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pubmed-article:16599308pubmed:abstractTextCells of a mutant of Listeria monocytogenes lacking functional PBP5, an enzyme with DD-carboxypeptidase activity, make thicker cells walls. In this study we show that the muropeptide profile of the mutant, obtained after HPLC analysis of a muramidase digest of cell wall murein, differs from that for the wild type strain. The main differences embrace strongly reduced disaccharide-tripeptide content, strongly increased amounts of pentapeptide-containing muropeptides and a shift in profile from less cross-linked muropeptides (monomers, dimers) towards more highly cross-linked ones.lld:pubmed
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pubmed-article:16599308pubmed:authorpubmed-author:KorsakDorotaDlld:pubmed
pubmed-article:16599308pubmed:authorpubmed-author:MarkiewiczZdz...lld:pubmed
pubmed-article:16599308pubmed:authorpubmed-author:PopowskaMagda...lld:pubmed
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pubmed-article:16599308pubmed:year2005lld:pubmed
pubmed-article:16599308pubmed:articleTitleAnalysis of the murein of a Listeria monocytogenes EGD mutant lacking functional penicillin binding protein 5 (PBP5).lld:pubmed
pubmed-article:16599308pubmed:affiliationDepartment of General Microbiology, Faculty of Biology, Warsaw University, Poland. d.korsak@uw.edu.pllld:pubmed
pubmed-article:16599308pubmed:publicationTypeJournal Articlelld:pubmed
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