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Literature summary for 3.2.1.123 extracted from

  • Albrecht, S.; Vainauskas, S.; Stoeckmann, H.; McManus, C.; Taron, C.H.; Rudd, P.M.
    Comprehensive profiling of glycosphingolipid glycans using a novel broad specificity endoglycoceramidase in a high-throughput workflow (2016), Anal. Chem., 88, 4795-4802 .
    View publication on PubMed
Search for more literature for 3.2.1.123

Application

Application Comment Organism
analysis 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 Rhodococcus triatomae
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 Rhodococcus triatomae

Cloned(Commentary)

Cloned (Comment) Organism
-
 Rhodococcus triatomae

Organism

Organism UniProt Comment Textmining
Rhodococcus triatomae M2W5L3
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-
Rhodococcus triatomae BKS 15-14 M2W5L3
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodococcus triatomae

Synonyms

Synonyms Comment Organism
EGCase I
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 Rhodococcus triatomae