Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
The structure was elucidated in this paperNCBI PubMed ID: 16481326Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: Michel.Gilbert
nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Department of Medical Microbiology and Infectious Diseases, Erasmus MC, 3015 GD Rotterdam, The Netherlands, Department of Neurology, Dokkyo University School of Medicine, Tochigi 321-0293, Japan
We have identified a sialate-O-acetyltransferase in the lipo-oligosaccharide biosynthesis locus of Campylobacter jejuni. Strains possessing this locus are known to produce sialylated outer core structures that mimic host gangliosides, and have been implicated in triggering the onset of Guillain-Barre syndrome. The acetyltransferase, which was cloned and expressed as a fusion construct in Escherichia coli, is soluble and homologous with members of the NodL-LacA-CysE family of O-acetyltransferases. This enzyme catalyzes the transfer of O-acetyl groups onto oligosaccharide-bound sialic acid, with a high specificity for terminal a2,8-linked residues. The modification is directed to C9, and not C7, as is believed to occur more commonly in other organisms. Despite their wide prevalence and importance in both eukaryotes and prokaryotes, this is the first report to describe the characterization of a purified sialate-O-acetyltransferase
biosynthesis, transfer, Campylobacter jejuni, specificity, modification, sialic acid, acetyltransferase, O-acetyl
Structure type: oligomer
Location inside paper: p.11481, fig. 3B, p.11484
Aglycon: 6(5-fluorescein-carboxamido)-hexanoic acid succimidyl ester (FCHASE)
Trivial name: oligosaccharide-bound sialic acid
Contained glycoepitopes: IEDB_136044,IEDB_136794,IEDB_137472,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_35,SB_39,SB_42,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88
Methods: 1H NMR, genetic methods, biochemical methods
Enzymes that release or process the structure: sialate O-acetyltransferse (SOAT)
Biosynthesis and genetic data: genetic data
Synthetic data: chemical and enzymatic
Comments, role: high specificity SOAT for t)a(2-8) residues of 5-N-acetyl-neuraminic acid
NCBI Taxonomy refs (TaxIDs): 197Reference(s) to other database(s): GTC:G92550NU, GlycomeDB:
27901
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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