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homoglutathione/soya
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Glutathione and homoglutathione synthesis in legume root nodules.
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High-performance liquid chromatography (HPLC) with fluorescence detection was used to study thiol metabolism in legume nodules. Glutathione (GSH) was the major non-protein thiol in all indeterminate nodules examined, as well as in the determinate nodules of cowpea (Vigna unguiculata), whereas
From sulfur to homoglutathione: thiol metabolism in soybean.
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Sulfur is an essential plant nutrient and is metabolized into the sulfur-containing amino acids (cysteine and methionine) and into molecules that protect plants against oxidative and environmental stresses. Although studies of thiol metabolism in the model plant Arabidopsis thaliana (thale cress)
Molecular characterization of the homo-phytochelatin synthase of soybean Glycine max: relation to phytochelatin synthase.
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The phytochelatin homologs homo-phytochelatins are heavy metal-binding peptides present in many legumes. To study the biosynthesis of these compounds, we have isolated and functionally expressed a cDNA GmhPCS1 encoding homo-phytochelatin synthase from Glycine max, a plant known to accumulate
Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays).
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Unlike animals which accumulate glutathione (gamma-glutamyl-L-cysteinyl-glycine) alone as their major thiol antioxidant, several crops synthesize alternative forms of glutathione by varying the carboxy residue. The molecular basis of this variation is not well understood, but the substrate
Manipulation of plant tolerance to herbicides through co-ordinated metabolic engineering of a detoxifying glutathione transferase and thiol cosubstrate.
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The diphenyl ether herbicide fomesafen can be used selectively in soybean (Glycine max) due to its rapid detoxification by tau class glutathione transferases (GmGSTUs) which preferentially utilize the endogenous thiol homoglutathione (hGSH) as cosubstrate. Soybean cDNAs encoding GmGSTU21, which is
A reassessment of substrate specificity and activation of phytochelatin synthases from model plants by physiologically relevant metals.
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Phytochelatin synthases (PCS) catalyze phytochelatin (PC) synthesis from glutathione (GSH) in the presence of certain metals. The resulting PC-metal complexes are transported into the vacuole, avoiding toxic effects on metabolism. Legumes have the unique capacity to partially or completely replace
Effect of Nitrogen Nutrition on Remobilization of Protein Sulfur in the Leaves of Vegetative Soybean and Associated Changes in Soluble Sulfur Metabolites.
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The hypothesis that protein S is remobilized from mature leaves in response to N stress but not S stress was examined by transferring vegetative soybean (Glycine max L. Merr) plants grown with adequate sulfate and nitrate to nutrient medium with low sulfate (5 [mu]M) and nitrate at either 15, 7.5,
Allocation of S in Generative Growth of Soybean.
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Soybean plants (Glycine max L. Merr) were grown with 100 [mu]M S and 15 mM N and studied with respect to S allocation during grain development. The grains accounted for 87% of the S taken up after d 42, the balance coming from internal redistribution of S from leaves and pods. Detailed studies of
Structural basis for evolution of product diversity in soybean glutathione biosynthesis.
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The redox active peptide glutathione is ubiquitous in nature, but some plants also synthesize glutathione analogs in response to environmental stresses. To understand the evolution of chemical diversity in the closely related enzymes homoglutathione synthetase (hGS) and glutathione synthetase (GS),
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