Catabolism of glycoprotein glycans. Characterization of a lysosomal endo-N-acetyl-beta-d-glucosaminidase specific for glycans with a terminal chitobiose residue

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Abstract
An endo-N-acetyl-β-d-glucosaminidase active towards oligosaccharides with a reducing terminal [bis(N-acetylglucosamine)] residue has been characterized in rat liver. The primary structure of its reaction products was determined using high-resolution 1H-NMR spectroscopy. The enzyme is predominantly located in the lysosomal fraction, presents a maximum of activity at pH 3.5 and is completely inactive towards conjugated glycans, i.e. glycoproteins and glycopeptides as well as on glycoasparagines. These results support the existence of a new pathway for the degradation of glycoprotein glycans inside the lysosome. In particular, this enzymic activity may be the origin of oligosaccharides bearing a single terminal reducing N-acetylglucosamine residue which are excreted in the urine of patients with various exoglycosidase deficiencies.