A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide.
A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide.
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DOI：
10.1016/s0006-291x(86)80375-8
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发表时间：
1986-11
影响因子：
3.1
通讯作者：
S. Li;R. Degasperi;J. E. Muldrey;Y. Li
中科院分区：
文献类型：
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作者：
S. Li;R. Degasperi;J. E. Muldrey;Y. Li
在水蛭水蛭中发现了一种水解神经酰胺和各种鞘糖脂中糖链之间键的新型酶。该酶从LacCer、GbOse3Cer、GbOse4Cer、GbOse5Cer、nLcOse4Cer、GM3、GM2、GM1、GD1a和GT 1释放完整的寡糖，同时释放神经酰胺。通过使用氚标记的GM 1作为底物，我们发现该酶的最适pH在pH 4和5之间。由于该酶切割神经酰胺和各种鞘糖脂中的糖链之间的连接，对糖链没有明显的偏好，我们建议将这种酶称为神经酰胺聚糖酶。
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.