Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9268298rdf:typepubmed:Citationlld:pubmed
pubmed-article:9268298lifeskim:mentionsumls-concept:C0016832lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C1025560lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0521009lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0006556lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0012780lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0204727lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0205409lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0521033lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C1157346lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0663613lld:lifeskim
pubmed-article:9268298lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:9268298pubmed:issue35lld:pubmed
pubmed-article:9268298pubmed:dateCreated1997-10-2lld:pubmed
pubmed-article:9268298pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:abstractTextent-Kaurene is the first cyclic diterpene intermediate of gibberellin biosynthesis in both plants and fungi. In plants, ent-kaurene is synthesized from geranylgeranyl diphosphate via copalyl diphosphate in a two-step cyclization catalyzed by copalyl diphosphate synthase and ent-kaurene synthase. A cell-free system of the fungus Phaeosphaeria sp. L487 converted labeled geranylgeranyl diphosphate to ent-kaurene. A cDNA fragment, which possibly encodes copalyl diphosphate synthase, was isolated by reverse transcription-polymerase chain reaction using degenerate primers based on the consensus motifs of plant enzymes. Translation of a full-length cDNA sequence isolated from the fungal cDNA library revealed an open reading frame for a 106-kDa polypeptide. The deduced amino acid sequence shared 24 and 21% identity with maize copalyl diphosphate synthase and pumpkin ent-kaurene synthase, respectively. A fusion protein produced by expression of the cDNA in Escherichia coli catalyzed the two-step cyclization of geranylgeranyl diphosphate to ent-kaurene. Amo-1618 completely inhibited the copalyl diphosphate synthase activity of the enzyme at 10(-6) M, whereas it did not inhibit the ent-kaurene synthase activity even at 10(-4) M. These results indicate that the fungus has a bifunctional diterpene cyclase that can convert geranylgeranyl diphosphate into ent-kaurene. They may be separate catalytic sites for the two cyclization reactions.lld:pubmed
pubmed-article:9268298pubmed:languageenglld:pubmed
pubmed-article:9268298pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:citationSubsetIMlld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9268298pubmed:statusMEDLINElld:pubmed
pubmed-article:9268298pubmed:monthAuglld:pubmed
pubmed-article:9268298pubmed:issn0021-9258lld:pubmed
pubmed-article:9268298pubmed:authorpubmed-author:ImaiRRlld:pubmed
pubmed-article:9268298pubmed:authorpubmed-author:KamiyaYYlld:pubmed
pubmed-article:9268298pubmed:authorpubmed-author:SassaTTlld:pubmed
pubmed-article:9268298pubmed:authorpubmed-author:KawaideHHlld:pubmed
pubmed-article:9268298pubmed:issnTypePrintlld:pubmed
pubmed-article:9268298pubmed:day29lld:pubmed
pubmed-article:9268298pubmed:volume272lld:pubmed
pubmed-article:9268298pubmed:ownerNLMlld:pubmed
pubmed-article:9268298pubmed:authorsCompleteYlld:pubmed
pubmed-article:9268298pubmed:pagination21706-12lld:pubmed
pubmed-article:9268298pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:meshHeadingpubmed-meshheading:9268298-...lld:pubmed
pubmed-article:9268298pubmed:year1997lld:pubmed
pubmed-article:9268298pubmed:articleTitleEnt-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis.lld:pubmed
pubmed-article:9268298pubmed:affiliationLaboratory for Plant Hormone Function, Frontier Research Program, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan.hkwaide@postman.riken.go.jplld:pubmed
pubmed-article:9268298pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9268298pubmed:publicationTypeComparative Studylld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9268298lld:pubmed