Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:15950163rdf:typepubmed:Citationlld:pubmed
pubmed-article:15950163lifeskim:mentionsumls-concept:C0022895lld:lifeskim
pubmed-article:15950163lifeskim:mentionsumls-concept:C0060980lld:lifeskim
pubmed-article:15950163pubmed:issue6lld:pubmed
pubmed-article:15950163pubmed:dateCreated2005-6-13lld:pubmed
pubmed-article:15950163pubmed:abstractTextOf the proteins encoded by the three structural genes of the lac operon, the galactoside acetyltransferase (thiogalactoside transacetylase, LacA, GAT) encoded by lacA is the only protein whose biological role remains in doubt. Here, we briefly note the classical literature that led to the identification and initial characterization of GAT, and focus on more recent results which have revealed its chemical mechanism of action and its membership in a large superfamily of structurally similar acyltransferases. The structural and sequence similarities of several members of this superfamily confirm the original claim for GAT as a CoA-dependent acetyltransferase specific for the 6-hydroxyl group of certain pyranosides, but do not yet point to the identity of the natural substrate(s) of the enzyme.lld:pubmed
pubmed-article:15950163pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15950163pubmed:languageenglld:pubmed
pubmed-article:15950163pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15950163pubmed:citationSubsetIMlld:pubmed
pubmed-article:15950163pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15950163pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15950163pubmed:statusMEDLINElld:pubmed
pubmed-article:15950163pubmed:monthJunlld:pubmed
pubmed-article:15950163pubmed:issn1631-0691lld:pubmed
pubmed-article:15950163pubmed:authorpubmed-author:RoderickSteve...lld:pubmed
pubmed-article:15950163pubmed:issnTypePrintlld:pubmed
pubmed-article:15950163pubmed:volume328lld:pubmed
pubmed-article:15950163pubmed:ownerNLMlld:pubmed
pubmed-article:15950163pubmed:authorsCompleteYlld:pubmed
pubmed-article:15950163pubmed:pagination568-75lld:pubmed
pubmed-article:15950163pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:meshHeadingpubmed-meshheading:15950163...lld:pubmed
pubmed-article:15950163pubmed:year2005lld:pubmed
pubmed-article:15950163pubmed:articleTitleThe lac operon galactoside acetyltransferase.lld:pubmed
pubmed-article:15950163pubmed:affiliationDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. roderick@aecom.yu.edulld:pubmed
pubmed-article:15950163pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15950163pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:15950163pubmed:publicationTypeReviewlld:pubmed
pubmed-article:15950163pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
entrez-gene:945674entrezgene:pubmedpubmed-article:15950163lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15950163lld:pubmed