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decarboxylase/acker schmalwand
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Structural roles of cysteine 50 and cysteine 230 residues in Arabidopsis thaliana S-adenosylmethionine decarboxylase.
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The Arabidopsis thaliana S-Adenosylmethionine decarboxylase (AdoMetDC) cDNA (GenBank U63633) was cloned. Site-specific mutagenesis was performed to introduce mutations at the conserved cysteine Cys(50), Cys(83), and Cys(230), and lys(81) residues. In accordance with the human AdoMetDC, the C50A and
Identification of functionally important residues of Arabidopsis thaliana S-adenosylmethionine decarboxylase.
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The Arabidopsis thaliana S-adenosylmethionine decarboxylase (AdoMetDC) cDNA (GenBank(TM) U63633) was cloned, and the AdoMetDC protein was expressed, purified, and characterized. The K(m) value for S-adenosylmethionine (AdoMet) is 23.1 microM and the K(i) value for methylglyoxal bis-(guanylhydrazone)
Role of Arginine decarboxylase (ADC) in Arabidopsis thaliana defence against the pathogenic bacterium Pseudomonas viridiflava.
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Polyamine biosynthesis starts with putrescine production through the decarboxylation of arginine or ornithine. In Arabidopsis thaliana, putrescine is synthesised exclusively by arginine decarboxylase (ADC), which exists as two isoforms (ADC1 and 2) that are differentially regulated by abiotic
The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana.
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Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate-biosynthetic pathway leading to S-lysine: the decarboxylation of meso-diaminopimelate to form S-lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of
Mutants of the cruciferous plant Arabidopsis thaliana lacking glycine decarboxylase activity.
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A mutant of Arabidopsis thaliana (L.) Heyn. (a small plant in the crucifer family) that lacks glycine decarboxylase activity owing to a recessive nuclear mutation has been isolated on the basis of a growth requirement for high concentrations of atmospheric CO2. Mitochondria isolated from leaves of
Regulation of Arabidopsis thaliana (L.) Heynh Arginine decarboxylase by potassium deficiency stress.
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Arginine decarboxylase (ARGdc) is the first enzyme in one of the two pathways to putrescine in plants. ARGdc enzyme activity has been shown to be induced by many environmental factors, including potassium deficiency stress. We investigated the mechanism for induction of ARGdc activity during
Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase.
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Sequence comparison with the mevalonate diphosphate decarboxylase (MVD) amino acid sequence of Saccharomyces cerevisiae identified an EST clone corresponding to a cDNA that may encode Arabidopsis thaliana MVD (AtMVD1). This enzyme catalyses the synthesis of isopentenyl diphosphate, the building
Molecular and enzymatic characterizations of novel bifunctional 3beta-hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis thaliana.
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We have isolated two cDNAs from Arabidopsis thaliana encoding bifunctional 3beta-hydroxysteroid dehydrogenase/C-4 decarboxylases (3betaHSD/D) involved in sterol synthesis, termed At3betaHSD/D1 and At3betaHSD/D2. Transformation of the yeast ergosterol auxotroph erg26 mutant, which lacks 3betaHSD/D
Hetero- and homodimerization of Arabidopsis thaliana arginine decarboxylase AtADC1 and AtADC2.
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The arginine decarboxylase enzyme (ADC) carries out the production of agmatine from arginine, which is the precursor of the first polyamine (PA) known as putrescine; subsequently, putrescine is turned into the higher PAs, spermidine and spermine. In Arabidopsis thaliana PA production occurs only
Effect of reduced arginine decarboxylase activity on salt tolerance and on polyamine formation during salt stress in Arabidopsis thaliana.
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Polyamines have been suggested to play an important role in stress protection. However, attempts to determine the function of polyamines have been complicated by the fact that, dependent on the conditions, polyamine contents increase or decrease during stress. To determine the importance of
Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana.
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Full-length tyrosine decarboxylase cDNA (TyrDC) from Arabidopsis thaliana was identified by rapid amplification of cDNA ends-PCR and isolated by RT-PCR. The TyrDC mRNA was substantially induced by drought stress and wounding, and was considerably decreased by salt stress. By using TyrDC protein
Overexpression of Actinidia deliciosa pyruvate decarboxylase 1 gene enhances waterlogging stress in transgenic Arabidopsis thaliana.
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Ethanolic fermentation is classically associated with waterlogging tolerance when plant cells switch from respiration to anaerobic fermentation. Pyruvate decarboxylase (PDC), which catalyzes the first step in this pathway, is thought to be the main regulatory enzyme. Here, we cloned a full-length
Molecular characterization of the Arabidopsis thaliana flavoprotein AtHAL3a reveals the general reaction mechanism of 4'-phosphopantothenoylcysteine decarboxylases.
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The Arabidopsis thaliana flavoprotein AtHAL3a, which is linked to plant growth and salt and osmotic tolerance, catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in coenzyme A biosynthesis. AtHAL3a is similar in sequence and structure to the LanD
Arginine decarboxylase (polyamine synthesis) mutants of Arabidopsis thaliana exhibit altered root growth.
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Putrescine and polyamines are produced by two alternative pathways in plants. One pathway starts with the enzyme arginine decarboxylase; the other with ornithine decarboxylase. The authors developed an in vivo screening strategy to identify mutants with low levels of arginine decarboxylase activity.
Analysis of the role of the pyruvate decarboxylase gene family in Arabidopsis thaliana under low-oxygen conditions.
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Plants under low-oxygen conditions adapt their metabolism by inducing the fermentative pathway, with ethanol as the predominant end product. Activities of pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required for this pathway. While a single gene encodes ADH in Arabidopsis, a
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