Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 19617350Publication DOI: 10.1074/jbc.M109.022772Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: strent
mail.utexas.edu
Institutions: From the Department of Molecular Biochemistry and Biochemistry, Medical College of Georgia, Augusta, Georgia 30912, USA, Section of Molecular Genetics and Microbiology and Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, Texas 78712
The lipopolysaccharide (LPS) of V. cholerae has been reported to contain a single 3-deoxy-D-manno-octulosonic acid (Kdo) residue that is phosphorylated. The phosphorylated Kdo-sugar further links the hexa-acylated V. cholerae lipid A domain to the core oliogosaccharide and O-antigen. In this report, we confirm that V. cholerae possess the enzymatic machinery to synthesize a phosphorylated Kdo residue. Further, we have determined that the presence of the phosphate group on the Kdo residue is necessary for secondary acylation in V. cholerae. The requirement for a secondary subsitutent on the Kdo residue (either an additional Kdo-sugar or a phosphate group) was also found to be critical for secondary acylation catalyzed by LpxL proteins from B. pertussis, E. coli, and H. influenzae. Although three putative late acyltransferase orthologs have been identified in the V. cholerae genome (Vc0212, Vc0213, and Vc1577), only Vc0213 appears to be functional. Vc0213 functions as a myristoyl transferase acylating lipid A at the 2'-position of the glucosamine disaccharide. Generally acyl-ACPs serve as the fatty acyl donor for the acyltransferases required for LPS biosynthesis; however, in vitro assays indicate that Vc0213 preferentially utilizes myristoyl-CoA as an acyl donor. This is the first report to biochemically characterize enzymes involved in the biosynthesis of the V. cholerae Kdo-lipid A domain
Lipopolysaccharide, lipid A, 3-deoxy-D-manno-octulosonic acid, Vibrio cholerae, acyltransferase
Structure type: oligomer ; 1404.9
Location inside paper: p.25810, fig.6A, lipid IVA
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531
Methods: DNA techniques, TLC, MALDI-TOF MS, genetic methods, biochemical methods, enzyme assay
Biosynthesis and genetic data: genetic data
Related record ID(s): 23708, 31242, 31243, 31244, 31245, 31246, 31247, 31248
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
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