A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids.
A novel glycosphingolipid-degrading enzyme was found in the cultured supernatant of Rhodococcus sp. G-74-2. It was purified 34.7-fold from the supernatant with 32.2% recovery by ammonium sulfate precipitation followed by Sephadex G-100 chromatography. The enzyme was demonstrated capable of cleaving the linkage between the oligosaccharide and ceramide of various acidic and neutral glycosphingolipids, producing intact oligosaccharides and ceramides. However, it was noted to hardly make any attack on linkages between monosaccharides and ceramides (cerebrosides) or between oligosaccharides and diacylglycerol (glycoglycerolipids). The enzyme preparation was completely free from various exoglycosidases and proteases. Furthermore, it was found to degrade neither N-linked nor O-linked glycoproteins. This enzyme, which is tentatively called endoglycoceramidase, should greatly facilitate the study of glycosphingolipids.
D002240:Carbohydrate Sequence; D002518:Ceramides / Q000378:metabolism*; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D005677:G(M1) Ganglioside / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006028:Glycosphingolipids / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D012240:Rhodococcus / Q000201:enzymology
D002518:Ceramides; D006028:Glycosphingolipids; D009844:Oligosaccharides; D005677:G(M1) Ganglioside; C018835:asialo GM1 ganglioside; D006026:Glycoside Hydrolases; C050427:endoglycoceramidase