| pubmed-article:12782296 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12782296 | lifeskim:mentions | umls-concept:C0994493 | lld:lifeskim |
| pubmed-article:12782296 | lifeskim:mentions | umls-concept:C0596577 | lld:lifeskim |
| pubmed-article:12782296 | lifeskim:mentions | umls-concept:C0599874 | lld:lifeskim |
| pubmed-article:12782296 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
| pubmed-article:12782296 | pubmed:issue | 1-3 | lld:pubmed |
| pubmed-article:12782296 | pubmed:dateCreated | 2003-6-3 | lld:pubmed |
| pubmed-article:12782296 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:abstractText | Flavone synthases (FNSs) catalyze the oxidation of flavanones to flavones, i.e. the formation of apigenin from (2S)-naringenin. While many plants express a microsomal-type FNS II, the soluble FNS I appears to be confined to a few species of the Apiaceae and was cloned recently from parsley plants. FNS I belongs to the Fe(II)/2-oxoglutarate-dependent dioxygenases characterized by short conserved sequence elements for cofactor binding, and its evolutionary context and mode of action are under investigation. Using a homology-based reverse transcription polymerase chain reaction approach, two additional flavonoid-specific dioxygenases were cloned from immature parsley leaflets, which were identified as flavanone 3beta-hydroxylase (FHT) and flavonol synthase (FLS) after expression in yeast cells. Sequence alignments revealed marginal differences among the parsley FNS I and FHT polypeptides of only 6%, while much less identity (about 29%) was observed with the parsley FLS. Analogous to FNS I, FLS oxidizes the flavonoid gamma-pyrone by introducing a C2, C3 double bond, and (2R,3S)-dihydrokaempferol (cis-dihydrokaempferol) was proposed recently as the most likely intermediate in both FNS I and FLS catalysis. Incubation of either FNS I or FLS with cis-dihydrokaempferol exclusively produced kaempferol and confirmed the assumption that flavonol formation occurs via hydroxylation at C3 followed by dehydratation. However, the lack of apigenin in these incubations ruled out cis-dihydrokaempferol as a free intermediate in FNS I catalysis. Furthermore, neither (+)-trans-dihydrokaempferol nor unnatural (-)-trans-dihydrokaempferol and 2-hydroxynaringenin served as a substrate for FNS I. Overall, the data suggest that FNS I has evolved uniquely in some Apiaceae as a paraphyletic gene from FHT, irrespective of the fact that FNS I and FLS catalyze equivalent desaturation reactions. | lld:pubmed |
| pubmed-article:12782296 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12782296 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12782296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12782296 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12782296 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12782296 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:WellmannFrank... | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:LukacinRichar... | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:BritschLothar... | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:MaternUlrichU | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:MartensStefan... | lld:pubmed |
| pubmed-article:12782296 | pubmed:author | pubmed-author:ForkmannGertG | lld:pubmed |
| pubmed-article:12782296 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12782296 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:12782296 | pubmed:volume | 544 | lld:pubmed |
| pubmed-article:12782296 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12782296 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12782296 | pubmed:pagination | 93-8 | lld:pubmed |
| pubmed-article:12782296 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12782296 | pubmed:meshHeading | pubmed-meshheading:12782296... | lld:pubmed |
| pubmed-article:12782296 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12782296 | pubmed:articleTitle | Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. | lld:pubmed |
| pubmed-article:12782296 | pubmed:affiliation | Institut für Pharmazeutische Biologie, Philipps-Universität Marburg, Deutschhausstrasse 17 A, Germany. | lld:pubmed |
| pubmed-article:12782296 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12782296 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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