Linked Life Data

11010873

Source:http://linkedlifedata.com/resource/pubmed/id/11010873

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:11010873rdf:typepubmed:Citationlld:pubmed
pubmed-article:11010873lifeskim:mentionsumls-concept:C0004611lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C1295863lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0009015lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0080194lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0017337lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0679058lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C1547699lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C2700640lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0772162lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:11010873lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:11010873pubmed:issue10lld:pubmed
pubmed-article:11010873pubmed:dateCreated2000-10-17lld:pubmed
pubmed-article:11010873pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:abstractTextA 81-kDa protein from Mycobacterium sp. strain PYR-1 was expressed in response to exposure of the strain to the polycyclic aromatic hydrocarbon pyrene and recovered by two-dimensional gel electrophoresis. The N-terminal sequence of the protein indicated that it was similar to catalase-peroxidase. An oligonucleotide probe designed from this sequence was used to screen a genomic library of Mycobacterium sp. strain PYR-1, and a positive clone, containing a part of the gene encoding the 81-kDa protein, was isolated. A gene-walking technique was used to sequence the entire gene, which was identified as katG for catalase-peroxidase. The deduced KatG protein sequence showed significant homology to KatGII of Mycobacterium fortuitum and clustered with catalase-peroxidase proteins from other Mycobacterium species in a phylogenetic tree. The katG gene was expressed in Escherichia coli to produce a protein with catalase-peroxidase activity. Since the induction of this catalase-peroxidase occurred in pyrene-induced cultures and the exposure of these cultures to hydrogen peroxide reduced pyrene metabolism, our data suggest that this enzyme plays a role in polycyclic aromatic hydrocarbon metabolism by strain PYR-1.lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:languageenglld:pubmed
pubmed-article:11010873pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:citationSubsetIMlld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11010873pubmed:statusMEDLINElld:pubmed
pubmed-article:11010873pubmed:monthOctlld:pubmed
pubmed-article:11010873pubmed:issn0099-2240lld:pubmed
pubmed-article:11010873pubmed:authorpubmed-author:CernigliaC...lld:pubmed
pubmed-article:11010873pubmed:authorpubmed-author:KhanA AAAlld:pubmed
pubmed-article:11010873pubmed:authorpubmed-author:WangR FRFlld:pubmed
pubmed-article:11010873pubmed:authorpubmed-author:XinJ XJXlld:pubmed
pubmed-article:11010873pubmed:authorpubmed-author:WennerstromDDlld:pubmed
pubmed-article:11010873pubmed:issnTypePrintlld:pubmed
pubmed-article:11010873pubmed:volume66lld:pubmed
pubmed-article:11010873pubmed:ownerNLMlld:pubmed
pubmed-article:11010873pubmed:authorsCompleteYlld:pubmed
pubmed-article:11010873pubmed:pagination4300-4lld:pubmed
pubmed-article:11010873pubmed:dateRevised2009-11-18lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:meshHeadingpubmed-meshheading:11010873...lld:pubmed
pubmed-article:11010873pubmed:year2000lld:pubmed
pubmed-article:11010873pubmed:articleTitleCloning, expression, and characterization of the katG gene, encoding catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading bacterium Mycobacterium sp. strain PYR-1.lld:pubmed
pubmed-article:11010873pubmed:affiliationMicrobiology Division, National Center for Toxicological Research, Food and Drug Administration, Jefferson, Arkansas 72079, USA.lld:pubmed
pubmed-article:11010873pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11010873pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11010873lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11010873lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11010873lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11010873lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11010873lld:pubmed