Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 18201574Publication DOI: 10.1016/j.febslet.2008.01.005Journal NLM ID: 0155157Publisher: Elsevier
Correspondence: C. Albermann <imba
imb.uni-stuttgart.de>
Institutions: Institute of Microbiology, Universitat Stuttgart, Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
GDP-N-acetyl-d-perosamine is a precursor of the LPS-O-antigen biosynthesis in Escherichia coli O157:H7. Like other GDP-6-deoxyhexoses, GDP-N-acetyl-d-perosamine is supposed to be synthesized via GDP-4-keto-6-deoxy-d-mannose, followed by a transamination- and an acetylation-reaction catalyzed by PerA and PerB. In this study, we have overproduced and purified PerA and PerB from E. coli O157:H7 in E. coli BL21. The recombinant proteins were partly characterized and the final product of the reaction catalyzed by PerB was shown to be GDP-N-acetyl-d-perosamine by chromatography, mass spectrometry, and 1H-NMR. The functional expression of PerB provides another enzymatically defined pathway for the synthesis of GDP-deoxyhexoses, which is needed to further study the corresponding glycosyltransferases in vitro
Escherichia coli O157, Escherichia coli O157:H7, GDP-N-acetyl-D-perosamine, LPS-O-antigen biosynthesis
Structure type: polymer chemical repeating unit
Location inside paper: p. 479
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_136045,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_146664,IEDB_152214,IEDB_174333,IEDB_885822,IEDB_983931,SB_192,SB_86
Methods: 13C NMR, 1H NMR, SDS-PAGE, TLC, genetic methods, biochemical methods, HPLC, LC-MS
Biosynthesis and genetic data: genetic data, biochemical data
Synthetic data: enzymatic
Related record ID(s): 23535, 23536, 23537, 23538
NCBI Taxonomy refs (TaxIDs): 83334Reference(s) to other database(s): GTC:G09328SI, GlycomeDB:
37110
Show glycosyltransferases
There is only one chemically distinct structure:
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