Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:19133500rdf:typepubmed:Citationlld:pubmed
pubmed-article:19133500lifeskim:mentionsumls-concept:C0205474lld:lifeskim
pubmed-article:19133500lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:19133500lifeskim:mentionsumls-concept:C0450442lld:lifeskim
pubmed-article:19133500lifeskim:mentionsumls-concept:C0870071lld:lifeskim
pubmed-article:19133500lifeskim:mentionsumls-concept:C0936012lld:lifeskim
pubmed-article:19133500pubmed:issue4lld:pubmed
pubmed-article:19133500pubmed:dateCreated2009-1-12lld:pubmed
pubmed-article:19133500pubmed:abstractTextBacteria in a biofilm are enmeshed in a self-synthesized extracellular polysaccharide matrix (PGA), which is a linear polymer of beta(1,6)-linked N-acetylglucosamine (GlcNAc) residues. Dispersin B (DspB), a soluble glycoside hydrolase produced by the periodontal pathogen Actinobacillus actinomycetemcomitans degrades PGA. The enzyme DspB is an alpha/beta TIM-barrel protein and belongs to family 20 glycosyl hydrolases members. The enzyme activity of DspB with regard to its substrate specificity towards beta(1,6)-linked GlcNAc polymers and its endo/exo character was investigated through ligand docking and the hydrolysis of synthetic oligosaccharides. Ligand docking analysis suggested that beta(1,6)-linked GlcNAc oligosaccharide bound to the active site better that beta(1,4)-linked GlcNAc oligosaccharide. Our combined results indicate that DspB is an exo-acting enzyme that hydrolyzes beta(1,6)-linked N-acetylglucosamine oligomers.lld:pubmed
pubmed-article:19133500pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:languageenglld:pubmed
pubmed-article:19133500pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:citationSubsetIMlld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19133500pubmed:statusMEDLINElld:pubmed
pubmed-article:19133500pubmed:monthDeclld:pubmed
pubmed-article:19133500pubmed:issn0236-5383lld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:LiptákAAlld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:KaplanJ BJBlld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:RamasubbuNNlld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:KerriganJ EJElld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:RagunathCClld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:JánossyLLlld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:GyémántGyöngy...lld:pubmed
pubmed-article:19133500pubmed:authorpubmed-author:KandraLiliLlld:pubmed
pubmed-article:19133500pubmed:issnTypePrintlld:pubmed
pubmed-article:19133500pubmed:volume59lld:pubmed
pubmed-article:19133500pubmed:ownerNLMlld:pubmed
pubmed-article:19133500pubmed:authorsCompleteYlld:pubmed
pubmed-article:19133500pubmed:pagination439-51lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:meshHeadingpubmed-meshheading:19133500...lld:pubmed
pubmed-article:19133500pubmed:year2008lld:pubmed
pubmed-article:19133500pubmed:articleTitleModeling and biochemical analysis of the activity of antibiofilm agent Dispersin B.lld:pubmed
pubmed-article:19133500pubmed:affiliationAcademic Systems and Technologies, University of Medicine and Dentistry of New Jersey, Newark, NJ 07103, USA.lld:pubmed
pubmed-article:19133500pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19133500pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:19133500pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:19133500lld:pubmed