Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
Publication DOI: 10.1039/b700034kJournal NLM ID: 101154995Publisher: The Royal Society of Chemistry
Correspondence: chen
chem.ucdavis.edu
Institutions: Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA
Carbohydrate modification is a common phenomenon in nature. Many carbohydrate modifications such as some epimerization, O-acetylation, O-sulfation, O-methylation, N-deacetylation, and N-sulfation, take place after the formation of oligosaccharide or polysaccharide backbones. These modifications can be categorized as carbohydrate post-glycosylational modifications (PGMs). Carbohydrate PGMs further extend the complexity of the structures and the synthesis of carbohydrates and glycoconjugates. They also increase the capacity of the biological regulation that is achieved by finely tuning the structures of carbohydrates. Developing efficient methods to obtain structurally defined naturally occurring oligosaccharides, polysaccharides, and glycoconjugates with carbohydrate PGMs is essential for understanding the biological significance of carbohydrate PGMs. Combined with high-throughput screening methods, synthetic carbohydrates with PGMs are invaluable probes in structure-activity relationship studies. We illustrate here several classes of carbohydrates with PGMs and their applications. Recent progress in chemical, enzymatic, and chemoenzymatic syntheses of these carbohydrates and their derivatives are also presented
synthesis, regulation, glycoconjugates, polysaccharides, enzymatic, modification, structure-activity relationship, methods, epimerization
Structure type: monomer
Location inside paper: p.867,scheme 1
Trivial name: sialoside
Contained glycoepitopes: IEDB_136794,IEDB_141494,IEDB_146100,IEDB_149174,SB_170,SB_171,SB_172,SB_84
Enzymes that release or process the structure: sialic acid aldolase, a CMP-sialic acid synthetase, and an a2,3- or an a2,6-sialyltransferase
Synthetic data: chemical and enzymatic
Comments, role: ManNAc and mannose derivatives can be directly converted to naturally occurring sialosides in one-pot using three enzymes
Related record ID(s): 21669, 21670, 21671, 21672, 21673, 21674, 21675, 21676, 21677, 21678
NCBI Taxonomy refs (TaxIDs): 197
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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