Literature DB >> 15686943

Identification of a UDP-Gal: GlcNAc-R galactosyltransferase activity in Escherichia coli VW187.

Pedro J Montoya-Peleaz1, John G Riley, Walter A Szarek, Miguel A Valvano, John S Schutzbach, Inka Brockhausen.   

Abstract

A novel acceptor substrate for galactosyltransferase was synthesized containing GlcNAcalpha-pyrophosphate, covalently bound to a hydrophobic phenoxyundecyl moiety (GlcNAc alpha-O-PO(3)-PO(3)-(CH(2))(11)-O-Phenyl). The new substrate was used to develop an assay for a galactosyltransferase activity from Escherichia coli strain VW187 that is involved in lipopolysaccharide synthesis and has not been studied by others. We showed that Gal was transferred from UDP-Gal to the novel acceptor substrate. This was a significant improvement over our previous preliminary assays of the enzyme using endogenous substrate, and showed that these synthetic substrates are useful for assaying enzymes that utilize lipid-bound substrates in O-chain synthesis in Gram-negative bacteria.

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Year:  2005        PMID: 15686943     DOI: 10.1016/j.bmcl.2004.11.077

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  8 in total

1.  Characterization of two UDP-Gal:GalNAc-diphosphate-lipid β1,3-galactosyltransferases WbwC from Escherichia coli serotypes O104 and O5.

Authors:  Shuo Wang; Diana Czuchry; Bin Liu; Anna N Vinnikova; Yin Gao; Jason Z Vlahakis; Walter A Szarek; Lei Wang; Lu Feng; Inka Brockhausen
Journal:  J Bacteriol       Date:  2014-06-23       Impact factor: 3.490

2.  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.

Authors:  Changchang Xu; Bin Liu; Bo Hu; Yanfang Han; Lu Feng; John S Allingham; Walter A Szarek; Lei Wang; Inka Brockhausen
Journal:  J Bacteriol       Date:  2010-11-05       Impact factor: 3.490

3.  Identification and Biochemical Characterization of the Novel α2,3-Sialyltransferase WbwA from Pathogenic Escherichia coli Serotype O104.

Authors:  Diana Czuchry; Paul Desormeaux; Melissa Stuart; Donald L Jarvis; Khushi L Matta; Walter A Szarek; Inka Brockhausen
Journal:  J Bacteriol       Date:  2015-09-21       Impact factor: 3.490

4.  Identification and biochemical characterization of WbwB, a novel UDP-Gal: Neu5Ac-R α1,4-galactosyltransferase from the intestinal pathogen Escherichia coli serotype O104.

Authors:  Diana Czuchry; Walter A Szarek; Inka Brockhausen
Journal:  Glycoconj J       Date:  2017-10-24       Impact factor: 2.916

5.  Acceptor substrate specificity of UDP-Gal: GlcNAc-R beta1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1.

Authors:  Inka Brockhausen; John G Riley; Meileen Joynt; Xiaojing Yang; Walter A Szarek
Journal:  Glycoconj J       Date:  2008-06-07       Impact factor: 2.916

6.  Characterization of two beta-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152.

Authors:  Inka Brockhausen; Bo Hu; Bin Liu; Kenneth Lau; Walter A Szarek; Lei Wang; Lu Feng
Journal:  J Bacteriol       Date:  2008-05-16       Impact factor: 3.490

Review 7.  Crossroads between Bacterial and Mammalian Glycosyltransferases.

Authors:  Inka Brockhausen
Journal:  Front Immunol       Date:  2014-10-20       Impact factor: 7.561

8.  Assaying Paenibacillus alvei CsaB-Catalysed Ketalpyruvyltransfer to Saccharides by Measurement of Phosphate Release.

Authors:  Fiona F Hager-Mair; Cordula Stefanović; Charlie Lim; Katharina Webhofer; Simon Krauter; Markus Blaukopf; Roland Ludwig; Paul Kosma; Christina Schäffer
Journal:  Biomolecules       Date:  2021-11-20
  8 in total

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