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lactate dehydrogenase/acker schmalwand
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The intrinsically disordered protein LEA7 from Arabidopsis thaliana protects the isolated enzyme lactate dehydrogenase and enzymes in a soluble leaf proteome during freezing and drying.
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The accumulation of Late Embryogenesis Abundant (LEA) proteins in plants is associated with tolerance against stresses such as freezing and desiccation. Two main functions have been attributed to LEA proteins: membrane stabilization and enzyme protection. We have hypothesized previously that LEA7
Functional analysis of a wheat group 3 late embryogenesis abundant protein (TdLEA3) in Arabidopsis thaliana under abiotic and biotic stresses
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Late embryogenesis abundant (LEA) proteins are highly hydrophilic and thermostable proteins that could be induced by abiotic stresses in plants. Previously, we have isolated a group 3 LEA gene TdLEA3 in wheat. The data show that TdLEA3 was largely disordered under fully hydrated conditions and was
D-Lactate dehydrogenase as a marker gene allows positive selection of transgenic plants.
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D-Lactate negatively affects Arabidopsis thaliana seedling development in a concentration-dependent manner. At media D-lactate concentrations greater than 5-10mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate
RcLEA, a late embryogenesis abundant protein gene isolated from Rosa chinensis, confers tolerance to Escherichia coli and Arabidopsis thaliana and stabilizes enzyme activity under diverse stresses.
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The late embryogenesis abundant (LEA) protein family is a large protein family that is closely associated with resistance to abiotic stresses in many organisms, such as plants, bacteria and animals. In this study, we isolated a LEA gene, RcLEA, which was cytoplasm-localized, from Rosa chinensis.
Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways.
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The Arabidopsis thaliana locus At5g06580 encodes an ortholog to Saccharomyces cerevisiae d-lactate dehydrogenase (AtD-LDH). The recombinant protein is a homodimer of 59-kDa subunits with one FAD per monomer. A substrate screen indicated that AtD-LDH catalyzes the oxidation of d- and l-lactate,
d-Lactate Dehydrogenase Links Methylglyoxal Degradation and Electron Transport through Cytochrome c.
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Glycolysis generates methylglyoxal (MGO) as an unavoidable, cytotoxic by-product in plant cells. MGO scavenging is performed by the glyoxalase system, which produces d-lactate as an end product. d-Lactate dehydrogenase (d-LDH) is encoded by a single gene in Arabidopsis (Arabidopsis thaliana;
Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro.
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CONCLUSIONS
Expression of eight LEA genes enhanced desiccation tolerance in yeast, including two LEA_2 genes encoding atypical, stably folded proteins. The recombinant proteins showed enzyme, but not membrane protection during drying. To screen for possible functions of late embryogenesis abundant
Engineered synthesis of rosmarinic acid in Escherichia coli resulting production of a new intermediate, caffeoyl-phenyllactate.
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OBJECTIVE
To achieve high production of rosmarinic acid and derivatives in Escherichia coli which are important phenolic acids found in plants, and display diverse biological activities.
RESULTS
The synthesis of rosmarinic acid was achieved by feeding caffeic acid and constructing an artificial
Identification of a novel LEA protein involved in freezing tolerance in wheat.
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Late embryogenesis abundant (LEA) proteins are a family of hyper-hydrophilic proteins that accumulate in response to cellular dehydration. Originally identified as plant proteins associated with seed desiccation tolerance, LEA proteins have been identified in a wide range of organisms such as
[The content of nitric oxide in blood plasma of health persons depending on age.]
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The article considers results of study of total concentration of nitrites and nitrates (NOx) in blood plasma of healthy individuals residing in St. Petersburg. The samples from 58 healthy individuals were analyzed and out of them - 31 aged 18-25 years and 27 aged 48-63 years. The concentration of
A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity.
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We previously showed that cor15, a cold-regulated gene from Arabidopsis thaliana, encodes a 15 kDa polypeptide designated COR15. Here we report that COR15 has potent cryoprotective activity in an in vitro cryoprotection assay. Specifically, COR15 was very effective in protecting the cold-labile
Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo.
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Late embryogenesis abundant (LEA) proteins are essential to the ability of resurrection plants and orthodox seeds to protect the subcellular milieu against irreversible damage associated with desiccation. In this work, we investigated the structure and function of six LEA proteins expressed during
Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers.
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Many plants acquire increased freezing tolerance when they are exposed to nonfreezing temperatures of a certain duration. This process is known as cold acclimation and allows plants to protect themselves from freezing injury. A wide variety of polypeptides are induced during cold acclimation, among
Disordered cold regulated15 proteins protect chloroplast membranes during freezing through binding and folding, but do not stabilize chloroplast enzymes in vivo.
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Freezing can severely damage plants, limiting geographical distribution of natural populations and leading to major agronomical losses. Plants native to cold climates acquire increased freezing tolerance during exposure to low nonfreezing temperatures in a process termed cold acclimation. This
Biochemical characterization of proline dehydrogenase in Arabidopsis mitochondria.
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Proline has multiple functions in plants. Besides being a building block for protein biosynthesis proline plays a central role in the plant stress response and in further cellular processes. Here, we report an analysis on the integration of proline dehydrogenase (ProDH) into mitochondrial metabolism
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