Linked Life Data

8706749

Source:http://linkedlifedata.com/resource/pubmed/id/8706749

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8706749rdf:typepubmed:Citationlld:pubmed
pubmed-article:8706749lifeskim:mentionsumls-concept:C0014834lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C0021467lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C1514468lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C1323252lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C0021469lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:8706749lifeskim:mentionsumls-concept:C0064534lld:lifeskim
pubmed-article:8706749pubmed:issue2lld:pubmed
pubmed-article:8706749pubmed:dateCreated1996-9-10lld:pubmed
pubmed-article:8706749pubmed:abstractTextThis paper reports the biochemical characterization of the flavoprotein L-aspartate oxidase from Escherichia coli. Modification of a previously published procedure allowed overexpression of the holoenzyme in an unproteolysed form. L-Aspartate oxidase is a monomer of 60 kDa containing 1 mol of noncovalently bound FAD/mol protein. A polarographic and two spectrophotometric coupled assays have been set up to monitor the enzymatic activity continuously. L-Aspartate oxidase was subjected to product inhibition since iminoaspartate, which results from the oxidation of L-aspartate, binds to the enzyme with a dissociation constant (Kd) equal to 1.4 microM. The enzyme binds FAD by a simple second-order process with Kd 0.67 microM. Site-directed mutagenesis of the residues E43, G44, S45, F47 and Y48 located in the putative binding site of the isoallossazinic portion of FAD reduces the affinity for the coenzyme.lld:pubmed
pubmed-article:8706749pubmed:languageenglld:pubmed
pubmed-article:8706749pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:citationSubsetIMlld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8706749pubmed:statusMEDLINElld:pubmed
pubmed-article:8706749pubmed:monthJullld:pubmed
pubmed-article:8706749pubmed:issn0014-2956lld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:RonchiSSlld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:NegreEElld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:GassenH GHGlld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:TedeschiGGlld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:SimonicTTlld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:FuldS LSLlld:pubmed
pubmed-article:8706749pubmed:authorpubmed-author:MortarinoMMlld:pubmed
pubmed-article:8706749pubmed:issnTypePrintlld:pubmed
pubmed-article:8706749pubmed:day15lld:pubmed
pubmed-article:8706749pubmed:volume239lld:pubmed
pubmed-article:8706749pubmed:ownerNLMlld:pubmed
pubmed-article:8706749pubmed:authorsCompleteYlld:pubmed
pubmed-article:8706749pubmed:pagination418-26lld:pubmed
pubmed-article:8706749pubmed:dateRevised2007-7-23lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:meshHeadingpubmed-meshheading:8706749-...lld:pubmed
pubmed-article:8706749pubmed:year1996lld:pubmed
pubmed-article:8706749pubmed:articleTitleL-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.lld:pubmed
pubmed-article:8706749pubmed:affiliationIstituto di Fisiologia Veterinaria e Biochimica, Università di Milano, Italy.lld:pubmed
pubmed-article:8706749pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8706749pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:8706749pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:947049entrezgene:pubmedpubmed-article:8706749lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8706749lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8706749lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8706749lld:pubmed