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  • Title: Inhibition of UDP-GlcNAc:Gal beta 1-3GalNAc-R (GlcNAc to GalNAc) beta 6-N-acetylglucosaminyltransferase from acute myeloid leukaemia cells by photoreactive nitrophenyl substrate derivatives.
    Author: Toki D, Granovsky MA, Reck F, Kuhns W, Baker MA, Matta KL, Brockhausen I.
    Journal: Biochem Biophys Res Commun; 1994 Jan 28; 198(2):417-23. PubMed ID: 7802860.
    Abstract:
    Cells from patients with acute myeloid leukaemia (AML) contain an abnormally high UDP-GlcNAc: Gal beta 1-3GalNAc-R (GlcNAc to GalNAc) beta 6-N-acetylglucosaminyltransferase (core 2 beta 6-Gn-T) activity. Upon UV irradiation at 350 nm, the substrate Gal beta 1-3GalNAc alpha-p-nitrophenyl acted as an effective inhibitor for this enzyme but not for several other transferases. Preincubation with Gal beta 1-3GalNAc alpha-benzyl but not GalNAc alpha-benzyl protected core 2 beta 6-Gn-T from inhibition indicating that the inhibitor is specific for the substrate binding site of core 2 beta 6-Gn-T. A number of other nitrophenyl-sugar derivatives similarly acted as inhibitors for core 2 beta 6-Gn-T. GalNAc alpha-pnp at higher concentrations also inactivated UDP-Gal: GalNAc-R beta 3-galactosyltransferase from rat liver and AML cells and inhibition could be reduced by substrate protection. These results suggest that pnp-sugar derivatives may prove useful as specific inhibitors of glycosyltransferases and as affinity labels.
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