| Sumario: | Galactofuranose metabolism is a good target for the development of novel chemotherapeutic agents for the treatment of some microbial infections. This is a valid objective because galactofuranose is absent in mammals. Two enzymes are involved in the biosynthesis of molecules containing galactofuranose: a mutase, which catalyzes the interconversion of UDP-Galp and UDP-Galf, and D-galactofuranosyltransferases. The mechanism of action of the mutase and its inhibition is currently being investigated, whereas studies on the galactofuranosyltransferases have been hampered by the lack of a labeled galactofuranose nucleotide. In the present work we describe the chemical synthesis of UDP-α-D-[6-3H]Galf and we prove its effectiveness for incorporation of radioactive galactofuranose into a natural acceptor. This is the first report on the chemical synthesis of a labeled donor of galactofuranose with the potential for studying the galactofuranosyltransferases independently from the UDP-Galp mutase. © Wiley-VCH Verlag GmbH & Co. KGaA, 2005.
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