Phosphoenolpyruvate Carboxylase
Mostrando 1-12 de 268 artigos, teses e dissertações.
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1. Divisão espacial da atividade das enzimas PEPC e da NR e sua regulação por citocininas em folhas de Guzmania monostachia induzidas ao CAM / Spatial division of PEPC and NR enzymes activity and its regulation by cytokinins in CAM induced leaves of Guzmania monostachia
Estudos anteriores realizados no Laboratório de Fisiologia Vegetal do IBUSP com Guzmania monostachia demonstraram que quando essas plantas são submetidas ao déficit hídrico ocorre a indução do CAM, com maior expressão desse metabolismo na porção foliar apical. Para outra espécie (Vriesea gigantea), foi verificada a maior atividade da enzima nitrato
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 07/08/2012
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2. Calcium partially relieves the deleterius effects of hypoxia on a maize cultivar selected for waterlogging tolerance.
Low soil oxygen concentrations due to waterlogging or transient flooding severely reduce maize production. However, genotypes with tolerance or even resistance to hypoxia develop morphological and biochemical adaptation mechanisms which may prove to be useful criteria for the selection and breeding of new improved genotypes. The objective of this work was to
Revista Brasileira de Milho e Sorgo. Publicado em: 2011
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3. Effects of ZmDof1 and OsDof25 transcriptional factors superexpression on nitrogen usage efficiency in Arabidopsis. / Efeito da superexpressão dos fatores de transcrição ZmDof1 e OsDof25 sobre a eficiência de uso de nitrogênio em Arabidopsis.
To improve nitrogen usage efficiency in plants the rice transcriptional factor OsDof25 was identified and cloned, whose probably orthologe is the maize ZmDof1, already identified and partially characterized. The ZmDof1 was also cloned for comparative analysis with OsDof25, in order to confirm this last one as ZmDof1 orthologe in rice. The constructions for A
Publicado em: 2009
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4. Multiple Forms of Plant Phosphoenolpyruvate Carboxylase Associated with Different Metabolic Pathways 1
The physical and kinetic properties of multiple forms of phosphoenolpyruvate carboxylase were studied in leaves of C4 and C3 species, their F1 and F3 hybrids, in greening maize leaves, in Crassulacean acid metabolism plants, and in nongreen root tissues. Four different forms are suggested: a C4 photosynthetic phosphoenolpyruvate carboxylase with high Km for
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5. Alteration of growth yield by overexpression of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase in Escherichia coli.
Phosphoenolpyruvate and oxaloacetate are key intermediates at the junction between catabolism and biosynthesis. Alteration of carbon flow at these branch points will affect the growth yield and the formation of products. We attempted to modulate the metabolic flow between phosphoenolpyruvate and oxaloacetate by overexpressing phosphoenolpyruvate carboxylase
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6. Anapleurotic CO2 Fixation by Phosphoenolpyruvate Carboxylase in C3 Plants 1
The role of phosphoenolpyruvate carboxylase in photosynthesis in the C3 plant Nicotiana tabacum has been probed by measurement of the 13C content of various materials. Whole leaf and purified ribulose bisphosphate carboxylase are within the range expected for C3 plants. Aspartic acid purified following acid hydrolysis of this ribulose bisphosphate carboxylas
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7. Evidence for Light-stimulated Synthesis of Phosphoenolpyruvate Carboxylase in Leaves of Maize 1
Illumination (22,000 lumens per meter2) of etiolated maize plants for 80 hours brings about a 5-fold increase in phosphoenolpyruvate carboxylase activity per unit of protein. An increase in carboxylase protein and incorporation of [35S]methionine into the protein occurs simultaneously with the activity increase. In green plants, the level of phosphoenolpyruv
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8. Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coli.
Fermentative production of succinic acid from glucose by Escherichia coli was significantly increased by overexpression of phosphoenolpyruvate carboxylase. In contrast, overexpression of phosphoenolpyruvate carboxykinase had no effect. Under optimized conditions, induction of the carboxylase resulted in a 3.5-fold increase in the concentration of succinic ac
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9. Reduced nicotinamide adenine dinucleotide-activated phosphoenolpyruvate carboxylase in Pseudomonas MA: potential regulation between carbon assimilation and energy production.
Comparison of enzyme activities in crude extracts of methylamine-grown Pseudomonas MA (ATCC 23319) to those in succinate-grown cells indicates the involvement of an acetyl coenzyme A-independent phosphoenolpyruvate carboxylase in one-carbon metabolism. The purified phosphoenolpyruvate carboxylase is activated specifically by reduced nicotinamide adenine dinu
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10. Phosphoenolpyruvate Carboxykinase in Plants Exhibiting Crassulacean Acid Metabolism 1
Phosphoenolpyruvate carboxykinase has been found in significant activities in a number of plants exhibiting Crassulacean acid metabolism. Thirty-five species were surveyed for phosphoenolpyruvate carboxykinase, phosphoenolpyruvate carboxylase, ribulose diphosphate carboxylase, malic enzyme, and malate dehydrogenase (NAD). Plants which showed high activities
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11. Kinetic Studies of the Form of Substrate Bound by Phosphoenolpyruvate Carboxylase 1
Phosphoenolpyruvate carboxylase isolated from maize (Zea mays L.) leaves was assayed with varying concentrations of free phosphoenolpyruvate at several fixed-varying concentrations of free magnesium higher than required to saturate the enzyme reaction. These assays produced velocity data which were found to form a family of individual lines when plotted agai
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12. Circadian rhythms in the activity of a plant protein kinase.
Bryophyllum fedtschenkoi is a Crassulacean acid metabolism plant whose phosphoenolpyruvate carboxylase is regulated by reversible phosphorylation in response to a circadian rhythm. A partially purified protein kinase phosphorylated phosphoenolpyruvate carboxylase in vitro with a stoichiometry approaching one per subunit and caused a concomitant 5- to 10-fold