Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 7961456Publication DOI: 10.1128/jb.176.22.6944-6951.1994Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: raetz
biochem.duke.edu
Institutions: Department of Biochemistry, Merck Research Laboratories, Rahway, USA
Unlike Escherichia coli, living cells of Pseudomonas aeruginosa can complete the fatty acylation of lipid A when the biosynthesis of 3-deoxy-D-manno-octulosonate (Kdo) is inhibited (R. C. Goldman, C. C. Doran, S. K. Kadam, and J. O. Capobianco, J. Biol. Chem. 263:5217-5233, 1988). In this study, we demonstrate the presence of a novel enzyme in extracts of P. aeruginosa that can transfer lauroyl-acyl carrier protein (ACP) to a tetraacyl disaccharide-1,4'-bis-phosphate precursor of lipid A (termed lipid IVA) that accumulates in Kdo-deficient mutants of E. coli. Comparable E. coli extracts cannot transfer laurate from lauroyl-ACP to lipid IVA, only to (Kdo)2-lipid IVA (K. A. Brozek, and C. R. H. Raetz, J. Biol. Chem. 265:15410-15417, 1990). P. aeruginosa extracts do not utilize myristoyl- or R-3-hydroxymyristoyl-ACP instead of lauroyl-ACP to acylate lipid IVA. Laurate incorporation in P. aeruginosa extracts is dependent upon time, protein concentration, and the presence of Triton X-100 but is inhibited by lauroyl-coenzyme A. P. aeruginosa extracts transfer only one laurate to lipid IVA, whereas E. coli extracts can transfer two laurates to (Kdo)2-lipid IVA. These results demonstrate that incorporation of laurate into lipid A does not require prior attachment of Kdo in all gram-negative bacteria
Pseudomonas aeruginosa, Escherichia coli, endotoxin, glycolipid
Structure type: oligomer
Location inside paper: Fig. 2, bottom structure
Trivial name: Kdo2-Lipid A
Compound class: glycolipid
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772
Methods: FAB-MS, TLC, radiolabeling, radioactivity measurement, extraction, cell growth, centrifugation, HR-FAB-MS, protein determination
Enzymes that release or process the structure: Kdo transferase (kdtA), lauroyl-acyltransferase (lauroyl-ACP), myristoyl-acyltransferase (myristoyl-ACP)
Related record ID(s): 47776, 47777, 47779
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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