| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/2000/01/rdf-schema#comment | "The lpxH gene encodes the UDP-2,3-diacylglucosamine-specific pyrophosphatase that catalyzes the fourth step of lipid A biosynthesis in Escherichia coli. To confirm the function of lpxH, we constructed KB21/pKJB5. This strain contains a kanamycin insertion element in the chromosomal copy of lpxH, complemented by plasmid pKJB5, which is temperature-sensitive for replication and harbors lpxH(+). KB21/pKJB5 grows at 30 degrees C but loses viability at 44 degrees C, demonstrating that lpxH is essential. CDP-diglyceride hydrolase (Cdh) catalyzes the same reaction as LpxH in vitro but is non-essential and cannot compensate for the absence of LpxH. The presence of Cdh in cell extracts interferes with the LpxH assay. We therefore constructed KB25/pKJB5, which contains both an in-frame deletion of cdh and a kanamycin insertion mutation in lpxH, covered by pKJB5. When KB25/pKJB5 cells are grown at 44 degrees C, viability is lost, and all in vitro LpxH activity is eliminated. A lipid migrating with synthetic UDP-2,3-diacylglucosamine accumulates in KB25/pKJB5 following loss of the covering plasmid at 44 degrees C. This material was converted to the expected products, 2,3-diacylglucosamine 1-phosphate and UMP, by LpxH. Pseudomonas aeruginosa contains two proteins with sequence similarity to E. coli LpxH. The more homologous protein catalyzes UDP-2,3-diacylglucosamine hydrolysis in vitro. The corresponding gene complements KB25/pKJB5 at 44 degrees C, but the less homologous gene does not. The accumulation of UDP-2,3-diacylglucosamine in our lpxH mutant is consistent with the observation that the lipid A disaccharide synthase LpxB, the next enzyme in the pathway, cannot condense two UDP-2,3-diacylglucosamine molecules, but instead utilizes UDP-2,3-diacylglucosamine as its donor and 2,3-diacylglucosamine 1-phosphate as its acceptor."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m204068200"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m204068200"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m204068200"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Raetz C.R.H."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Raetz C.R.H."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Babinski K.J."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Babinski K.J."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Kanjilal S.J."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/author | "Kanjilal S.J."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/pages | "25947-25956"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/pages | "25947-25956"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/title | "Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/title | "Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene."xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12000771 |
| http://purl.uniprot.org/citations/12000771 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12000771 |