Fluorescent uridine diphospho-sugar analogues as molecular probes

摘要

Glycosyltransferases are a family of enzymes that are responsible for the transfer of a sugar moiety from a donor to an acceptor. For example the bovine galactosyltransferase, β1,4GalT, catalyses the transfer of galactose from uridine diphosphogalactose (UDP-Gal) to N-acetyl glucosamine to form the galactose-glucosamine construct, N-acetyl lactosamine. Glycosyl transferases are found in both mammals and bacteria where they have multiple roles including the decoration of cell membranes and cell walls with polysaccharides that can lead to important effects in inflammation, cell migration and the immune response. Endogenous sugar nucleotides and their structural analogues are sought after as probes for this family of enzymes, as inhibitor candidates and as tools for assay development, and, as such, they represent key targets for chemical synthesis.