A Cytoplasmic Peptide: N-Glycanase and ER-Associated Degradation

  • Tadashi Suzuki


Peptide: N-glycanase (PNGase) hydrolyzes the amide bond between proximal GlcNAc and the linkage Asn residue of N-linked glycopeptides/glycoproteins, releasing free oligosaccharides bearing N,N′-diacetylchitobiose structure at their reducing termini (after spontaneous release of ammonia). This enzyme has been widely used as a tool reagent for analyzing the structure and functions of N-linked glycan chains on glycoproteins. The occurrence of cytoplasmic PNGase activity has been reported in a wide variety of eukaryotes (Suzuki et al. 2002 and references therein). The cytoplasmic PNGase was found to be quite distinct in terms of enzymatic properties from the “reagent” PNGases of plant and bacterial origin. A gene encoding the cytoplasmic enzyme, PNG1, was first identified in Saccharomyces cerevisiae (Suzuki et al. 2000). This gene has highly conserved its orthologues and can be found throughout eukaryotes (Suzuki et al. 2002).


Paper Electrophoresis ERAD Substrate Bovine Pancreatic Ribonuclease Free Oligosaccharide Glass Bead Method 
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© Springer 2008

Authors and Affiliations

  • Tadashi Suzuki
    • 1
  1. 1.Glycometabolome Laboratory, Systems Glycobiology Research Group, Frontier Research SystemRIKEN InstituteWako, SaitamaJapan

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