TABLE 2.
Substrate specificity of the sialyltransferase CstII from RM1503 measured using FCHASE-reducing end glycan derivatives (at 0.5 mm) and determined using CE
CstII from RM1503 promotes LNB sialylation with greater than 5-fold more efficiency than terminal Gal-β1,3-GalNAcβ (GM1a) and Gal-β1,4-Glcβ (Lac) acceptors, which are natural substrates for the enzyme in strains expressing ganglioside mimics.
| Acceptor (−FCHASE) | Specific activity | |
|---|---|---|
| milliunits/mg | ||
| LNB- | Galβ-1,3-GlcNAc- | 111.9 |
| GM1a- | Galβ-1,3-GalNAcβ-1,4-[NeuAcα-2,3-]-Galβ-1,4-Glc- | 17.5 |
| Lac- | Galβ-1,4-Glc- | 16.8 |
| LacNAc | Galβ-1,4-GlcNAc- | 6.6 |
| 3′Sialyl-Lac- | NeuAcα-2,3-Galβ-1,4-Glc- | 0.1 |