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- Title
Transglycosylation and Reverse Hydrolysis Reactions of Endoglycoceramidase from the Jellyfish, Cyanea nozakii1.
- Authors
Horibata, Yasuhiro; Higashi, Hideyosbi; Ito, Makoto
- Abstract
Endoglycoceramidase (EGCase: EC 3.2.1.123) is an enzyme capable of cleaving the glyco-sidic linkage between oligosaccharides and ceramides in various glycosphingolipids. We report here transglycosylation and reverse hydrolysis reactions of EGCase from the jellyfish Cynaea nozakii. Various alkyl-GMl oligosaccharides (alkyl-II3NeuAcGgOse4) were synthesized when GM1 ganglioside was treated with the EGCase in the presence of 1-alkanols. Among various 1-alkanols tested, methanol was found to be the most preferential acceptor, followed by 1-hexanol and 1-pentanol. GM1 was the best donor, followed by GDlb and GTlb, when methanol was used as an acceptor. However, neither globoside nor glucosylceramide was utilized by the enzyme as a donor substrate. The enzyme transferred oligosaccharides from various glycosphingolipids to NBD-ceramide, a fluorescent ceramide, producing NBD-labeled glycosphingolipids. In addition to the transglycosylation reaction, the enzyme catalyzed the reverse hydrolysis reaction; lactose was condensed to ceramide to generate lactosylceramide in the presence of the enzyme. These results indicate that the jellyfish enzyme will facilitate the synthesis of various neoglycoconjugates and glycosphingolipids.
- Subjects
JELLYFISHES; ENDOGLYCOCERAMIDASE; OLIGOSACCHARIDES; GLYCOSPHINGOLIPIDS; GANGLIOSIDES
- Publication
Journal of Biochemistry, 2001, Vol 130, Issue 2, p263
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a002981