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. Author manuscript; available in PMC: 2014 Apr 28.
Published in final edited form as: Biochim Biophys Acta. 2013 Apr 8;1830(8):4274–4281. doi: 10.1016/j.bbagen.2013.04.001

Table 1.

Kinetic parameters of glycosyltransferases for acceptor and donor substrates. Assays were carried out as described in the Material and methods section, using the indicated acceptor substrates to determine the KM and Vmax values (Origin Pro 8.0). Bn, benzyl; pnp, p-nitrophenyl.

Enzyme Substrate KM (mM) Vmax (μmol/h/mg)
C1GalT GalNAcα-Bn 0.8 0.14
UDP-Gal (using GalNAcα-Bn) 1.0 0.16
C3GnT GalNAcα-Bn 3.0 0.95
UDP-GlcNAc (using GalNAcα-Bn) 2.8 1.30
GalNAcα-perillyl 0.3 0.40
Ac-A-(GalNAcα)TG-NH2 0.7 1.10
C2GnT1 Galβ1–3GalNAcα-pnp 1.1 0.08
UDP-GlcNAc (using Galβ1–3GalNAcα-pnp) 3.2 0.10
C2GnT2 Galβ1–3GalNAcα-pnp 2.1 1.50
UDP-GlcNAc (using Galβ1–3GalNAcα-pnp) 2.2 1.70
GlcNAcβ1–3GalNAcα-pnp 5.8 1.00
UDP-GlcNAc (using GlcNAcβ1–3GalNAcα-pnp) 2.1 0.80