A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide

Su Chen Li; Rita Degasperi; James E. Muldrey; Yu Teh Li

doi:10.1016/S0006-291X(86)80375-8

A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide

Su Chen Li
, Rita Degasperi
, James E. Muldrey
, Yu Teh Li

Research output: Contribution to journal › Article › peer-review

79 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	346-352
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	141
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(86)80375-8
State	Published - 26 Nov 1986
Externally published	Yes

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@article{f72fd17719be47058c38b3f4a202b637,

title = "A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide",

abstract = "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.",

author = "Li, \{Su Chen\} and Rita Degasperi and Muldrey, \{James E.\} and Li, \{Yu Teh\}",

note = "Funding Information: Acknowledgements - This investigation was supported by Grants PCM 82-19489 from the National Science Foundation and NS 09626 from the National Institutes of Health.",

year = "1986",

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doi = "10.1016/S0006-291X(86)80375-8",

language = "English",

volume = "141",

pages = "346--352",

journal = "Biochemical and Biophysical Research Communications",

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AU - Li, Su Chen

AU - Degasperi, Rita

AU - Muldrey, James E.

AU - Li, Yu Teh

N1 - Funding Information: Acknowledgements - This investigation was supported by Grants PCM 82-19489 from the National Science Foundation and NS 09626 from the National Institutes of Health.

PY - 1986/11/26

Y1 - 1986/11/26

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0023057673

U2 - 10.1016/S0006-291X(86)80375-8

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide

Abstract

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