[14] CERAMIDE GLYCANASE (cas 106769-66-8) from the leech Macrobdella decora and oligosaccharide-transferring activity

Add time:08/05/2019    Source:sciencedirect.com

Publisher SummaryCERAMIDE GLYCANASE (cas 106769-66-8) (CGase) is an endoglycosidase that releases the intact glycan chain from various glycosphingolipids by cleaving the linkage between the ceramide and the glycan chain. This enzyme is found in the leech Macrobdella and in other annelids such as the European leech, Hirudo medicinalis, and the earthworm, Lumbricus terrestris. Many exoglycosidases can catalyze transglycosylation of a monosaccharide in addition to hydrolysis. In contrast, the transfer of an intact complex oligosaccharide by endoglycosidases is less common. The CGase isolated from the leech can transfer the intact oligosaccharide from various glycosphingolipids (GSLs) to suitable acceptors. This oligosaccharide transferring reaction can be used to synthesize neoglycoconjugates for studying the biological functions expressed by glycan chains in GSLs. The hydrolysis of glycosphingolipids (GSLs) by CGase in the absence of a detergent is very slow. The reaction is stimulated by bile salts. Among various bile salts tested, sodium cholate is most effective, except for the hydrolysis of LacCer.

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