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Published TCIMAIL newest issue No.200
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Endoglycoceramidase (EGCase): Glycosphingolipid-hydrolyzing Enzyme
No.185(December 2020)
Endoglycoceramidases (EGCases) derived from the genus Rhodococcus are endo-type hydrolases reported by Ito et al.,1) and work under detergent-containing reactive conditions in vitro. For preparation of analytical oligosaccharide samples cleaved from glycolipids extracted from cells, recombinant EGCase (rEGCase II) (3) is the enzyme that has generally been used.2) Moreover, rEGCase I (1) is capabile of releasing ceramides from organic glucosylceramide.3) To strip oligosaccharides from the surface of living cells without detergent reagents, the mixture reagents, rEGCase II assisted by Activator II (4) and rEGCase I assisted by Activator II (2) are helpful because Activator II replaces the surfactant as the enzyme-activating protein.4,5)
These enzymes were commercialized under license from National Institute of Advanced Industrial Science and Technology (AIST). Host actinomycete was used for enzyme production under license from Kyushu University.
References
- 1) A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids.
- 2) Purification and characterization of glycosphingolipid-specific endoglycosidases (endoglycoceramidases) from a mutant strain of Rhodococcus sp. Evidence for three molecular species of endoglycoceramidase with different specificities.
- 3) Preparation and characterization of EGCase I, applicable to the comprehensive analysis of GSLs, using a rhodococcal expression system
- 4) Specific hydrolysis of intact erythrocyte cell‐surface glycosphingolipids by endoglycoceramidase
- 5) Kinetics of endoglycoceramidase action toward cell-surface glycosphingolipids of erythrocytes
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