Luigi Panza, Pietro L. Chiappini, Giovanni Russo, Daniela Monti and Sergio Riva
The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.