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amyrin/arabidopsis thaliana
L'enllaç es desa al porta-retalls
Pàgina 1 des de 17 resultats
Identification of a product specific beta-amyrin synthase from Arabidopsis thaliana.
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Triterpene skeletons are produced by oxidosqualene cyclases (OSCs). The genome sequencing of Arabidopsis thaliana revealed the presence of thirteen OSC homologous genes including At1g78950, which has been revised recently as two independent ORFs, namely At1g78950 and At1g78955. The cDNA
Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol.
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The Arabidopsis thaliana LUP1 gene encodes an enzyme that converts oxidosqualene to pentacyclic triterpenes. Lupeol and beta-amyrin were previously reported as LUP1 products. Further investigation described here uncovered the additional products germanicol, taraxasterol, psi-taraxasterol, and
Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana.
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A vast array of triterpenes are found in living organisms in addition to lanosterol and cycloartenol, which are involved in sterol biosynthesis in non-photosynthetic and photosynthetic eukaryotes respectively. The chemical structure of these triterpenes is determined by a single step catalysed by
Momilactone sensitive proteins in Arabidopsis thaliana.
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The labdane-related diterpenoid, momilactone B has potent growth inhibitory activity and was demonstrated to play a particularly critical role in the allelopathy of rice (Oryza sativa L.). However, there is limited information available about the mode of action of momilactone B on the growth
Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene.
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A 2274 bp Arabidopsis thaliana cDNA was isolated that encodes a protein 57% identical to cycloartenol synthase from the same organism. The expressed recombinant protein encodes lupeol synthase, which converts oxidosqualene to the triterpene lupeol as the major product. Lupeol synthase is a
Cloning and characterization of a cDNA encoding beta-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice.
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An oxidosqualene cyclase cDNA, termed GgbAS1, was isolated from cultured cells of licorice (Glycyrrhiza glabra) by heterologous hybridization with cDNA of Arabidopsis thaliana LUP1 lupeol synthase. The yeast transformed with an expression vector containing the open reading frame of GgbAS1 produced
Pathway engineering for the production of β-amyrin and cycloartenol in Escherichia coli-a method to biosynthesize plant-derived triterpene skeletons in E. coli.
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Cycloartenol is biosynthetically the first sterol skeleton, which is metabolized to phytosterols such as β-sitosterol and stigmasterol. β-Amyrin is the most commonly occurring aglycone skeleton for oleanane-type saponins such as glycyrrhizin and saikosaponins. It has been regarded that these cyclic
Novel triterpene oxidizing activity of Arabidopsis thaliana CYP716A subfamily enzymes.
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Triterpenoids have diverse chemical structures and bioactivities. Cytochrome P450 monooxygenases play a key role in their structural diversification. In higher plants, CYP716A subfamily enzymes are triterpene oxidases. In this study, Arabidopsis thaliana CYP716A1 and CYP716A2 were characterized by
Composition and physiological function of the wax layers coating Arabidopsis leaves: β-amyrin negatively affects the intracuticular water barrier.
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Plants prevent dehydration by coating their aerial, primary organs with waxes. Wax compositions frequently differ between species, organs, and developmental stages, probably to balance limiting nonstomatal water loss with various other ecophysiological roles of surface waxes. To establish
Arabidopsis camelliol C synthase evolved from enzymes that make pentacycles.
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We establish by heterologous expression that the Arabidopsis thaliana oxidosqualene cyclase At1g78955 (CAMS1) makes camelliol C (98%), achilleol A (2%), and beta-amyrin (0.2%). CAMS1 is the first characterized cyclase that generates predominantly a monocyclic triterpene alcohol. Phylogenetic
Efficient production of glycyrrhetinic acid in metabolically engineered Saccharomyces cerevisiae via an integrated strategy.
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Overexpression of a synthetic insect-plant geranyl pyrophosphate synthase gene in Camelina sativa alters plant growth and terpene biosynthesis.
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CONCLUSIONS
A novel plastidial homodimeric insect-plant geranyl pyrophosphate synthase gene is synthesized from three different cDNA origins. Its overexpression in Camelina sativa effectively alters plant development and terpenoid metabolism. Geranyl pyrophosphate synthase (GPPS) converts one
[Optimization of synthetic pathway and fermentation process of yeast cell factories for production of oleanoic acid].
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OBJECTIVE
To optimize the synthetic pathway and fermentation process of yeast cell factories for production of oleanoic acid.
METHODS
Using the DNA assembler method, one copy of Glycyrrhiza glabra beta-amyrin synthase (GgbAS), Medicago truncatula oleanolic acid synthase (MtOAS) and Arabidopsis
Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases.
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Two new triterpene synthase cDNAs, named as OEW and TRW, were cloned from olive leaves (Olea europaea) and from dandelion roots (Taraxacum officinale), respectively, by the PCR method with primers designed from the conserved sequences found in the known oxidosqualene cyclases. Their ORFs consisted
Molecular characterization of the pentacyclic triterpenoid biosynthetic pathway in Catharanthus roseus.
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Catharanthus roseus is an important medicinal plant and the sole commercial source of monoterpenoid indole alkaloids (MIA), anticancer compounds. Recently, triterpenoids like ursolic acid and oleanolic acid have also been found in considerable amounts in C. roseus leaf cuticular wax layer. These
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