Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: chronic gastritis [ICD11:
DA42.Z 
, ICD11:
XT8W ];
infection due to Helicobacter pylori [ICD11:
XN3DY ]
NCBI PubMed ID: 18491328Publication DOI: 10.1002/cbic.200700775Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: warren.wakarchuk
nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council Canada, 100 Sussex Drive, Ottawa, ON K1A0R6, Canada
Helicobacter pylori is a highly persistent and common pathogen in humans. It is the causative agent of chronic gastritis and its further stages. HP0826 is the β-1,4-galactosyltransferase involved in the biosynthesis of the LPS O-chain backbone of H. pylori. Though it was first cloned nearly a decade ago, there are surprisingly limited data about the characteristics of HP0826, especially given its prominent role in H. pylori pathogenicity. We here demonstrate that HP0826 is a highly efficient and promiscuous biocatalyst. We have exploited two novel enzymatic activities for the quantitative synthesis of the thiodisaccharide Gal-β-S-1,4-GlcNAc-pNP as well as Gal-β-1,4-Man-pNP. We further show that Neisseria meningitidis β-1,4-galactosyltransferases LgtB can be used as an equally efficient catalyst in the latter reaction. Thiodisaccharides have been extensively used in structural biology but can also have therapeutic uses. The Gal-β-1,4-Man linkage is found in the Leishmania species LPG backbone disaccharide repeats and cap, which have been associated with vector binding in Leishmaniasis
specificity, glycosyltransferases, acceptor, kinetics, saccharides, biocatalysis
Structure type: monomer
Location inside paper: p.1633, scheme 1, compound 1
Trivial name: UDP-α-D-galactopyranose, UDP-galactopyranose
Compound class: nucleoside diphosphate sugar
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_141794,IEDB_145001,IEDB_151528,IEDB_190606,SB_7
Methods: 13C NMR, 1H NMR, NMR-2D, ESI-MS, genetic methods, biochemical methods, capillary electrophoresis (CE)
Biosynthesis and genetic data: biochemical data, genetic data
Synthetic data: enzymatic
Comments, role: This commerical substrate identical to that from H. pilori was used in the enzymatic synthesis.
Related record ID(s): 23095, 23194, 23196, 23334
NCBI Taxonomy refs (TaxIDs): 210
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error