| pubmed-article:17697255 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17697255 | lifeskim:mentions | umls-concept:C1197533 | lld:lifeskim |
| pubmed-article:17697255 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
| pubmed-article:17697255 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:17697255 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17697255 | lifeskim:mentions | umls-concept:C0059246 | lld:lifeskim |
| pubmed-article:17697255 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:17697255 | pubmed:dateCreated | 2007-8-16 | lld:pubmed |
| pubmed-article:17697255 | pubmed:abstractText | Pseudomonas aeruginosa bacteriophage endolysins KZ144 (phage phiKZ) and EL188 (phage EL) are highly lytic peptidoglycan hydrolases (210 000 and 390 000 units mg(-1)), active on a broad range of outer membrane-permeabilized Gram-negative species. Site-directed mutagenesis indicates E115 (KZ144) and E155 (EL188) as their respective essential catalytic residues. Remarkably, both endolysins have a modular structure consisting of an N-terminal substrate-binding domain and a predicted C-terminal catalytic module, a property previously only demonstrated in endolysins originating from phages infecting Gram-positives and only in an inverse arrangement. Both binding domains contain conserved repeat sequences, consistent with those of some peptidoglycan hydrolases of Gram-positive bacteria. Fusions of these domains with green fluorescent protein immediately label all outer membrane-permeabilized Gram-negative bacteria tested, isolated P. aeruginosa peptidoglycan and N-acetylated Bacillus subtilis peptidoglycan, demonstrating the broad range of peptidoglycan-binding capacity by these domains. Specifically, A1 chemotype peptidoglycan and fully N-acetylated glucosamine units are essential for binding. Both KZ144 and EL188 appear to be a natural chimeric enzyme, originating from a recombination of a cell wall-binding domain encoded by a Bacillus or Clostridium species and a catalytic domain of an unknown ancestor. | lld:pubmed |
| pubmed-article:17697255 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17697255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17697255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17697255 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17697255 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:17697255 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:VolckaertGuid... | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:HertveldtKirs... | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:MichielsChris... | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:LavigneRobR | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:BriersYvesY | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:LagaertStijnS | lld:pubmed |
| pubmed-article:17697255 | pubmed:author | pubmed-author:CornelissenAn... | lld:pubmed |
| pubmed-article:17697255 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17697255 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:17697255 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17697255 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17697255 | pubmed:pagination | 1334-44 | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:meshHeading | pubmed-meshheading:17697255... | lld:pubmed |
| pubmed-article:17697255 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17697255 | pubmed:articleTitle | Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL. | lld:pubmed |
| pubmed-article:17697255 | pubmed:affiliation | Division of Gene Technology, Department of Biosystems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, B-3001 Leuven, Belgium. yves.briers@biw.kuleuven.be | lld:pubmed |
| pubmed-article:17697255 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17697255 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1258427 | entrezgene:pubmed | pubmed-article:17697255 | lld:entrezgene |
| family:PF01471.13 | family:pubmed | pubmed-article:17697255 | lld:pfam |
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