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phospholipase/soia
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In silico and in vitro characterization of phospholipase A₂ isoforms from soybean (Glycine max).
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At the present, no secreted phospholipase A₂ (sPLA₂) from soybean (Glycine max) was investigated in detail. In this work we identified five sequences of putative secreted sPLA₂ from soybean after a BLAST search in G. max database. Sequence analysis showed a conserved PA2c domain bearing the Ca²⁺
Phospholipase D from soybean (Glycine max L.) suspension-cultured cells: purification, structural and enzymatic properties.
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Phospholipase D (phosphatidylcholine phosphatidohydrolase EC 3.1.4.4) from soybean (Glycine max L.) suspension-cultured cell was purified around 1,200-fold to homogeneity by acetone precipitation, Macro-Prep High Q anion exchange, and octyl-Sepharose CL-4B affinity chromatography. The purified
Kinetic characterization, optimum conditions for catalysis and substrate preference of secretory phospholipase A2 from Glycine max in model membrane systems.
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Two secretory phospholipase A2 (sPLA2s) from Glycine max, GmsPLA2-IXA-1 and GmsPLA2-XIB-2, have been purified as recombinant proteins and the activity was evaluated in order to obtain the optimum conditions for catalysis using mixed micelles and lipid monolayers as substrate. Both sPLA2s showed a
Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones.
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Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces. The effect of IAA and IPA auxins over the activity of recombinant sPLA2 isoforms from Glycine max was studied using membrane model
Genomic analysis of phospholipase D family and characterization of GmPLDαs in soybean (Glycine max).
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Phospholipase D (PLD) and its product phosphatidic acid play important roles in the regulation of plant growth, development, and stress responses. The genome database analysis has revealed PLD family in Arabidopsis, rice, poplar and grape. In this study, we report a genomic analysis of 18 putative
Genome-Wide Analysis and Expression Profiling of the Phospholipase C Gene Family in Soybean (Glycine max).
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Phosphatidylinositol-specific phospholipase C (PI-PLC) hydrolyses phosphatidylinositol-4,5-bisphosphate to produce diacylglycerol and inositol 1,4,5-trisphosphate. It plays an important role in plant development and abiotic stress responses. However, systematic analysis and expression profiling of
Phosphatidylinositol specific phospholipase C of plant stems : membrane associated activity concentrated in plasma membranes.
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A phosphatidylinositol-specific phospholipase C of plant stems (EC 3.1.4.10) assayed at pH 6.6 and at 30 degrees C cleaved phosphatidylinositol such that more than 85% of the product was inositol-1-phosphate. Other phospholipids were cleaved 5 to 10% or less under these conditions. The phospholipase
Timecourse microarray analyses reveal global changes in gene expression of susceptible Glycine max (soybean) roots during infection by Heterodera glycines (soybean cyst nematode).
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Changes in gene expression within roots of Glycine max (soybean), cv. Kent, susceptible to infection by Heterodera glycines (the soybean cyst nematode [SCN]), at 6, 12, and 24 h, and 2, 4, 6, and 8 days post-inoculation were monitored using microarrays containing more than 6,000 cDNA inserts.
Secretory Phospholipases A2 in Plants.
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Secreted phospholipases (sPLA2s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA2s were reported from plants. This review discusses the newly
Activation of Plasma Membrane NADH Oxidase Activity by Products of Phospholipase A.
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An auxin-stimulated NADH oxidase activity (NADH oxidase I) of plasma membrane vesicles, highly purified by aqueous two-phase partition from soybean (Glycine max Merr.) hypocotyls was activated by lysophospholipids and fatty acids, both products of phospholipase A action. The activation of NADH
Activation of Phospholipase A by Plant Defense Elicitors.
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Participation of phospholipase A (PLase A) in plant signal transduction has been documented for auxin stimulation of growth but not for elicitation of any plant defense response. In this paper, we report two independent assays for monitoring PLase A induction in plant cells and have used these
Transphosphatidylation by immobilized phospholipase D in aqueous media.
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Phospholipase D (PLD) from Streptomyces sp. was immobilized by covalent binding to aminopropyl-glass activated by glutardialdehyde and to the macroporous synthetic polymer VA-Epoxy Biosynth (from Riedel-de Häen, Seelze, Germany) pre-activated by epoxy groups. The immobilized PLDs were examined for
Action and Inhibition of Endogenous Phospholipases during Isolation of Plant Membranes.
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Endogenous phospholipase D and phosphatidic acid phosphatase activities were demonstrated in membrane fractions isolated from soybean (Glycine max L.) hypocotyls. Phospholipase D activity was distributed widely among different membrane fractions while phosphatidic acid phosphatase was found
Phosphatidic acid activates a wound-activated MAPK in Glycine max.
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Many plant species demonstrate a systemic increase in phosphatidic acid (PA) levels after being wounded (Lee et al., 1997). To understand the role of PA in wound signal transduction, we investigated if PA can activate protein kinases in soybean (Glycine max L.). We found that a MAPK is activated in
A rapid response to a plant hormone: auxin stimulates phospholipase A2 in vivo and in vitro.
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Addition of the active auxins indole-3-acetic acid, 2,4-dichlorophenoxyacetic acid or alpha-naphthylacetic acid to cultured soybean (Glycine max L.) cells prelabeled with ethanolamine or choline increased the radioactivity in the lysophosphatidylethanolamine (LPE) or lysophosphatidylcholine (LPC)
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