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

@article{Suzuki2004NGlycosylationdeglycosylationAA,
  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},
  year={2004},
  volume={12},
  pages={183-193}
}
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.
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TLDR
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It is demonstrated that N-glycosylation is critical for the function of bPepT2.
Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases
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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.
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References

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TLDR
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
TLDR
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.
TLDR
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.
TLDR
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.
TLDR
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.
TLDR
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?
TLDR
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.
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