pubmed-article:9268298 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:9268298 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:9268298 | pubmed:issue | 35 | lld:pubmed |
pubmed-article:9268298 | pubmed:dateCreated | 1997-10-2 | lld:pubmed |
pubmed-article:9268298 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9268298 | pubmed:abstractText | ent-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:9268298 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9268298 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9268298 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9268298 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9268298 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9268298 | pubmed:author | pubmed-author:ImaiRR | lld:pubmed |
pubmed-article:9268298 | pubmed:author | pubmed-author:KamiyaYY | lld:pubmed |
pubmed-article:9268298 | pubmed:author | pubmed-author:SassaTT | lld:pubmed |
pubmed-article:9268298 | pubmed:author | pubmed-author:KawaideHH | lld:pubmed |
pubmed-article:9268298 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9268298 | pubmed:day | 29 | lld:pubmed |
pubmed-article:9268298 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:9268298 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9268298 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9268298 | pubmed:pagination | 21706-12 | lld:pubmed |
pubmed-article:9268298 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9268298 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9268298 | pubmed:articleTitle | Ent-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:9268298 | pubmed:affiliation | Laboratory for Plant Hormone Function, Frontier Research Program, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan.hkwaide@postman.riken.go.jp | lld:pubmed |
pubmed-article:9268298 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9268298 | pubmed:publicationType | Comparative Study | lld:pubmed |
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