase F, or are analyzed via mass spectrometry, by which the oligosaccharide can be characterized and the protein or peptide fragment from which it came can be characterized. (wikipedia.org)
• The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. (lookformedical.com)

Mannose3

• PNGase F works by cleaving between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides from N-linked glycoproteins and glycopeptides. (wikipedia.org)
• It cleaves all asparagine-linked complex, hybrid, or high mannose oligosaccharides unless the core GlcNAc contains an alpha 1,3- fucose. (wikipedia.org)
• Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE . (lookformedical.com)

Occur1

• PNGase F requires a minimum of two GlcNAc oligosaccharide residues attached to the asparagine in order for catalysis to occur. (wikipedia.org)

Common1

• This enzyme utilizes a catalytic triad of cysteine-histidine-aspartate in its active site, which is a common motif for amidases. (wikipedia.org)

Alpha1

• Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. (lookformedical.com)

Oligosaccharide3

• PNGase F requires a minimum of two GlcNAc oligosaccharide residues attached to the asparagine in order for catalysis to occur. (wikipedia.org)
• In most instances, proteins of interest are denatured and treated with PNGase F. Following this, they are either subjected to gel electrophoresis, in which protein migration changes due to the deglycosylation by PNGase F, or are analyzed via mass spectrometry, by which the oligosaccharide can be characterized and the protein or peptide fragment from which it came can be characterized. (wikipedia.org)
• An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. (nih.gov)

Glycoproteins2

• PNGase F works by cleaving between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides from N-linked glycoproteins and glycopeptides. (wikipedia.org)
• Aspartylglucosaminidase (EC 3.5.1.26), the lysosomal enzyme which hydrolyzes the N-acetylglucosamine-asparagine linkages in glycoproteins, was purified from human liver to homogeneity. (nih.gov)

Enzyme2

• This enzyme utilizes a catalytic triad of cysteine-histidine-aspartate in its active site, which is a common motif for amidases. (wikipedia.org)
• Amino acid composition revealed only 2 methionine residues/enzyme molecule. (nih.gov)

Glycopeptides1

• It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. (musc.edu)

Activity2

• It requires the presence of more than two amino-acid residues in the substrate for activity. (nih.gov)
• Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae. (musc.edu)