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benzaldehyde/harilik müürlook

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ArtiklidKliinilistes uuringutesPatendid
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A total of eleven alkali-released, aromatic compounds were identified by HPLC, MS and NMR analyses in cell wall extracts from Arabidopsis thaliana roots. Nine of them together constituted the three complete series of 4-hydroxy-, 4-hydroxy-3-methoxy, and 4-hydroxy-3,5-dimethoxy-substituted
Plant perception of insect feeding involves integration of the multiple signals involved: wounding, oral secretions, and substrate borne feeding vibrations. Although plant responses to wounding and oral secretions have been studied, little is known about how signals from the rapidly transmitted

Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP+ oxidoreductase.

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We expressed a cDNA encoding the Arabidopsis thaliana defense-related protein ELI3-2 in Escherichia coli to determine its biochemical function. Based on a protein database search, this protein was recently predicted to be a mannitol dehydrogenase [Williamson, J. D., Stoop, J. M. H., Massel, M. O.,

An aldehyde oxidase in developing seeds of Arabidopsis converts benzaldehyde to benzoic Acid.

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Arabidopsis (Arabidopsis thaliana) siliques synthesize high levels of benzoic acid (BA), which is incorporated into several glucosinolate compounds. The origin of BA in the siliques has not yet been determined. Here, we show that siliques have higher levels of benzaldehyde (BD)-oxidizing activity
Objectives: Chiral 2-hydroxycarboxylic acids and 2-hydroxycarboxamides are valuable synthons for the chemical industry. Results: The biocatalytic syntheses of (R)-mandelic acid

Arabidopsis Chy1 null mutants are deficient in benzoic acid-containing glucosinolates in the seeds.

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The specific set of reactions that lead to the synthesis of benzoic acid in plants is still unclear, and even the subcellular compartment in which these reactions occur is unknown. Biosynthesis of both vegetative tissues and seeds of Arabidopsis thaliana contain a class of defense compounds termed

Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris.

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To investigate the biochemical and enzymatic properties of two aldehyde oxidase (AO) isoforms of Arabidopsis thaliana, we expressed AAO1 and AAO2 cDNAs in a heterologous yeast (Pichia pastoris) system and successfully obtained the proteins in active forms. The expressed AAO1 and AAO2 proteins gave
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