ArticleGlycoconjugate journal2006
UDP-Gal: GlcNAc-R beta1,4-galactosyltransferase--a target enzyme for drug design. Acceptor specificity and inhibition of the enzyme.
Article in Glycoconjugate journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Hans Paulsen: Contributions to the Investigations of Glycoprotein Biosynthesis.Molecules (Basel, Switzerland) · 2025Review
- Characterization of Human Recombinant β1,4-GalNAc-Transferase B4GALNT1 and Inhibition by Selected Compounds.Molecules (Basel, Switzerland) · 2025Article
- Article
- Discovery of Novel Inhibitors Targeting Multi-UDP-hexose Pyrophosphorylases as Anticancer Agents.Molecules (Basel, Switzerland) · 2020Article
- Thioglycosides Are Efficient Metabolic Decoys of Glycosylation that Reduce Selectin Dependent Leukocyte Adhesion.Cell chemical biology · 2018Article
- Identification and characterization of the 4-epimerase AglW from the archaeon Methanococcus maripaludis.Glycoconjugate journal · 2018Article
- A mechanism for bistability in glycosylation.PLoS computational biology · 2018Article
- An acceptor analogue of β-1,4-galactosyltransferase: Substrate, inhibitor, or both?Carbohydrate research · 2017Article
- Donor substrate promiscuity of bacterial β1-3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1-4-galactosyltransferases.Bioorganic & medicinal chemistry · 2016Article
- Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer.Frontiers in oncology · 2015Review
- Characterization of two UDP-Gal:GalNAc-diphosphate-lipid β1,3-galactosyltransferases WbwC from Escherichia coli serotypes O104 and O5.Journal of bacteriology · 2014Article
- Investigations on β1,4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate.Glycoconjugate journal · 2013Article
- Acceptor specificities and selective inhibition of recombinant human Gal- and GlcNAc-transferases that synthesize core structures 1, 2, 3 and 4 of O-glycans.Biochimica et biophysica acta · 2013Article
- Glycosylation potential of human prostate cancer cell lines.Glycoconjugate journal · 2012Article
- Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis.Journal of bacteriology · 2011Article
- Specificity of β1,4-galactosyltransferase inhibition by 2-naphthyl 2-butanamido-2-deoxy-1-thio-β-D-glucopyranoside.Glycoconjugate journal · 2010Article
- Deoxygenated disaccharide analogs as specific inhibitors of beta1-4-galactosyltransferase 1 and selectin-mediated tumor metastasis.The Journal of biological chemistry · 2009Article
- Acceptor substrate specificity of UDP-Gal: GlcNAc-R beta1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1.Glycoconjugate journal · 2008Article
- Characterization of two beta-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galactosyltransferases are important enzymes for the extension of the glycan chains of glycoproteins and glycolipids, and play critical roles in cell surface functions and in the immune system. In this work, the acceptor specificity and several inhibitors of bovine beta1,4-Gal-transferase T1 (beta4GalT, EC 2.4.1.90) were studied. Series of analogs of N-acetylglucosamine (GlcNAc) and GlcNAc-carrying glycopeptides were synthesized as acceptor substrates. Modifications were made at the 3-, 4- and 6-positions of the sugar ring of the acceptor, in the nature of the glycosidic linkage, in the aglycone moiety and in the 2-acetamido group. The acceptor specificity studies showed that the 4-hydroxyl group of the sugar ring was essential for beta4GalT activity, but that the 3-hydroxyl could be replaced by an electronegative group. Compounds having the anomeric beta-configuration were more active than those having the alpha-configuration, and O-, S- and C-glycosyl compounds were all active as substrates. The aglycone was a major determinant for the rate of Gal-transfer. Derivatives containing a 2-naphthyl aglycone were inactive as substrates although quinolinyl groups supported activity. Several compounds having a bicyclic structure as the aglycone were found to bind to the enzyme and inhibited the transfer of Gal to control substrates. The best small hydrophobic GlcNAc-analog inhibitor was found to be 1-thio-N-butyrylGlcNbeta-(2-naphthyl) with a K(i) of 0.01 mM. These studies help to delineate beta4GalT-substrate interactions and will aid in the development of biologically applicable inhibitors of the enzyme.
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