Linked Life Data

10828446

Source:http://linkedlifedata.com/resource/pubmed/id/10828446

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10828446rdf:typepubmed:Citationlld:pubmed
pubmed-article:10828446lifeskim:mentionsumls-concept:C0020792lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C0317894lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C0002520lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C1709915lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C1554080lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C1706198lld:lifeskim
pubmed-article:10828446lifeskim:mentionsumls-concept:C0051793lld:lifeskim
pubmed-article:10828446pubmed:issue1lld:pubmed
pubmed-article:10828446pubmed:dateCreated2000-7-6lld:pubmed
pubmed-article:10828446pubmed:abstractTextAmylosucrase from Neisseria polysaccharea catalyzes the synthesis of an amylose-like polymer from sucrose. Sequence alignment revealed that it belongs to the glycoside hydrolase family 13. Site-directed mutagenesis enabled the identification of functionally important amino acid residues located at the active center. Asp-294 is proposed to act as the catalytic nucleophile and Glu-336 as general acid base catalyst in amylosucrase. The conserved Asp-401, His-195 and His-400 residues are critical for the enzymatic activity. These results provide strong support for the predicted close structural and functional relationship between the sucrose-glucosyltransferases and enzymes of the alpha-amylase family.lld:pubmed
pubmed-article:10828446pubmed:languageenglld:pubmed
pubmed-article:10828446pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:citationSubsetIMlld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10828446pubmed:statusMEDLINElld:pubmed
pubmed-article:10828446pubmed:monthMaylld:pubmed
pubmed-article:10828446pubmed:issn0014-5793lld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:MonsanPPlld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:SvenssonBBlld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:Remaud-Simeon...lld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:SarçabalPPlld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:WillemotRRlld:pubmed
pubmed-article:10828446pubmed:authorpubmed-author:Potocki de...lld:pubmed
pubmed-article:10828446pubmed:issnTypePrintlld:pubmed
pubmed-article:10828446pubmed:day26lld:pubmed
pubmed-article:10828446pubmed:volume474lld:pubmed
pubmed-article:10828446pubmed:ownerNLMlld:pubmed
pubmed-article:10828446pubmed:authorsCompleteYlld:pubmed
pubmed-article:10828446pubmed:pagination33-7lld:pubmed
pubmed-article:10828446pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:meshHeadingpubmed-meshheading:10828446...lld:pubmed
pubmed-article:10828446pubmed:year2000lld:pubmed
pubmed-article:10828446pubmed:articleTitleIdentification of key amino acid residues in Neisseria polysaccharea amylosucrase.lld:pubmed
pubmed-article:10828446pubmed:affiliationCentre de Bioingénierie Gilbert Durand, UMR CNRS 5504, UR INRA 792, INSA, 135 Avenue de Rangueil, 31 077 Toulouse Cedex 4, France.lld:pubmed
pubmed-article:10828446pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10828446pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
literatureCitation:4811_108...literatureCitation:pubmedpubmed-article:10828446lld:drugbank
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10828446lld:pubmed