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decarboxylase/oryza sativa
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Seite 1 von 48 Ergebnisse
Knockdown of glycine decarboxylase complex alters photorespiratory carbon isotope fractionation in Oryza sativa leaves.
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The influence of reduced glycine decarboxylase complex (GDC) activity on leaf atmosphere CO2 and 13CO2 exchange was tested in transgenic Oryza sativa with the GDC H-subunit knocked down in leaf mesophyll cells. Leaf measurements on transgenic gdch knockdown and wild-type plants were carried out in
Increased polyamine biosynthesis enhances stress tolerance by preventing the accumulation of reactive oxygen species: T-DNA mutational analysis of Oryza sativa lysine decarboxylase-like protein 1.
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A highly oxidative stress-tolerant japonica rice line was isolated by T-DNA insertion mutation followed by screening in the presence of 50 mM H(2)O(2). The T-DNA insertion was mapped to locus Os09g0547500, the gene product of which was annotated as lysine decarboxylase-like protein (GenBank
Expression of arginine decarboxylase in seedlings of indica rice (Oryza sativa L.) cultivars as affected by salinity stress.
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The effect of salinity stress on the activity of arginine decarboxylase (ADC, EC 4.1.1.19), the first enzyme in biosynthesis of polyamines (PA) from arginine, as well as its transcript level has been compared in salt-sensitive (M-1-48) and salt-tolerant (Pokkali) rice cultivars. Treatment of 72 h
Purification and partial characterization of pyruvate decarboxylase from Oryza sativa L.
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Pyruvate decarboxylase(PyrDC) was purified from rice bran to a specific activity of 1 mu kat/mg and partially characterized. The holoenzyme is a tetramer of two types of subunits with molecular masses 64 kDa and 62 kDa. Purified rice PyrDC exhibits positive cooperative kinetics with respect to
Enhanced resistance to rice blast and sheath blight in rice (oryza sativa L.) by expressing the oxalate decarboxylase protein Bacisubin from Bacillus subtilis.
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Oxalate decarboxylase (OxDC), catalyzing the degradation of oxalic acid, is widely distributed in varieties of organisms. In this study, an oxalate decarboxylase gene from Bacillus subtilis strain BS-916, Bacisubin, was transformed into rice variety Nipponbare to generate transgenic rice with
Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus.
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We have isolated full-length cDNAs for two distinct isoforms of glutamate decarboxylase (GAD), designated OsGAD1 and OsGAD2 from a rice shoot cDNA library. Open reading frames found in OsGAD1 and OsGAD2 cDNAs encode putative proteins of 501 (56.7 kDa) and 500 amino acids (55.6 kDa), respectively.
Sequence of a cDNA from Oryza sativa (L.) encoding the pyruvate decarboxylase 1 gene.
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Cloning and characterization of a rice cDNA encoding glutamate decarboxylase.
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In this study, we have isolated a rice (Oryza sativa L.) glutamate decarboxylase (RicGAD) clone from a root cDNA library, using a partial Arabidopsis thaliana GAD gene as a probe. The rice root cDNA library was constructed with mRNA, which had been derived from the roots of rice seedlings subjected
Cloning and expression of rice glutamate decarboxylase (GAD) in Escherichia coli.
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Glutamate decarboxylase (GAD) converts L-glutamate to g-aminobutyric acid (GABA), which is a non-protein amino acid present in all organisms with some activities including improvement of neurve and cytoskeltal functions. Therefore, GAD is considered as a key molecule to use in molecular therapy of
Differential expression of an S-adenosyl-L-methionine decarboxylase gene involved in polyamine biosynthesis under low temperature stress in japonica and indica rice genotypes.
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We have investigated the regulation of the rice (Oryza sativa) gene OsSAMDC, which encodes an S-adenosyl-L-methionine decarboxylase (SAMDC) involved in polyamine biosynthesis. Clones representing genes differentially expressed at 5 degrees C and 20 degrees C were isolated from a cDNA library
Expression of a heterologous S-adenosylmethionine decarboxylase cDNA in plants demonstrates that changes in S-adenosyl-L-methionine decarboxylase activity determine levels of the higher polyamines spermidine and spermine.
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We posed the question of whether steady-state levels of the higher polyamines spermidine and spermine in plants can be influenced by overexpression of a heterologous cDNA involved in the later steps of the pathway, in the absence of any further manipulation of the two synthases that are also
Ethylene-Induced Polyamine Accumulation in Rice (Oryza sativa L.) Coleoptiles.
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Effects of ethylene on free polyamine biosynthesis in rice (Oryza sativa L. cv Taichung Native 1) coleoptiles were investigated in sealed and aerobic conditions. In sealed conditions, putrescine increased significantly and coincided with ethylene accumulation. Application of ethylene in sealed
Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.).
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Lipoic acid is an essential disulfide cofactor required for the lipoate-dependent enzymes including pyruvate dehydrogenase (PDH), alpha-ketoglutarate dehydrogenase (KGDH), and glycine cleavage enzymes that function in key metabolic pathways in most prokaryotes and eukaryotes. Lipoic acid is
Reduction in the endogenous arginine decarboxylase transcript levels in rice leads to depletion of the putrescine and spermidine pools with no concomitant changes in the expression of downstream genes in the polyamine biosynthetic pathway.
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We investigated whether down-regulation of arginine decarboxylase (ADC) activity and concomitant changes in polyamine levels result in changes in the expression of downstream genes in the polyamine pathway. We generated transgenic rice (Oryza sativa L.) plants in which the rice adc gene was
Arginine decarboxylase transgene expression and analysis of environmental stress tolerance in transgenic rice.
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Arginine decarboxylase (ADC) cDNA from oat (Avena sativa L.) was introduced into rice (Oryza sativa L.) genome by an Agrobacterium-mediated transformation method. Expression of the ADC transgene under the control of an ABA-inducible promoter led to stress-induced upregulation of ADC activity and
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