l tyrosine/arabidopsis thaliana

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Identification and Partial Characterization of an L-Tyrosine Aminotransferase (TAT) from Arabidopsis thaliana.

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The aminotransferase gene family in the model plant Arabidopsis thaliana consists of 44 genes. Twenty six of these enzymes are classified as characterized meaning that the reaction(s) that the enzyme catalyzes are documented using experimental means. The remaining 18 enzymes are uncharacterized and

Characterization of transgenic Arabidopsis thaliana with metabolically engineered high levels of p-hydroxybenzylglucosinolate.

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The cytochrome P450 CYP79A1 catalyzes the conversion of L-tyrosine to p-hydroxyphenylacetaldoxime, the first step in the biosynthetic pathway of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. We have demonstrated that introduction of CYP79A1 into Arabidopsis thaliana (L.) Heynh.

Nitrosative stress triggers microtubule reorganization in Arabidopsis thaliana.

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Microtubules (MTs) are essential components of the cytoskeleton and fulfil multiple cellular functions in developmental processes, readily responding to intrinsic and external cues. Nitric oxide signalling is well established in plants, and the MT cytoskeleton is one of its potential targets. To

Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. Catalyzes the conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of benzylglucosinolate.

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Glucosinolates are natural plant products gaining increasing interest as cancer-preventing agents and crop protectants. Similar to cyanogenic glucosides, glucosinolates are derived from amino acids and have aldoximes as intermediates. We report cloning and characterization of cytochrome P450 CYP79A2

Biochemical properties and subcellular localization of tyrosine aminotransferases in Arabidopsis thaliana.

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Plants produce various L-tyrosine (Tyr)-derived compounds that are of pharmaceutical or nutritional importance to humans. Tyr aminotransferase (TAT) catalyzes the reversible transamination between Tyr and 4-hydroxyphenylpyruvate (HPP), the initial step in the biosynthesis of many Tyr-derived plant

TAT1 and TAT2 tyrosine aminotransferases have both distinct and shared functions in tyrosine metabolism and degradation in Arabidopsis thaliana.

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Plants produce various l-tyrosine (Tyr)-derived compounds that are critical for plant adaptation and have pharmaceutical or nutritional importance for human health. Tyrosine aminotransferases (TATs) catalyze the reversible reaction between Tyr and 4-hydroxyphenylpyruvate (HPP), representing the

Imbalance of tyrosine by modulating TyrA arogenate dehydrogenases impacts growth and development of Arabidopsis thaliana.

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L-Tyrosine is an essential aromatic amino acid required for synthesis of proteins and a diverse array of plant natural products; however, little is known how the levels of tyrosine are controlled in planta and linked to overall growth and development. Most plants synthesize tyrosine by TyrA

Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana.

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Full-length tyrosine decarboxylase cDNA (TyrDC) from Arabidopsis thaliana was identified by rapid amplification of cDNA ends-PCR and isolated by RT-PCR. The TyrDC mRNA was substantially induced by drought stress and wounding, and was considerably decreased by salt stress. By using TyrDC protein

Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate.

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The aromatic amino acids L-phenylalanine and L-tyrosine and their plant-derived natural products are essential in human and plant metabolism and physiology. Here we identified Petunia hybrida and Arabidopsis thaliana genes encoding prephenate aminotransferases (PPA-ATs), thus completing the

On the mode of action of the herbicides cinmethylin and 5-benzyloxymethyl-1, 2-isoxazolines: putative inhibitors of plant tyrosine aminotransferase.

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BACKGROUND The mode of action of the grass herbicides cinmethylin and 5-benzyloxymethyl-1,2-isoxazolines substituted with methylthiophene (methiozolin) or pyridine (ISO1, ISO2) was investigated. RESULTS Physiological profiling using a series of biotests and metabolic profiling in treated duckweed

Role of aromatic aldehyde synthase in wounding/herbivory response and flower scent production in different Arabidopsis ecotypes.

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Aromatic L-amino acid decarboxylases (AADCs) are key enzymes operating at the interface between primary and secondary metabolism. The Arabidopsis thaliana genome contains two genes, At2g20340 and At4g28680, encoding pyridoxal 5'-phosphate-dependent AADCs with high homology to the recently identified

Engineered synthesis of rosmarinic acid in Escherichia coli resulting production of a new intermediate, caffeoyl-phenyllactate.

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OBJECTIVE To achieve high production of rosmarinic acid and derivatives in Escherichia coli which are important phenolic acids found in plants, and display diverse biological activities. RESULTS The synthesis of rosmarinic acid was achieved by feeding caffeic acid and constructing an artificial

Rational Engineering of Phenylalanine Accumulation in Pseudomonas taiwanensis to Enable High-Yield Production of Trans-Cinnamate.

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Microbial biocatalysis represents a promising alternative for the production of a variety of aromatic chemicals, where microorganisms are engineered to convert a renewable feedstock under mild production conditions into a valuable chemical building block. This study describes the rational

Evolution of allosteric regulation in chorismate mutases from early plants.

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Plants, fungi, and bacteria synthesize the aromatic amino acids: l-phenylalanine, l-tyrosine, and l-tryptophan. Chorismate mutase catalyzes the branch point reaction of phenylalanine and tyrosine biosynthesis to generate prephenate. In Arabidopsis thaliana, there are two plastid-localized chorismate

The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.

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In Arabidopsis thaliana, four genes have been annotated as provisionally encoding PAL. In this study, recombinant native AtPAL1, 2, and 4 were demonstrated to be catalytically competent for l-phenylalanine deamination, whereas AtPAL3, obtained as a N-terminal His-tagged protein, was of very low

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