3.2.1.123: endoglycosylceramidase
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For detailed information about endoglycosylceramidase, go to the full flat file.
Word Map on EC 3.2.1.123
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3.2.1.123
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glycosphingolipids
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gangliosides
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cgases
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n-deacylase
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yamagata
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ganglio
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macrobdella
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decora
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gm1a
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diagnostics
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analysis
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drug development
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medicine
- 3.2.1.123
- glycosphingolipids
- gangliosides
- cgases
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n-deacylase
-
yamagata
-
ganglio
-
macrobdella
- decora
- gm1a
- diagnostics
- analysis
- drug development
- medicine
Reaction
Synonyms
ceramidase, endoglycosyl-, ceramide glycanase, EGALC, EGC, EGCase, EGCase I, EGCase II, EGCase III, EGCII, EGCrP1, EGCrP2, endo-glycoceramidase II, endogalactosylceramidase, endoglycoceramidase, endoglycoceramidase I, endoglycoceramidase II, endoglycoceramidase-related protein, glycosyl-N-acetyl-sphingosine 1,1-beta-D-glucanohydrolase, oligogalactosyl-N-acylsphingosine 1,1'-beta-galactohydrolase
ECTree
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Application on EC 3.2.1.123 - endoglycosylceramidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
diagnostics
drug development
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rational redesign of EGC toward the synthesis of novel ganglioside-derived therapeutics
medicine
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release of glycans from the ceramide moieties of glycosphingolipids by endoglycoceramidase II treatment in order to analyze structures of glycosphingolipids in normal human colorectal epithelial cells, and characteristic alterations of oligosaccharide structures in malignant transformation
analysis
M2W5L3
the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease
analysis
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the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease
-
diagnostics
M2W5L3
the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease
diagnostics
-
the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease
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