http://www.cnr.it/ontology/cnr/individuo/prodotto/ID28133
Molecular characterization of b-amyrin-like synthase from Aster sedifolius L. and triterpenoid saponin analysis (Articolo in rivista)
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- Label
- Molecular characterization of b-amyrin-like synthase from Aster sedifolius L. and triterpenoid saponin analysis (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.plantsci.2008.04.004 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Cammareri M.; Consiglio F.; Pecchia P.; Corea G.; Lanzotti V.; Ibeas J.I.; Tava A.; Conicella C. (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR-IGV, Research Institute of Plant Genetics, Research Division: Portici, Via Universita` 133, 80055 Portici, Italy
Department of Chemistry of Natural Products, University of Naples Federico II, Via D. Montesano 49, 80131 Naples, Italy
DISTAAM, University of Molise, Via De Sanctis, 86100 Campobasso, Italy
Centro Andaluz de Bilog´a del Desarrollo, UPO-CSIC, Carretera de Utrera Km 1, 41013 Sevilla, Spain
C.R.A.-Istituto Sperimentale per le Colture Foraggere, viale Piacenza 29, 26900 Lodi, Italy (literal)
- Titolo
- Molecular characterization of b-amyrin-like synthase from Aster sedifolius L. and triterpenoid saponin analysis (literal)
- Abstract
- Triterpenoid saponins are secondary metabolites showing a remarkable structural variety, as well as
notable biological activities. They are synthesised via the isoprenoid pathway by 2,3-oxidosqualene
cyclization mediated by oxidosqualene cyclase (OSC) enzymes. In our previous work, three new
oleanane-type triterpene saponins (astersedifolioside A-C) were isolated from the aerial tissues of Aster
sedifolius L. In this work, the full-length cDNA of a new OSC, designated AsOXA1, was isolated from A.
sedifolius. The AsOXA1 open reading frame consisting of 2286 bp was predicted to encode a protein of 761
amino acid residues. The deduced amino acid sequence of AsOXA1 showed QW and DCTAE motifs which
are highly conserved among the known triterpene synthases. In addition, the comparative and
phylogenetic analysis evidenced that AsOXA1 was closely related to other plant OSCs, and particularly, bamyrin
synthases including that one of Panax ginseng with which it shared a high degree of identity (79%).
Recombinant AsOXA1 has been shown to produce b-amyrin in yeast. RT-PCR analysis evidenced that
AsOXA1 was a tissue-specific gene differentially expressed during plant development. Transcripts of
AsOXA1 accumulated strongly in leaf at the early reproductive stage but were deficient in root. On the
contrary, the accumulation of astersedifoliosides resulted 10-fold higher in roots than in aerial tissues.
Molecular and biochemical results have been discussed. (literal)
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