Production and characterization of active soluble human beta1,4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta1-->4 GlcNAc linkage.
An active and soluble human beta1,4-galactosyltransferase (beta-GT) was produced in Escherichia coli using a maltose-binding protein fusion system. The purified recombinant beta-GT has a K(m) value of 0.035 mM for UDP-galactose and a V(max) of 643 x 10(3) nmol/mg/h. The enzyme catalyzes the transfer of galactose from UDP-galactose to N-linked oligosaccharides. The properties of the purified enzyme were identical to those of bovine milk beta-GT.
Shibatani
S
S
Medical Research Laboratory, Toyobo Co. Ltd., 2-1-1 Katata, Ohtsu, Shiga 520-0292, Japan.
Fujiyama
K
K
Nishiguchi
S
S
Seki
T
T
Maekawa
Y
Y