acetaldehyde/arabidopsis thaliana

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Identification of superoxide production by Arabidopsis thaliana aldehyde oxidases AAO1 and AAO3.

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Plant aldehyde oxidases (AOs) have gained great attention during the last years as they catalyze the last step in the biosynthesis of the phytohormone abscisic acid by oxidation of abscisic aldehyde. Furthermore, oxidation of indole-3-acetaldehyde by AOs is likely to represent one route to produce

Isolation and biochemical analysis of ethyl methanesulfonate-induced alcohol dehydrogenase null mutants of arabidopsis thaliana (L.) Heynh.

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Several mutants have been isolated at the Arabidopsis thaliana (L.) Heynh. alcohol dehydrogenase (ADH) gene locus using allyl alcohol selection on ethyl methanesulfonate (EMS)-mutagenized seeds. Eleven mutants were isolated in the ADH1-A electrophoretic allele, and 21 in the ADH1-S allele. These

Indole-3-acetaldehyde dehydrogenase-dependent auxin synthesis contributes to virulence of Pseudomonas syringae strain DC3000.

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The bacterial pathogen Pseudomonas syringae modulates plant hormone signaling to promote infection and disease development. P. syringae uses several strategies to manipulate auxin physiology in Arabidopsis thaliana to promote pathogenesis, including its synthesis of indole-3-acetic acid (IAA), the

GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase.

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GEK1, an Arabidopsis thaliana gene product, was recently identified through its involvement in ethanol tolerance. Later, this protein was shown to display 26% strict identity with archaeal d-Tyr-tRNA(Tyr) deacylases. To determine whether it actually possessed deacylase activity, the product of the

Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma plantagineum and Arabidopsis thaliana.

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In order to identify genes that are critical for the ABA-dependent stress response in the resurrection plant Craterostigma plantagineum, a gene was isolated with homology to class 3 variable substrate aldehyde dehydrogenases (ALDH). The C. plantagineum gene Cp-ALDH constitutes a novel class of plant

Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana.

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Aldehyde oxidase (AO; EC 1.2.3.1) activity was measured in seedlings of wild type or an auxin-overproducing mutant, superroot1 (sur1), of Arabidopsis thaliana. Activity staining for AO after native polyacrylamide gel electrophoresis separation of seedling extracts revealed that there were three

Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana.

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Using degenerate primers designed by deduced amino acid sequences of known aldehyde oxidases (AO) from maize and bovine, two independent cDNA fragments were amplified by reverse transcription-polymerase chain reaction (PCR). The two corresponding full-length cDNAs (atAO-1 and atAO-2; 4,484 and 4,228

Polymorphism of alcohol dehydrogenase in Arabidopsis thaliana (L.) Heynh.: genetical and biochemical characterization.

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Zymograms of Arabidopsis alcohol dehydrogenase (ADH; EC 1.1.1.1) show a unique anodal migrating band. Three electrophoretic variants were identified among geographical races and designated slow (S), fast (F), and superfast (A), according to their mobility on Tris-citrate starch gels. In plants ADH

A novel ethanol-hypersensitive mutant of Arabidopsis.

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A novel ethanol-hypersensitive mutant, geko1 (gek1), was isolated from Arabidopsis thaliana. The gek1 mutant displays an enhanced sensitivity (10-100 times greater than the wild type) to ethanol in growth medium, while it grows normally in the absence of ethanol, and responds normally to other

Metabolite fingerprinting in transgenic lettuce.

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Metabolite fingerprinting has been achieved using direct atmospheric pressure chemical ionization-mass spectrometry (APCI-MS) and linked gas chromatography (GC-APCI/EI-MS) for transgenic lettuce (Lactuca sativa L. cv. Evola) plants expressing an IPT gene under the control of the senescence-specific

Failure to Maintain Acetate Homeostasis by Acetate-Activating Enzymes Impacts Plant Development.

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The metabolic intermediate acetyl-coenzyme A (acetyl-CoA) links anabolic and catabolic processes and coordinates metabolism with cellular signaling by influencing protein acetylation. In this study we demonstrate that in Arabidopsis thaliana, two distinctly localized acetate-activating enzymes,

The role of acetyl-coenzyme a synthetase in Arabidopsis.

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The acs1 knockout mutant that has a disruption in the plastidic acetyl-coenzyme A (CoA) synthetase (ACS; At5g36880) gene was used to explore the role of this protein and plastidic acetate metabolism in Arabidopsis (Arabidopsis thaliana). Disruption of the ACS gene decreased ACS activity by 90% and

Tobacco as a production platform for biofuel: overexpression of Arabidopsis DGAT and LEC2 genes increases accumulation and shifts the composition of lipids in green biomass.

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When grown for energy production instead for smoking, tobacco can generate a large amount of inexpensive biomass more efficiently than almost any other agricultural crop. Tobacco possesses potent oil biosynthesis machinery and can accumulate up to 40% of seed weight in oil. In this work, we explored

Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases.

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Plant aromatic amino acid decarboxylase (AAAD) enzymes are capable of catalyzing either decarboxylation or decarboxylation-deamination on various combinations of aromatic amino acid substrates. These two different activities result in the production of arylalkylamines and the formation of aromatic

Auxin biosynthesis in pea: characterization of the tryptamine pathway.

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One pathway leading to the bioactive auxin, indole-3-acetic acid (IAA), is known as the tryptamine pathway, which is suggested to proceed in the sequence: tryptophan (Trp), tryptamine, N-hydroxytryptamine, indole-3-acetaldoxime, indole-3-acetaldehyde (IAAld), IAA. Recently, this pathway has been

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