A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide
SC Li, R Degasperi, JE Muldrey, YT Li - Biochemical and biophysical …, 1986 - Elsevier
SC Li, R Degasperi, JE Muldrey, YT Li
Biochemical and biophysical research communications, 1986•ElsevierA novel type of enzyme which hydrolyzes the linkage between the ceramide and the sugar
chain in various glycosphingolipids has been found in the leech, Hirudomedicinalis. This
enzyme releases the intact oligosaccharide from LacCer, GbOse 3 Cer, GbOse 4 Cer,
GbOse 5 Cer, nLcOse 4 Cer, GM3, GM2, GM1, GD1a and GT1 with the concurrent release of
ceramides. By using tritium-labeled GM1 as substrate we found the optimum pH of this
enzyme to be between pH 4 and 5. Since the enzyme cleaves the linkage between the …
chain in various glycosphingolipids has been found in the leech, Hirudomedicinalis. This
enzyme releases the intact oligosaccharide from LacCer, GbOse 3 Cer, GbOse 4 Cer,
GbOse 5 Cer, nLcOse 4 Cer, GM3, GM2, GM1, GD1a and GT1 with the concurrent release of
ceramides. By using tritium-labeled GM1 as substrate we found the optimum pH of this
enzyme to be between pH 4 and 5. Since the enzyme cleaves the linkage between the …
Summary
A novel type of enzyme which hydrolyzes the linkage between the ceramide and the sugar chain in various glycosphingolipids has been found in the leech, Hirudomedicinalis. This enzyme releases the intact oligosaccharide from LacCer, GbOse3Cer, GbOse4Cer, GbOse5Cer, nLcOse4Cer, GM3, GM2, GM1, GD1a and GT1 with the concurrent release of ceramides. By using tritium-labeled GM1 as substrate we found the optimum pH of this enzyme to be between pH 4 and 5. Since the enzyme cleaves the linkage between the ceramide and the sugar chain in various glycosphingolipids with no apparent preference toward the sugar chain, we propose to call this enzyme ceramide-glycanase.
Elsevier
