Table 5.

Glycosyltransferases used in this study. All of the enzymes used are human, inverting transferases having a predicted GT-A fold [52]. The GT family assignment is from the CAZy data bank. The DxD motif may contain one or more catalytically active acidic amino acids. Although N-glycosylation sites are present, their occupation by N-glycans and their function in enzyme stability has only been shown for C2GnT1 [42]. Multiple Cys residues function in forming protein dimers (C1GalT) [14] and/or disulfide bonds (C1GnT1) [45]. -T, -transferase.

Enzyme names	Accession #	EC#	GT family	Fold	DxD motif	N-Glycan sites	Cys
C1GalT, core 1 β1,3-Gal-T, Core 1 synthase, T-synthase, Core 1-T	NP_064541	2.4.1.122	GT31	GT-A	DAD	0	7
C3GnT, core 3 β1,3-GlcNAc-T, Core 3 synthase, β3GnT6	Q6ZMB0	2.4.1.147	GT31	GT-A	DDD	3	3
C2GnT1, core 2 β1,6-GlcNAc-T, Core 2-T	Q02742	2.4.1.102	GT14	GT-A	DE, DVDVD	2	2
C2GnT2, core 2/4 β1,6-GlcNAc-T, Core 4-T	AAD10824	2.4.1.148	GT14	GT-A	DE, DSD, DID	2	2