Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: gastroenteritis [ICD11:
1A40.0 
];
acute inflammatory demyelinating polyneuropathy [ICD11:
8C01.0 ];
infection due to Campylobacter jejuni [ICD11:
XN4Q5 ]
The structure was elucidated in this paperNCBI PubMed ID: 17087520Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: imper
mit.edu
Institutions: Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
In Campylobacter jejuni 2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose, termed N,N'-diacetylbacillosamine (Bac2,4diNAc), is the first carbohydrate in the glycoprotein N-linked heptasaccharide. With uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) as a starting point, two enzymes of the general protein glycosylation (Pgl) pathway in C. jejuni (PglF and PglE) have recently been shown to modify this sugar nucleotide to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-α-D-glycopyranose (UDP-4-amino-sugar) [Schoenhofen, I. C., et al. (2006) J. Biol. Chem. 281, 723-732]. PglD has been proposed to catalyze the final step in N,N'-diacetylbacillosamine synthesis by N-acetylation of the UDP-4-amino-sugar at the C4 position. We have cloned, overexpressed, and purified PglD from the pgl locus of C. jejuni NCTC 11168 and identified it as the acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine, utilizing acetyl-coenzyme A as the acetyl group donor. The UDP-N,N'-diacetylbacillosamine product was purified from the reaction by reverse phase C18 HPLC and the structure determined by NMR analysis. Additionally, the full-length PglF was overexpressed and purified in the presence of detergent as a GST fusion protein, allowing for derivation of kinetic parameters. We found that the UDP-4-amino-sugar was readily synthesized from UDP-GlcNAc in a coupled reaction using PglF and PglE. We also demonstrate the in vitro biosynthesis of the complete heptasaccharide lipid-linked donor by coupling the action of eight enzymes (PglF, PglE, PglD, PglC, PglA, PglJ, PglH, and PglI) in the Pgl pathway in a single reaction vessel.
biosynthesis, Campylobacter jejuni, glycosylation, acetyltransferase
Structure type: oligomer
Location inside paper: p.13665, fig. 6
Aglycon: ->1)undecaprenol
Trivial name: isoprenepyrophosphate-linked disaccharide
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_885822
Methods: 1H NMR, 31P NMR, ESI-MS, MALDI-MS, genetic methods, biochemical methods, HPLC, capillary electrophoresis (CE)
Enzymes that release or process the structure: PglC, PglA (transferase)
Biosynthesis and genetic data: genetic data,biochemical data
Synthetic data: enzymatic
Related record ID(s): 23625, 23933, 23934, 23935, 23936
NCBI Taxonomy refs (TaxIDs): 197Reference(s) to other database(s): GlycomeDB:
37326
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error