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  • Title: Mechanism of human alpha-1,3-fucosyltransferase V: glycosidic cleavage occurs prior to nucleophilic attack.
    Author: Murray BW, Wittmann V, Burkart MD, Hung SC, Wong CH.
    Journal: Biochemistry; 1997 Jan 28; 36(4):823-31. PubMed ID: 9020780.
    Abstract:
    alpha-1,3-Fucosyltransferase V (FucT V) catalyzes the transfer of 1-fucose from the donor sugar guanosine 5'-diphospho-beta-1-fucose (GDP-Fuc) to an acceptor sugar. A secondary isotope effect on the fucosyltransfer reaction with guanosine 5'-diphospho-[1-2H]-beta-1-fucose (GDP-[1-2H]-Fuc) as the substrate was observed and determined to be Dv = 1.32 +/- 0.13 and DV/K = 1.27 +/- 0.07. Competitive inhibition of FucT V by guanosine 5'-diphospho-2-deoxy-2-fluoro-beta-1-fucose (GDP-2F-Fuc) was observed with an inhibition constant of 4.2 microM which represents the most potent inhibitor of this enzyme to date. Incubation of GDP-2F-Fuc with FucT V and an acceptor molecule prior to the addition of GDP-Fuc had no effect on the potency of inhibition, indicating that GDP-2F-Fuc is neither an inactivator nor a slow substrate. Both the observed secondary isotope effect and the inhibition by GDP-2F-Fuc are consistent with a charged, sp2-hybridized, transition-state structure. A convenient and efficient synthesis of GDP-[1-2H]-Fuc and GDP-2F-Fuc and a nonradioactive, fluorescence assay for fucosyltransferase activity have been developed.
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