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carboxylase/soja
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Effect of irradiance during growth of Glycine max on photosynthetic capacity and percent activation of ribulose 1,5-bisphosphate carboxylase.
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The initial (in vivo) and total (activity present after preincubation with CO2 and Mg(2+)) activities of ribulose bisphosphate carboxylase were both assayed in extracts of leaves of soybean (Glycine max) plants which had been grown under 4 different irradiance levels. The total carboxylase activity
The PEP-carboxylase kinase gene family in Glycine max (GmPpcK1-4): an in-depth molecular analysis with nodulated, non-transgenic and transgenic plants.
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Phosphoenolpyruvate carboxylase (PEPC) is a widely distributed metabolic enzyme among plant and prokaryotic species. In vascular plants, the typical PEPC is regulated post-translationally by a complex interplay between opposing metabolite effectors and reversible protein phosphorylation. This
Phosphorylation of Soybean (Glycine max L.) Nodule Phosphoenolpyruvate Carboxylase in Vitro Decreases Sensitivity to Inhibition by L-Malate.
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Phosphoenolpyruvate carboxylase (PEPC) from soybean (Glycine max L.Merr.) nodules was purified 187-fold to a final specific activity of 56 units mg-1 of protein. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) revealed one major polypeptide band, with a molecular mass of 110
Co-localization of carbonic anhydrase and phosphoenol-pyruvate carboxylase and localization of pyruvate kinase in roots and hypocotyls of etiolated Glycine max seedlings.
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We investigated the presence of carbonic anhydrase in root and hypocotyl of etiolated soybean using enzymatic, histochemical, immunohistochemical and in situ hybridization approaches. In parallel, we used in situ hybridization and immunolocalization to determine the expression pattern and
Sequence of a soybean (Glycine max L.) phosphoenolpyruvate carboxylase cDNA.
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rbcS SRS4 promoter from Glycine max and its expression activity in transgenic tobacco.
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The regulatory region of the ribulose-1,5-bisphosphate carboxylase small subunit gene SRS4 from soybean (Glycine max) was cloned using TAIL-PCR and general PCR, and named the rbcS promoter. The promoter was fused with the GUS gene and introduced into Nicotiana tabacum via Agrobacterium-mediated leaf
Effects of Light and Elevated Atmospheric CO(2) on the Ribulose Bisphosphate Carboxylase Activity and Ribulose Bisphosphate Level of Soybean Leaves.
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Soybean (Glycine max L. Merr. cv Bragg) was grown throughout its life cycle at 330, 450, and 800 microliters CO(2) per liter in outdoor controlled-environment chambers under solar irradiance. Leaf ribulose-1,5-bisphosphate carboxylase (RuBPCase) activities and ribulose-1,5-bisphosphate (RuBP) levels
A multisubunit acetyl coenzyme A carboxylase from soybean.
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A multisubunit form of acetyl coenzyme A (CoA) carboxylase (ACCase) from soybean (Glycine max) was characterized. The enzyme catalyzes the formation of malonyl CoA from acetyl CoA, a rate-limiting step in fatty acid biosynthesis. The four known components that constitute plastid ACCase are biotin
3-Methylcrotonyl-coenzyme A carboxylase is a component of the mitochondrial leucine catabolic pathway in plants
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3-Methylcrotonyl-coenzyme A carboxylase (MCCase) is a mitochondrial biotin-containing enzyme whose metabolic function is not well understood in plants. In soybean (Glycine max) seedlings the organ-specific and developmentally induced changes in MCCase expression are regulated by mechanisms that
Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates.
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Exposure of leaf sections from 2-week-old seedlings of sorghum (Sorghum bicolor L.) (C(4) plant), corn (Zea mays L.) (C(4)), peanut (Arachis hypogaea L.) (C(3) plant), and soybean (Glycine max L.) (C(3)) to 40 or 45 degrees C for up to 4 hours resulted in significant increases in the levels of 102
Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.
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3-Methylcrotonyl-CoA: carboxylase (EC 6.4.1.4; MCC) deficiency is an inborn error of the leucine degradation pathway (MIM *210200) characterized by increased urinary excretion of 3-hydroxyisovaleric acid and 3-methylcrotonylglycine. The clinical phenotypes are highly variable ranging from
Light adaptation/acclimation of photosynthesis and the regulation of ribulose-1,5-bisphosphate carboxylase activity in sun and shade plants.
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The consequences of light adaptation and acclimation of photosynthesis on photosynthetic nitrogen use efficiency (NUE), particularly as it relates to the efficiency of ribulose-1,5-bisphosphate carboxylase (Rubisco) use in photosynthetic CO(2) assimilation, was studied in the sun species Glycine max
cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene from soybean.
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A full-length cDNA encoding a subunit of phosphoenolpyruvate carboxylase (PEPC) was isolated from a developing seed expression library of the C3 plant Glycine max. The corresponding mRNA is present at similar levels in leaf, stem, root and developing seed. Two potential start codons exist, and the
Roots, cycles and leaves. Expression of the phosphoenolpyruvate carboxylase kinase gene family in soybean.
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Phosphorylation of phosphoenolpyruvate carboxylase (PEPc; EC 4.1.1.31) plays an important role in the control of central metabolism of higher plants. This phosphorylation is controlled largely at the level of expression of PEPc kinase (PPCK) genes. We have analyzed the expression of both PPCK genes
Identification and expression of a soybean nodule-enhanced PEP-carboxylase kinase gene (NE-PpcK) that shows striking up-/down-regulation in vivo.
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Various isoforms of plant phosphoenolpyruvate carboxylase (PEPC (Ppc)) are controlled post-translationally by an intricate interaction between allosteric regulation and reversible protein phosphorylation. In leaves and root nodules of legumes, these changes in PEPC phosphorylation state are governed
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