A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase

Article abstract of DOI:10.1016/S0968-0896(96)00263-5

Uridine 5'-diphospho-(2-deoxy-2-fluoro)galactose (UDP-2FGal), prepared and characterized for the first time by a chemoenzymatic method, was found to be a competitive inhibitor of β-1,4-galactosyltransferase with a K(i) value of 149 μM. This study supports that the glycosyltransferase reaction mechanism proceeds through a glycosidic cleavage transition state with sp² character developed at the anomeric center.