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  • Title: Recognition of beta-D-Gal p-(1-->3)-beta-D-Glc pNAc-OR acceptor analogues by the Lewis alpha-(1-->3/4)-fucosyltransferase from human milk.
    Author: Du M, Hindsgaul O.
    Journal: Carbohydr Res; 1996 Jun 05; 286():87-105. PubMed ID: 8925514.
    Abstract:
    The Lewis alpha-(1-->3/4)-fucosyltransferase (E.C. 2.4.1.65) transfers L-fucose from GDP-fucose to OH-4 of the Glc pNAc residue in the disaccharide beta-D-Galp-(1-->3)-beta-D-Glc pNAc-OR [R = (CH2)8COOMe] (1) to give the Lewis-A blood group determinant beta-D-Gal p-(1-->3)-[alpha-L-Fuc p-(1-->4)]-beta-D-Glc pNAc-OR. Five deoxy analogous of 1, as well as its N-propionyl derivative, were chemically synthesized and kinetically evaluated as both substrates and inhibitors for the enzyme from human milk. The unmodified acceptor 1 had Km = 640 microM with Vmax set arbitrarily to 100. The 6-deoxy (Km = 400 microM, V(max) = 90) and N-propionyl compounds (Km = 330 microM, V(max) = 170) remained excellent substrates while the 4-deoxy compound was a very weak competitive inhibitor with Ki = 9 mM. Deoxygenation of OH-2' and OH-4'(of the Gal residue) in 1 had little effect on the activity. The OH-6 group of the Gal residue proved to be critical for recognition by the enzyme since substitution of this group with hydrogen led to an inactive compound.
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