Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Organ / tissue: cell wallAssociated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 2285138Journal NLM ID: 0370535Publisher: Academic Press
Institutions: Max-Planck-Institut für Entwicklungsbiologie, Abt. Biochemie, Tübingen, Federal Republic of Germany
The length distribution of the glycan strands in the murein (peptidoglycan) sacculus of Escherichia coli has been analyzed after solubilization of the murein by complete digestion with human serum amidase. The glycan strands released were separated according to length by reversed-phase HPLC on wide-pore Nucleosil 300 C18 material at 50 degrees C, employing a convex gradient from 5 to 11% acetonitrile. The length of the fractionated glycan strands, which carry a nonreducing 1,6-anhydromuramic acid as a natural end group, was calculated from the ratio of total to nonreducing terminal muramic acid residues. This was possible after complete hydrolysis of the isolated glycan strands by muramidase followed by separation of the released nonreducing and reducing di- and tetrasaccharides by reversed-phase HPLC on Hypersil C18. The method established allows the separation of the glycan strands of murein, a poly-GlcNAc(β 1-4)MurNAc-polysaccharide, up to a degree of polymerization of approximately 60. The predominant lengths of the glycan strands were 5 to 10 GlcNAc(β 1-4)MurNAc disaccharide units.
Structure type: polymer chemical repeating unit
Location inside paper: Fig. 1a
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
Methods: HPLC, DEAE, ensymatoic digestion
Enzymes that release or process the structure: muramidaze
Comments, role: Parent molecule: murein;
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): CCSD:
41539
Show glycosyltransferases
There is only one chemically distinct structure:
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