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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2005-5-3
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pubmed:abstractText |
The lipid A domain anchors lipopolysaccharide (LPS) to the outer membrane and is typically a disaccharide of glucosamine that is both acylated and phosphorylated. The core and O-antigen carbohydrate domains are linked to the lipid A moiety through the eight-carbon sugar 3-deoxy-D-manno-octulosonic acid known as Kdo. Helicobacter pylori LPS has been characterized as having a single Kdo residue attached to lipid A, predicting in vivo a monofunctional Kdo transferase (WaaA). However, using an in vitro assay system we demonstrate that H. pylori WaaA is a bifunctional enzyme transferring two Kdo sugars to the tetra-acylated lipid A precursor lipid IV(A). In the present work we report the discovery of a Kdo hydrolase in membranes of H. pylori capable of removing the outer Kdo sugar from Kdo2-lipid A. Enzymatic removal of the Kdo group was dependent upon prior removal of the 1-phosphate group from the lipid A domain, and mass spectrometric analysis of the reaction product confirmed the enzymatic removal of a single Kdo residue by the Kdo-trimming enzyme. This is the first characterization of a Kdo hydrolase involved in the modification of gram-negative bacterial LPS.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15866922-10198035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15866922-10201887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15866922-10632700,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15866922-9851930
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3374-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15866922-Helicobacter pylori,
pubmed-meshheading:15866922-Hydrolases,
pubmed-meshheading:15866922-Lipid A,
pubmed-meshheading:15866922-Lipopolysaccharides,
pubmed-meshheading:15866922-Phosphates,
pubmed-meshheading:15866922-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15866922-Sugar Acids,
pubmed-meshheading:15866922-Temperature,
pubmed-meshheading:15866922-Transferases
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pubmed:year |
2005
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pubmed:articleTitle |
A novel 3-deoxy-D-manno-octulosonic acid (Kdo) hydrolase that removes the outer Kdo sugar of Helicobacter pylori lipopolysaccharide.
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pubmed:affiliation |
Department of Microbiology, J. H. Quillen College of Medicine, Johnson City, Tennessee 37614, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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