These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: UDP-N-trifluoroacetylglucosamine as an alternative substrate in N-acetylglucosaminyltransferase reactions.
    Author: Sala RF, MacKinnon SL, Palcic MM, Tanner ME.
    Journal: Carbohydr Res; 1998 Jan; 306(1-2):127-36. PubMed ID: 9691444.
    Abstract:
    The synthesis of UDP-N-trifluoroacetylglucosamine [uridine 5'-(2-trifluoroacetamido-2-deoxy-alpha-D-glucopyranosyl diphosphate, UDP-GlcNAc-F3] is reported. The compound is found to serve as a substrate for the core-2 GlcNAc transferase (EC 2.4.1.102) that is involved in the biosynthesis of O-linked glycoproteins and for the GlcNAcT-V transferase (EC 2.4.1.155) that is a key biosynthetic enzyme controlling the branching pattern of cell surface complex Asn-linked oligosaccharides. The trisaccharide beta-D-Galp-(1-->3) -[beta-D-GlcpNAc-F3(1-->6)] alpha-D-GalpNAc-OR [R = (CH2)8CO2Me] was prepared from beta-D-Galp-(1-->3) -alpha-D- GalpNAc-OR using the core-2 GlcNAc transferase. The tetrasaccharide beta-D-GlcpNAc-(1 -->2)-[beta-D-GlcpNAc-F3-(1-->6)]-alpha-D-Manp-(1-->6)-beta-D-Glcp -OR [R = (CH2)7CH3] using the GlcNAcT-V transferase. Removal of the trifluoroacetyl group was achieved under mild basic conditions to give the corresponding glucosamine containing tetrasaccharide. These examples demonstrate the feasibility of introducing masked forms of glucosamine residues into oligosaccharides using GlcNAc-specific transferases. The requirement for the trifluoroacetamido group as a specific recognition element was evident in the observation that neither UDP-glucosamine nor UDP-glucose served as a donor substrates for the core-2 GlcNAc transferase.
    [Abstract] [Full Text] [Related] [New Search]