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Fluorescent mannosides serve as acceptor substrates for glycosyltransferase and sugar-1-phosphate transferase activities in Euglena gracilis membranes

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  • Irina M. Ivanova
  • Sergey A. Nepogodiev
  • Gerhard Saalbach
  • Ellis C. O'Neill
  • Michael D. Urbaniak
  • Michael A.J. Ferguson
  • Sudagar S. Gurcha
  • Gurdyal S. Besra
  • Robert A. Field
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<mark>Journal publication date</mark>13/01/2017
<mark>Journal</mark>Carbohydrate Research
Volume438
Number of pages13
Pages (from-to)26-38
<mark>State</mark>Published
Early online date30/11/16
<mark>Original language</mark>English

Abstract

Synthetic hexynyl α-D-mannopyranoside and its α-1,6-linked disaccharide counterpart were fluorescently labelled through CuAAC click chemistry with 3-azido-7-hydroxycoumarin. The resulting triazolyl-coumarin adducts, which were amenable to analysis by TLC, HPLC and mass spectrometry, proved to be acceptor substrates for α-1,6-ManT activities in mycobacterial membranes, as well as α- and β-GalT activities in trypanosomal membranes, benchmarking the potential of the fluorescent acceptor approach against earlier radiochemical assays. Following on to explore the glycobiology of the benign protozoan alga Euglena gracilis, α-1,3- and α-1,2-ManT activities were detected in membrane preparations, along with GlcT, Glc-P-T and GlcNAc-P-T activities. These studies serve to demonstrate the potential of readily accessible fluorescent glycans as substrates for exploring carbohydrate active enzymes.