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 ]
The structure was elucidated in this paperNCBI 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: oligomer
Location inside paper: p.1633, scheme 1, compound 5, Gal-b-1,4-Man-b-pNP
Trivial name: 4-nitrophenyl (b-d-galactopyranosyl)-(1-4)-b-d-mannopyranoside
Contained glycoepitopes: IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_7,SB_72,SB_88
Methods: 13C NMR, 1H NMR, NMR-2D, ESI-MS, genetic methods, biochemical methods, capillary electrophoresis (CE)
Enzymes that release or process the structure: HP0826 (b-1,4-galactosyltransferase), LgtB (b-1,4-galactosyltransferase)
Biosynthesis and genetic data: biochemical data, genetic data
Synthetic data: enzymatic
Comments, role: There is no clear statement that HP0826 and LgtB enzymes work the same way in Helicobacter pylori. Commercial substrates were used.
Related record ID(s): 22710, 23194
NCBI Taxonomy refs (TaxIDs): 210Reference(s) to other database(s): GlycomeDB:
37031
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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