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stilbene/arabidopsis thaliana
Врската е зачувана во таблата со исечоци
Страница 1 од 27 резултати
Structural and kinetic analysis of the unnatural fusion protein 4-coumaroyl-CoA ligase::stilbene synthase.
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To increase the biochemical efficiency of biosynthetic systems, metabolic engineers have explored different approaches for organizing enzymes, including the generation of unnatural fusion proteins. Previous work aimed at improving the biosynthesis of resveratrol, a stilbene associated a range of
Tailoring tobacco hairy root metabolism for the production of stilbenes.
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Tobacco hairy root (HR) cultures, which have been widely used for the heterologous production of target compounds, have an innate capacity to bioconvert exogenous t-resveratrol (t-R) into t-piceatannol (t-Pn) and t-pterostilbene (t-Pt). We established genetically engineered HR carrying the gene
Effect of flexible linker length on the activity of fusion protein 4-coumaroyl-CoA ligase::stilbene synthase.
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In order to elucidate the effect of flexible linker length on the catalytic efficiency of fusion proteins, two short flexible peptide linkers of various lengths were fused between Arabidopsis thaliana 4-coumaroyl-CoA ligase (4CL) and Polygonum cuspidatum stilbene synthase (STS) to generate fusion
Expanded acceptor substrates flexibility study of flavonol 7-O-rhamnosyltransferase, AtUGT89C1 from Arabidopsis thaliana.
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Acceptor substrates flexibility of previously characterized flavonol 7-O-rhamnosyltransferase (AtUGT89C1) from Arabidopsis thaliana was explored with an endogenous nucleotide diphosphate sugar and five different classes of flavonoids (flavonols, flavones, flavanones, chalcone and stilbenes) through
Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase.
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We used 5-azido-[7-3H]indole-3-acetic acid (5-azido-[7-3H]IAA), a photoaffinity analogue of the plant hormone indole-3-acetic acid (IAA), to search for auxin-binding proteins in Arabidopsis thaliana membranes. We identified an auxin-binding protein with a molecular mass of 24 kDa (Atpm24) in
Overexpression of Arabidopsis thaliana soluble epoxide hydrolase 1 in Pichia pastoris and characterisation of the recombinant enzyme.
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Epoxide hydrolases are enzymes involved in metabolism and defense of plants. Genome scanning suggested the presence of several genes encoding epoxide hydrolase in Arabidopsis thaliana. To assure that the predicted genes are functional and the translated products have epoxide hydrolase activity
Diverse selective modes among orthologs/paralogs of the chalcone synthase (Chs) gene family of Arabidopsis thaliana and its relative A. halleri ssp. gemmifera.
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As a model system, Arabidopsis thaliana and its wild relatives have played an important role in the study of genomics and evolution in plants. In this study, we examined the genetic diversity of the chalcone synthase (Chs) gene, which encodes a key enzyme of the flavonoid pathway and is located on
VqbZIP1 isolated from Chinese wild Vitis quinquangularis is involved in the ABA signaling pathway and regulates stilbene synthesis.
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Resveratrol is an important phytoalexin in grapevine. Not only does it confer increased disease resistance and but as a food component it offers significant benefits in human health. Abscisic acid (ABA) is an important phytohormone involved in many biological processes in plants and can also promote
The grapevine R2R3-type MYB transcription factor VdMYB1 positively regulates defense responses by activating the stilbene synthase gene 2 (VdSTS2).
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A stilbene synthase gene (SbSTS1) is involved in host and nonhost defense responses in sorghum.
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A chalcone synthase (CHS)-like gene, SbCHS8, with high expressed sequence tag abundance in a pathogen-induced cDNA library, was identified previously in sorghum (Sorghum bicolor). Genomic Southern analysis revealed that SbCHS8 represents a single-copy gene. SbCHS8 expression was induced in sorghum
Biosynthesis of plant-specific stilbene polyketides in metabolically engineered Escherichia coli.
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BACKGROUND
Phenylpropanoids are the precursors to a range of important plant metabolites such as the cell wall constituent lignin and the secondary metabolites belonging to the flavonoid/stilbene class of compounds. The latter class of plant natural products has been shown to function in a wide
Production of resveratrol from p-coumaric acid in recombinant Saccharomyces cerevisiae expressing 4-coumarate:coenzyme A ligase and stilbene synthase genes.
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Resveratrol is a well-known polyphenol present in red wine and exerts antioxidative and anti-carcinogenic effects on the human body. To produce resveratrol in a food-grade yeast, the 4-coumarate:coenzyme A ligase gene (4CL1) from Arabidopsis thaliana and stilbene synthase gene (STS) from Arachis
The methylation status of plant genomic DNA influences PCR efficiency.
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During the polymerase chain reaction (PCR), which is a versatile and widely used method, certain DNA sequences are rapidly amplified through thermocycling. Although there are numerous protocols of PCR optimization for different applications, little is known about the effect of DNA modifications,
Expression of a Grape VqSTS36-Increased Resistance to Powdery Mildew and Osmotic Stress in Arabidopsis but Enhanced Susceptibility to Botrytis cinerea in Arabidopsis and Tomato.
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Stilbene synthase genes make a contribution to improving the tolerances of biotic and abiotic stress in plants. However, the mechanisms mediated by these STS genes remain unclear. To provide insight into the role of STS genes defense against biotic and abiotic stress, we overexpressed VqSTS36 in
Expression of the Grape VqSTS21 Gene in Arabidopsis Confers Resistance to Osmotic Stress and Biotrophic Pathogens but Not Botrytis cinerea.
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Stilbene synthase (STS) is a key gene in the biosynthesis of various stilbenoids, including resveratrol and its derivative glucosides (such as piceid), that has been shown to contribute to disease resistance in plants. However, the mechanism behind such a role has yet to be elucidated. Furthermore,
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