Abstract
Free oligosaccharides (FOS) in the cytosol of eukaryotic cells are mainly generated during endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins. We characterized the enzymes involved in generation and degradation of FOS in the nematode Caenorhabditis elegans. 1) Peptide: N-glycanase (PNGase) from Caenorhabditis elegans, which releases FOS from misfolded glycoproteins in the cytosol, was shown to be a unique bifunctional enzyme having both deglycosylation and protein disulfide reductase activities. 2) Endo-β-N-acetylglucosaminidase was proven to release a single GlcNAc residue at the reducing end of FOS in vivo. 3) Luminal class 1 α-mannosidases, probably Golgi α-mannosidase I, was involved in generation of M5A´ isoform of Man5GlcNAc1 that is specific to C. elegans.
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