N-Glycosylation/deglycosylation as a mechanism for the post-translational modification/remodification of proteins

  title={N-Glycosylation/deglycosylation as a mechanism for the post-translational modification/remodification of proteins},
  author={Tadashi Suzuki and Ken Kitajima and Sadako Inoue and Yasuo Inoue},
  journal={Glycoconjugate Journal},
Abbreviations: PNGase, peptide-N4-(N-acetyl-b-d-gtucosaminyl) asparagine amidase or peptide:N-glycanase; endob-GlcNAc'ase, endo-b-N=acetyl-d-glucosaminidase; GPP, glycophosphoproteins; L-929 PNGase, PNGase isolated from C3H mouse-derived fibroblast cells, L-929; UNGs, unconjugated N-glycans; Xyl, xylose; Gal, galactose;. Ara, arabinose; Con A, concanavalin A; RER, rough endoplasmic reticulum; Man5GlcNAc2-pyrophosphoryl dolichol; pentamannosyl N,N' -diacetylchitobiosyl pyrophosphoryl dolichot. 
The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.
A review of the research history of cytoplasmic PNGase concludes that discovery of a human genetic disorder involving the NGLY1 gene clearly indicates that this enzyme plays a critical role in human biology.
Cytoplasmic peptide:N‐glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions
The primary structure and potential functions of the cytoplasmic PNGases are reviewed and a mouse homologue of Png1p bound not only to the Rad23 protein, but also to various proteins related to ubiquitin and/or the proteasome through an extended amino‐terminal domain.
Free N-linked oligosaccharide chains: Formation and degradation
Current knowledge about the formation, processing and degradation of free OSs in eukaryotes is summarized and the potential biological significance of this pathway is discussed.
An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling.
It is revealed that a bacterial endoglycosidase from Streptococcus pyogenes, EndoS, is complementary to other known endoglyCosidases (EndoA, EndoH) used for current protein remodeling and allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans.
Short communication: The essential role of N-glycosylation in the transport activity of bovine peptide transporter 2.
It is demonstrated that N-glycosylation is critical for the function of bPepT2.
Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases
A survey of different linkages and sugars demonstrated not only that unnatural linkages can be tolerated but they can provide insight into the scope of Endo-A transglycosylation activity.


Peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase) activity could explain the occurrence of extracellular xylomannosides in a plant cell suspension
The presence of peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase) activity in cell extracts as well in the culture medium that could explain the production of those compounds is demonstrated.
Catabolism of N-glycosylprotein glycans: evidence for a degradation pathway of sialyglyco-asparagines resulting from the combined action of the lysosomal aspartylglucosaminidase and endo-N-acetyl-β-d-glucosaminidase
A mixture of sialylglycoasparagines and sialyglycopeptides was successively incubated with lysosomal extracts and this process represents a new catabolic pathway for N-glycosyl-proteins which may account for the appearance of the oligosaccharides stored in tissues and urine of patients suffering from lysOSomal diseases.
Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation.
It is proposed here that PNGase-catalyzed N-deglycosylation is a functionally important universal feature in living cells.
Purification and Characterization of Endo-β-N-Acetylgluco-saminidase of Aspergillus oryzae
: An endo-beta-N-acetylglucosaminidase which hydrolyzes the N,N'-diacetylchitobiosyl linkage in asparagine-linked oligosaccharides was purified from the enzyme product of Aspergillus oryzae. Its
Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F.
Deglycosylation studies with PNGase F revealed that many proteins in their native conformation were susceptible to this enzyme but that prior denaturation in sodium dodecyl sulfate greatly decreased the amount of enzyme required for complete carbohydrate removal.
Further studies on endo-beta-N-acetylglucosaminidase D1.
The purification procedure for endo-beta-N-acetylglucosaminidase D was improved to yield an enzyme preparation which was homogeneous upon gel electrophoresis, indicating that the peptide portion of substrates does not have much effect on susceptibility to the enzyme.
Demonstration and cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver.
An endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo- N- acetyl-lactosaminic-type glycoasparagine substrate was demonstrated in rat liver and was predominantly present in the soluble (cytosolic) fraction.
Does an animal peptide:N-glycanase have the dual role as an enzyme and a carbohydrate-binding protein?
The de-N-glycosylating enzyme activity of L-929 PNGase was inhibited by yeast mannan and triomannose, Manα1 → 3(Man α1 → 6)Man, but not by mannose and α-methyl-d-mannoside.