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Showing 1 to 11 of 11 for “"dihydroorotase"”.

  1. Untersuchungen zur pflanzlichen Pyrimidin de-novo Synthese : Bedeutung des Enzyms Dihydroorotase

    … von E.coli Knockout -Mutanten wurde das für Dihydroorotase kodierende Gen aus Solanum tuberosum und Arabidopsis thaliana kloniert. Beide Sequenzen kodieren für das in vivo funktionelle Protein. Im Falle der Kartoffel DHOase wurde durch RACE-PCR die vollst‰ndige untranslatierte 5'-Region …

    heid-diss Repository record for Untersuchungen zur pflanzlichen Pyrimidin de-novo Synthese : Bedeutung des Enzyms Dihydroorotase (opens in a new tab)

  2. Using peptides to examine the interaction interface between Aspartate transcarbamoylase and Dihydroorotase in pyrimidine biosynthesis in Aquifex aeolicus

    <p>Aspartate transcarbamoylase (ATCase) and Dihydroorotase (DHOase) catalyze the second and third steps, respectively, in <em>de novo</em> pyrimidine biosynthesis. Both enzymes form an active complex (DAC) in <em>Aquifex aeolicus</em>, where loop A of DHOase interacts with a domain of ATCase. The …

    emich Repository record for Using peptides to examine the interaction interface between Aspartate transcarbamoylase and Dihydroorotase in pyrimidine biosynthesis in Aquifex aeolicus (opens in a new tab)

  3. Characterizing the oligomeric structure and catalytic activity of the dihydroorotase and aspartate transcarbamoylase from the bacterium, <i>bacillus anthracis</i>

    … nucleotide biosynthesis for survival. The dihydroorotase domain is a key enzyme in pyrimidine biosynthesis and a promising drug target. The genes encoding the dihydroorotase (DHOase) and aspartate transcarbamoylase (ATCase) of <em>Bacillus anthracis</em> (<em>B. anthracis</em>) were cloned …

    emich Repository record for Characterizing the oligomeric structure and catalytic activity of the dihydroorotase and aspartate transcarbamoylase from the bacterium, <i>bacillus anthracis</i> (opens in a new tab)

  4. Studies on the regulation of pyrimidine nucleotide biosynthesis and its effect on ribonucleic acid accumulation during synchronous growth of Chlorella pyrenoidosa

    … levels of aspartate transcarbamylase and dihydroorotase, the first two enzymes on the pyrimidine nucleotide biosynthetic pathway during the cell cycle of this organism. When the apparent levels of these two enzymes were plotted on a relative increase basis, their rates of increase …

    vt Repository record for Studies on the regulation of pyrimidine nucleotide biosynthesis and its effect on ribonucleic acid accumulation during synchronous growth of Chlorella pyrenoidosa (opens in a new tab)

  5. Construction of a Pseudomonas aeruginosa Dihydroorotase Mutant and the Discovery of a Novel Link between Pyrimidine Biosynthetic Intermediates and the Ability to Produce Virulence Factors

    … auxotroph in the third step of the pathway, dihydroorotase (DHOase), failed to produce the siderophore pyoverdin. We created a PAO1 DHOase pyrimidine auxotroph to determine if this was also true for P. aeruginosa. Creation of this mutant was a two-step process, as P. aeruginosa has two pyrC …

    unt Repository record for Construction of a Pseudomonas aeruginosa Dihydroorotase Mutant and the Discovery of a Novel Link between Pyrimidine Biosynthetic Intermediates and the Ability to Produce Virulence Factors (opens in a new tab)

  6. Characterization of the Aspartate Transcarbamoylase that is Found in the pyrBC" Complex of Bordetella Pertussis

    … an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was undertaken to determine whether this pyrB gene was capable of expression alone or if it was capable of expression only when cotransformed with a functional pyrC'. When transformed into E. …

    unt Repository record for Characterization of the Aspartate Transcarbamoylase that is Found in the pyrBC" Complex of Bordetella Pertussis (opens in a new tab)

  7. Molecular properties of aspartate transcarbamoylase and related enaymes from wheat

    … aspartate transcarbamoylase (ATCase) and dihydroorotase (DHOase), in various organisms have been reviewed. The molecular organisation of these three enzymes has been investigated in wheat using gel filtration chromatography. CPSase activity could not be detected in gel filtered extracts …

    greenwich

  8. Characterization of the regulatory domain of the mammalian multifunctional De Novo pyrimidne biosynthetic enzyme CAD

    … aspartate transcarbamoylase (ATCase), and dihydroorotase (DHOase) are carried on a single 240-kDa polypeptide chain called CAD. Carbamoyl phosphate synthetase (CPSase), the first enzyme in the pathway catalyzes the synthesis of carbamoyl phosphate from two moles of ATP, bicarbonate, and …

    wayne-thes Repository record for Characterization of the regulatory domain of the mammalian multifunctional De Novo pyrimidne biosynthetic enzyme CAD (opens in a new tab)

  9. Structure-Function Studies on Aspartate Transcarbamoylase and Regulation of Pyrimidine Biosynthesis by a Positive Activator Protein, PyrR in Pseudomonas putida

    … of structure 2B3:3C'2. pyrC' encodes an inactive dihydroorotase with pyrB and pyrC' overlapping by 4 bp. Chapter III explores how catabolite repression affects pyrimidine metabolism. The global catabolite repression control protein, Crc, has been shown to affect pyrimidine metabolism in a number …

    unt Repository record for Structure-Function Studies on Aspartate Transcarbamoylase and Regulation of Pyrimidine Biosynthesis by a Positive Activator Protein, PyrR in Pseudomonas putida (opens in a new tab)

  10. Comparative biochemistry and genetic analysis of nucleoside hydrolase in Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas fluorescens.

    The pyrimidine salvage enzyme, nucleoside hydrolase, is catalyzes the irreversible hydrolysis of nucleosides into the free nucleic acid base and D-ribose. Nucleoside hydrolases have varying degrees of specificity towards purine and pyrimidine nucleosides. In E. coli, three genes were found that …

    unt Repository record for Comparative biochemistry and genetic analysis of nucleoside hydrolase in Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas fluorescens. (opens in a new tab)