A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase.
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 beta-1,4-galactosyltransferase with a Ki value of 149 microM. This study supports that the glycosyltransferase reaction mechanism proceeds through a glycosidic cleavage transition state with sp2 character developed at the anomeric center.
Hayashi
T
T
Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.
Murray
B W
BW
Wang
R
R
Wong
C H
CH
D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D009237:N-Acetyllactosamine Synthase / Q000037:antagonists & inhibitors*; D014531:Uridine Diphosphate Galactose / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism
D004791:Enzyme Inhibitors; C081992:UDP-2-fluoro-2-deoxygalactose; D014531:Uridine Diphosphate Galactose; D009237:N-Acetyllactosamine Synthase