@article { ISI:000084528000030,
	title = {Glycosyl fluorides can function as substrates for nucleotide phosphosugar-dependent glycosyltransferases},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {274},
	number = {53},
	year = {1999},
	month = {DEC 31},
	pages = {37717-37722},
	abstract = {alpha-Galactosyl fluoride is shown to function as a substrate, in place of uridine-5{\textquoteright}-diphosphogalactose, for the alpha-galactosyltransferase from Neisseria meningitidis. The reaction only occurs in the presence of catalytic quantities of uridine 5{\textquoteright}-diphosphate, In the presence of galactosyl accepters, the expected oligosaccharide product is formed in essentially quantitative yields, reaction having been performed on multi-milligram scales, In the absence of a suitable acceptor, the enzyme synthesizes uridine-5{\textquoteright}-diphosphogalactose, as demonstrated through a coupled assay in which uridine-5{\textquoteright}-diphosphogalactose is converted to uridine-5{\textquoteright}-diphosphoglucuronic acid with conversion of NAD to NADH. These glycosyl fluoride substrates therefore offer the potential of an inexpensive alternative donor substrate in the synthesis of oligosaccharides as well a means of generating steady state concentrations of nucleotide diphosphate sugars for in situ use by other enzymes. Further, they should prove valuable as mechanistic probes.},
	issn = {0021-9258},
	doi = {10.1074/jbc.274.53.37717},
	author = {Lougheed, B and Ly, HD and WAKARCHUK, WW and Withers, SG}
}
