| pubmed-article:19854897 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19854897 | lifeskim:mentions | umls-concept:C0027575 | lld:lifeskim |
| pubmed-article:19854897 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:19854897 | lifeskim:mentions | umls-concept:C2248757 | lld:lifeskim |
| pubmed-article:19854897 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:19854897 | lifeskim:mentions | umls-concept:C0065036 | lld:lifeskim |
| pubmed-article:19854897 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19854897 | pubmed:dateCreated | 2009-12-16 | lld:pubmed |
| pubmed-article:19854897 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19854897 | pubmed:abstractText | The lipooligosaccharide (LOS) of Neisseria meningitidis contains heptose (Hep) residues that are modified with phosphoethanolamine (PEtn) at the 3 (3-PEtn) and/or 6 (6-PEtn) position. The lpt3 (NMB2010) and lpt6 (NMA0408) genes of N. meningitidis, which are proposed to encode the required HepII 3- and 6-PEtn transferases, respectively, were cloned and overexpressed as C-terminally polyhistidine-tagged fusion proteins in Escherichia coli and found to localize to the inner membrane, based on sucrose density gradient centrifugation. Lpt3-His(6) and Lpt6-His(6) were purified from Triton X-100-solubilized membranes by nickel chelation chromatography, and dot blot analysis of enzymatic reactions with 3-PEtn- and 6-PEtn-specific monoclonal antibodies demonstrated conclusively that Lpt3 and Lpt6 are phosphatidylethanolamine-dependent LOS HepII 3- and 6-PEtn transferases, respectively, and that both enzymes are capable of transferring PEtn to both fully acylated LOS and de-O-acylated (de-O-Ac) LOS. Further enzymatic studies using capillary electrophoresis-mass spectrometry (MS) demonstrated that both Lpt3 and Lpt6 are capable of transferring PEtn to de-O-Ac LOS molecules already containing PEtn at the 6 and 3 positions of HepII, respectively, demonstrating that there is no obligate order of PEtn addition in the generation of 3,6-di-PEtn LOS moieties in vitro. | lld:pubmed |
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| pubmed-article:19854897 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19854897 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19854897 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19854897 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19854897 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19854897 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:LiJianjunJ | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:RichardsJames... | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:CoxAndrew DAD | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:StupakJacekJ | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:WenzelCory... | lld:pubmed |
| pubmed-article:19854897 | pubmed:author | pubmed-author:St... | lld:pubmed |
| pubmed-article:19854897 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19854897 | pubmed:volume | 192 | lld:pubmed |
| pubmed-article:19854897 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19854897 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19854897 | pubmed:pagination | 208-16 | lld:pubmed |
| pubmed-article:19854897 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
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| pubmed-article:19854897 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19854897 | pubmed:articleTitle | Functional characterization of Lpt3 and Lpt6, the inner-core lipooligosaccharide phosphoethanolamine transferases from Neisseria meningitidis. | lld:pubmed |
| pubmed-article:19854897 | pubmed:affiliation | Institute for Biological Sciences, 100 Sussex Drive, National Research Council, Ottawa, ON, Canada K1A 0R6. Cory.Wenzel@nrc-cnrc.gc.ca | lld:pubmed |
| pubmed-article:19854897 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19854897 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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