一种独特的糖鞘脂裂解酶（来自水蛭的神经酰胺聚糖酶）可裂解寡糖与神经酰胺之间的连接。
A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide.
作者信息
Li S C, DeGasperi R, Muldrey J E, Li Y T
出版信息
Biochem Biophys Res Commun. 1986 Nov 26;141(1):346-52. doi: 10.1016/s0006-291x(86)80375-8.
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, Hirudo medicinalis. 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.
在药用水蛭中发现了一种新型酶，它能水解各种糖鞘脂中神经酰胺与糖链之间的连接。这种酶从乳糖神经酰胺、GbOse3神经酰胺、GbOse4神经酰胺、GbOse5神经酰胺、nLcOse4神经酰胺、GM3、GM2、GM1、GD1a和GT1中释放出完整的寡糖，同时释放出神经酰胺。以氚标记的GM1为底物，我们发现该酶的最适pH值在4到5之间。由于该酶能切割各种糖鞘脂中神经酰胺与糖链之间的连接，且对糖链没有明显偏好，我们建议将这种酶称为神经酰胺聚糖酶。
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