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lipoxygenase/arabidopsis thaliana
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An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens, abscisic acid, and methyl jasmonate.
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We isolated and characterized a 2.8-kb, full-length, Arabidopsis thaliana cDNA clone encoding a lipoxygenase. DNA sequence analysis showed that the deduced amino acid sequence of the Arabidopsis protein is 72 to 78% similar to that of legume seed lipoxygenases. DNA blot analysis indicated that
Lipoxygenase 2 functions in exogenous nitric oxide-induced stomatal closure in Arabidopsis thaliana
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Nitric oxide (NO) and lipoxygenase (LOX)-derived oxylipins play important roles in stomatal closure in plants, and LOX-NO crosstalk has been indicated in mesophyll cells. However, whether the crosstalk also exists in guard cells is not clear and the detailed mechanisms remain unknown. Here, we
Structure and sequence of the Arabidopsis thaliana lipoxygenase 1 gene.
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We have isolated and sequenced the Arabidopsis thaliana LOX1 gene which encodes a lipoxygenase. The 5255 bp sequence includes 763 bp upstream from the start codon, 4345 bp spanning the coding region and 147 bp downstream from the stop codon. The coding region of the LOX1 gene consists of 8 exons
The activity of lipoxygenase in Arabidopsis thaliana (L.) Heynh -- a preliminary study.
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The activity of lipoxygenase (EC 1.13.11.12) in Arabidopsis thaliana (L.) Heynh seedlings and mature plants was estimated spectrophotometrically at 234 nm. Linoleic acid was used as a substrate. Lipoxygenase activity showed two pH optima: at 7.0 and 10.0 in seedlings, and at pH 8.0 and 10.0 in
Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana.
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Lipoxygenases (LOX) catalyze the oxygenation of polyunsaturated fatty acids, the first step in the biosynthesis of a large group of biologically active fatty acid metabolites collectively named oxylipins. In the present study we report the characterization of the enzymatic activity of the six
Four 13-lipoxygenases contribute to rapid jasmonate synthesis in wounded Arabidopsis thaliana leaves: a role for lipoxygenase 6 in responses to long-distance wound signals.
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Damage-inducible defenses in plants are controlled in part by jasmonates, fatty acid-derived regulators that start to accumulate within 30 s of wounding a leaf. Using liquid chromatography-tandem mass spectrometry, we sought to identify the 13-lipoxygenases (13-LOXs) that initiate wound-induced
Lipoxygenase in singlet oxygen generation as a response to wounding: in vivo imaging in Arabidopsis thaliana.
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Wounding, one of the most intensive stresses influencing plants ontogeny and lifespan, can be induced by herbivory as well as by physical factors. Reactive oxygen species play indispensable role both in the local and systemic defense reactions which enable "reprogramming" of metabolic pathways to
Lipoxygenase-derived 9-hydro(pero)xides of linoleoylethanolamide interact with ABA signaling to arrest root development during Arabidopsis seedling establishment.
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Ethanolamide-conjugated fatty acid derivatives, also known as N-acylethanolamines (NAEs), occur at low levels (μg per g) in desiccated seeds, and endogenous amounts decline rapidly with seedling growth. Linoleoylethanolamide (NAE18:2) is the most abundant of these NAEs in seeds of almost all plants,
Facilitation of Fusarium graminearum Infection by 9-Lipoxygenases in Arabidopsis and Wheat.
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Fusarium graminearum causes Fusarium head blight, an important disease of wheat. F. graminearum can also cause disease in Arabidopsis thaliana. Here, we show that the Arabidopsis LOX1 and LOX5 genes, which encode 9-lipoxygenases (9-LOXs), are targeted during this interaction to facilitate infection.
LED lights increase an antioxidant capacity of Arabidopsis thaliana under wound-induced stresses
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A comparison among four light emitting diode (LED) lights including red LED (R), blue LED (B), red (70%) + blue (30%) LED (RB) and white LED (W) as well as fluorescent (F) light was made on antioxidative capacity of Arabidopsis thaliana (L.) Heynh. in response to wounding. Under wound-stress
The Lipoxygenase Lox1 Is Involved in Light- and Injury-Response, Conidiation, and Volatile Organic Compound Biosynthesis in the Mycoparasitic Fungus Trichoderma atroviride
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The necrotrophic mycoparasite Trichoderma atroviride is a biological pest control agent frequently applied in agriculture for the protection of plants against fungal phytopathogens. One of the main secondary metabolites produced by this fungus is 6-pentyl-α-pyrone (6-PP). 6-PP is an organic
The green peach aphid, Myzus persicae, acquires a LIPOXYGENASE5-derived oxylipin from Arabidopsis thaliana, which promotes colonization of the host plant.
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Oxylipins derived from lipoxygenase (LOX) activity play important roles in plant growth, development and stress response. In a recent study, we provided evidence that infestation of Arabidopsis thaliana foliage by the green peach aphid (GPA; Myzus persicae), a phloem sap-consuming insect, was
Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases.
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Herein we characterize the Arabidopsis thaliana AtLOX1 and tomato (Solanum lycopersicum) LOXA proteins as linoleate 9S-lipoxygenases (9-LOX), and use the enzymes to test a model that predicts a relationship between substrate binding orientation and product stereochemistry. The cDNAs were
On the substrate binding of linoleate 9-lipoxygenases.
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Lipoxygenases (LOX; linoleate:oxygen oxidoreductase EC 1.13.11.12) consist of a class of enzymes that catalyze the regio- and stereo specific dioxygenation of polyunsaturated fatty acids. Here we characterize two proteins that belong to the less studied class of 9-LOXs, Solanum tuberosum StLOX1 and
Volatile compound biosynthesis by green leaves from an Arabidopsis thaliana hydroperoxide lyase knockout mutant.
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The degradation of polyunsaturated fatty acids through the lipoxygenase pathway is responsible for the production of volatile compounds that confer green sensory notes to the aroma of fruits and vegetables. The peroxidation of free linoleic or linolenic acid by action of lipoxygenase and then the
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