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. 2011 Jan 21;286(14):12361–12370. doi: 10.1074/jbc.M110.181750

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