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 |