Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 19124251Journal NLM ID: 9413298Publisher: Elsevier
Correspondence: N. Desroy <nicolas.desroy
mutabilis.fr>
Institutions: MUTABILIS SA, 102 Avenue Gaston Roussel, 93230 Romainville, France
Gram-negative bacteria lacking heptoses in their lipopolysaccharide (LPS) display attenuated virulence and increased sensitivity to human serum and to some antibiotics. Thus inhibition of bacterial heptose synthesis represents an attractive target for the development of new antibacterial agents. HldE is a bifunctional enzyme involved in the synthesis of bacterial heptoses. Development of a biochemical assay suitable for high-throughput screening allowed the discovery of inhibitors 1 and 2 of HldE kinase. Study of the structure-activity relationship of this series of inhibitors led to highly potent compounds.
Lipopolysaccharide, Escherichia coli, antibacterial, antivirulence drugs, membrane permeability, HldE, RfaE
Structure type: monomer
Location inside paper: p.1277, scheme 1
Trivial name: ADP-β-L-glycero-D-manno-heptose, ADP-L-glycero-β-D-manno-heptose
Contained glycoepitopes: IEDB_137353,IEDB_140947
Methods: 1H NMR, ESI-MS, biochemical methods
Enzymes that release or process the structure: HldD(RfaD) - epimerase
Biosynthesis and genetic data: genetic data, biochemical data
Synthetic data: chemical
Related record ID(s): 899, 21501, 23425, 23512
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GlycomeDB:
25190
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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