Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: diarrhea [ICD11:
ME05.1 
, ICD11:
SA55 ];
hemorrhagic colitis (HC) [ICD11:
1A40.0 ];
infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 23765664Publication DOI: 10.1007/978-1-62703-465-4_16Publisher: Totowa, NJ: Humana Press
Editors: Holst O, Walker JM, Beck A
Correspondence: I. Brockhausen <brockhau
queensu.ca>
Institutions: Department of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Canada
The outer membrane of gram-negative bacteria is stabilized by lipopolysaccharides (LPS). The O-antigenic polysaccharides of LPS are composed of repeating units that are exposed to and can interact with the environment. The glycosyltransferases that assemble these repeating units are encoded by the O-antigen gene cluster and utilize undecaprenol-phosphate-linked intermediates as natural acceptor substrates, and nucleotide sugars as donor substrates on the cytoplasmic face of the inner membrane. Many of the glycosyltransferase genes are known but the enzymatic functions of most of them remain to be identified. We describe here how the function of a recombinant glucosyltransferase WbdN from Escherichia coli O157 can be determined by NMR analysis of the enzyme product, using a synthetic acceptor substrate analog. A fluorescent acceptor substrate analog can be used in highly sensitive enzyme assays that allow the characterization of enzyme activity without the use of radioactive nucleotide sugar donor substrates.
NMR, glucosyltransferase, linkage analysis, WbdN, fluorescent acceptor substrate
Structure type: polymer chemical repeating unit
Location inside paper: p.200
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_136045,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_146664,IEDB_152214,IEDB_174333,IEDB_885822,IEDB_983931,SB_192,SB_86
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, sugar analysis, 31P NMR, MALDI-MS, Western blotting, NMR-1D, biochemical methods, HPLC
Biological activity: The characterization of WbdN activity with the use of synthetic fluorescent acceptor substrate.
Synthetic data: chemical and chemoenzymatic
Related record ID(s): 29487, 29488
NCBI Taxonomy refs (TaxIDs): 83334Reference(s) to other database(s): GTC:G60704LX, GlycomeDB:
3513
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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