EC Number |
Title |
Organism |
---|
3.2.1.123 | Comprehensive profiling of glycosphingolipid glycans using a novel broad specificity endoglycoceramidase in a high-throughput workflow |
Rhodococcus triatomae |
3.2.1.123 | Comprehensive profiling of glycosphingolipid glycans using a novel broad specificity endoglycoceramidase in a high-throughput workflow |
Rhodococcus triatomae BKS 15-14 |
3.2.1.123 | Hydrophobic interactions contribute to conformational stabilization of endoglycoceramidase II by mechanism-based probes |
Rhodococcus sp. |
3.2.1.123 | Mass spectrometry-based identification of carbohydrate anomeric configuration to determine the mechanism of glycoside hydrolases |
Rhodococcus sp. M-777 |
3.2.1.123 | Structural insights into the broad substrate specificity of a novel endoglycoceramidase I belonging to a new subfamily of GH5 glycosidases |
Rhodococcus equi |
3.2.1.123 | Structural insights into the broad substrate specificity of a novel endoglycoceramidase I belonging to a new subfamily of GH5 glycosidases |
Rhodococcus sp. M-777 |
3.2.1.123 | Structural insights into the broad substrate specificity of a novel endoglycoceramidase I belonging to a new subfamily of GH5 glycosidases |
Rhodococcus equi 103S |
3.2.1.123 | A novel endoglycoceramidase hydrolyzes oligogalactosylceramides to produce galactooligosaccharides and ceramides |
Rhodococcus equi |
3.2.1.123 | A novel fucosyl glycosphingolipid of brine shrimp that is highly sensitive to endoglycoceramidase |
Rhodococcus sp. |
3.2.1.123 | A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids [published erratum appears in J Biol Chem 1987 Feb 5;262(4):1926] |
Rhodococcus sp. |