lactate dehydrogenase/arabidopsis

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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

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

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 analysis of lactate dehydrogenase during hypoxic stress in Arabidopsis

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During waterlogging conditions plants switch from aerobic respiration to anaerobic fermentation to cope with the lack of available oxygen. Plants have two main fermentation pathways: ethanol and lactic acid fermentation. In this paper we carry out a functional analysis of the Arabidopsis lactate

The Arabidopsis KS-type dehydrin recovers lactate dehydrogenase activity inhibited by copper with the contribution of His residues.

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Dehydrin, which is one of the late embryogenesis abundant (LEA) proteins, is involved in the ability of plants to tolerate the lack of water. Although many reports have indicated that dehydrins bind heavy metals, the physiological role of this metal binding has not been well understood. Here, we

F-segments of Arabidopsis dehydrins show cryoprotective activities for lactate dehydrogenase depending on the hydrophobic residues.

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Although dehydrins show cryoprotective activities for freeze-sensitive enzymes, the underlying mechanism is still under investigation. Here, we report that F-segments conserved in some dehydrins cryoprotected lactate dehydrogenase (LDH) as well as K-segments, which were previously identified as

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

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

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.

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

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

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,

GLYCOLATE OXIDASE3, a Glycolate Oxidase Homolog of Yeast l-Lactate Cytochrome c Oxidoreductase, Supports l-Lactate Oxidation in Roots of Arabidopsis.

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In roots of Arabidopsis (Arabidopsis thaliana), l-lactate is generated by the reduction of pyruvate via l-lactate dehydrogenase, but this enzyme does not efficiently catalyze the reverse reaction. Here, we identify the Arabidopsis glycolate oxidase (GOX) paralogs GOX1, GOX2, and GOX3 as putative

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