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phenylalanine/oryza sativa
Veza se sprema u međuspremnik
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Identification of β-phenylalanine as a non-protein amino acid in cultivated rice, Oryza sativa.
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Non-protein amino acids, often analogs of the standard 20 protein amino acids, have been discovered in many plant species. Recent research with cultivated rice (Oryza sativa) identified (3R)-β-tyrosine, as well as a tyrosine amino mutase that synthesizes (3R)-β-tyrosine from the protein amino acid
Induction of Ltp (lipid transfer protein) and Pal (phenylalanine ammonia-lyase) gene expression in rice roots colonized by the arbuscular mycorrhizal fungus Glomus mosseae.
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The expression of a lipid transfer protein (LTP) gene is regulated in Oryza sativa roots in response to colonization by the mycorrhizal fungus Glomus mosseae. Transcript levels increased when the fungus forms appressoria and penetrates the root epidermis and decreased at the onset of the
Molecular and biochemical markers associated with leaffolder (Cnaphalocrocis medinalis G.) resistance in rice (Oryza sativa L.).
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Association of molecular markers namely isozymes and simple sequence repeats (SSRs) and various biochemical markers to leaffolder (Cnaphalocrocis medinalis G., a predominant insect pest of rice) resistance were studied in rice (Oryza sativa L.). Recombinant inbred lines (RILs) of F8 generation
3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase is regulated for the accumulation of polysaccharide-linked hydroxycinnamoyl esters in rice (Oryza sativa L.) internode cell walls.
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Polysaccharide-linked hydroxycinnamoyl esters (PHEs) over-accumulate in the internodes of a rice (Oryza sativa L.) mutant, Fukei 71 (F71). This accumulation is accompanied by over-expression of phenylalanine ammonialyase (PAL). In this study, we show that only one member of the
C-terminal extension of calmodulin-like 3 protein from Oryza sativa L.: interaction with a high mobility group target protein.
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A large number of calmodulin-like (CML) proteins are present in plants, but there is little detailed information on the functions of these proteins in rice (Oryza sativa L.). Here, the CML3 protein from rice (OsCML3) and its truncated form lacking the C-terminal extension (OsCML3m) were found to
Design and application of an in vivo reporter assay for phenylalanine ammonia-lyase.
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Phenylalanine ammonia-lyase (PAL) is an important enzyme that links primary metabolism to secondary metabolism. Its efficiency is often a critical factor that affects the overall flux of a related metabolic pathway, the titer of the final products, and the efficacy of PAL-based therapies. Thus, PAL
Transcriptome analysis reveals that barnyard grass exudates increase the allelopathic potential of allelopathic and non-allelopathic rice (Oryza sativa) accessions.
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Ultraviolet-B-Responsive Anthocyanin Production in a Rice Cultivar Is Associated with a Specific Phase of Phenylalanine Ammonia Lyase Biosynthesis.
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Seedlings of 17 rice (Oryza sativa L.) cultivars were classified on the basis of anthocyanin pigmentation into three groups: an acyanic group with 9 cultivars, a moderately cyanic group with 5 cultivars, and a cyanic group with 3 cultivars. Seedlings of the cyanic group were deep purple in color,
Two phenylalanine ammonia lyase isoforms are involved in the elicitor-induced response of rice to the fungal pathogen Magnaporthe oryzae.
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Suspension cultured cells of a blast-resistant rice genotype (Oryza sativa L. cv. Gigante Vercelli) were treated with cell wall hydrolysates prepared from the fungal pathogen Magnaporthe oryzae. As a consequence, a complex pattern of phenylalanine ammonia lyase time course specific activity levels
Overlapping expression of cytosolic glutamine synthetase and phenylalanine ammonia-lyase in immature leaf blades of rice.
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In order to estimate whether cytosolic glutamine synthetase (GS1; EC 6.3.1.2) is partly coupled to the reaction of phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) in developing organs of rice (Oryza sativa L.), we compared the expression pattern of transcripts and proteins for GS1 and PAL in the
The ectopic expression of phenylalanine ammonia lyase with ectopic accumulation of polysaccharide-linked hydroxycinnamoyl esters in internode parenchyma of rice mutant Fukei 71.
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Both polysaccharide-linked hydroxycinnamoyl esters (PHEs) and lignin are biosynthesized via the phenylpropanoid pathway. In the abnormal internode parenchyma of the rice (Oryza sativa L.) mutant Fukei 71, which has a defective recessive gene (d50), the biosynthesis of lignin and PHEs differs. . The
Combined mass spectrometry-based metabolite profiling of different pigmented rice (Oryza sativa L.) seeds and correlation with antioxidant activities.
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Nine varieties of pigmented rice (Oryza sativa L.) seeds that were black, red, or white were used to perform metabolite profiling by using ultra-performance liquid chromatography-quadrupole-time-of-flight mass spectrometry (UPLC-Q-TOF-MS) and gas chromatography (GC) TOF-MS, to measure antioxidant
Cyanobacteria-mediated phenylpropanoids and phytohormones in rice (Oryza sativa) enhance plant growth and stress tolerance.
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Phenylpropanoids, flavonoids and plant growth regulators in rice (Oryza sativa) variety (UPR 1823) inoculated with different cyanobacterial strains namely Anabaena oryzae, Anabaena doliolum, Phormidium fragile, Calothrix geitonos, Hapalosiphon intricatus, Aulosira fertilissima, Tolypothrix tenuis,
Structural determinants for pyrabactin recognition in ABA receptors in Oryza sativa.
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We determined the structure of OsPYL/RCAR3:OsPP2C50 complex with pyrabactin. Our results suggest that a less-conserved phenylalanine of OsPYL/RCAR subfamily I is one of considerations of ABA agonist development for Oryza sativa. Pyrabactin is a synthetic chemical mimicking abscisic acid (ABA), a
Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase.
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Phenylalanine ammonia-lyase (PAL) genomic sequences were isolated from a rice (Oryza sativa L.) genomic library using a PCR-amplified rice PAL DNA fragment as a probe. There is a small family of PAL genes in the rice genome. The nucleotide sequence of one PAL gene, ZB8, was determined. The ZB8 gene
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