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Showing 1 to 8 of 8 for “"pyrimidine pathway"”.

  1. Impaired virulence factor production in a dihydroorotate dehydrogenase mutant (pyrD) of Pseudomonas aeruginosa.

    … were created in the pyrB and pyrC genes of the pyrimidine pathway in Pseudomonas aeruginosa, not only were the resultant mutants auxotrophic for pyrimidines but they were also impaired in virulence factor production. Such a correlation had not been previously reported for P. aeruginosa, a …

    unt Repository record for Impaired virulence factor production in a dihydroorotate dehydrogenase mutant (pyrD) of Pseudomonas aeruginosa. (opens in a new tab)

  2. Isolation of a Pseudomonas aeruginosa Aspartate Transcarbamoylase Mutant and the Investigation of Its Growth Characteristics, Pyrimidine Biosynthetic Enzyme Activities, and Virulence Factor Production

    The pyrimidine biosynthetic pathway is an essential pathway for most organisms. Previous research on the pyrimidine pathway in Pseudomonas aeruginosa (PAO1) has shown that a block in the third step of the pathway resulted in both a requirement for exogenous pyrimidines and decreased ability to …

    unt Repository record for Isolation of a Pseudomonas aeruginosa Aspartate Transcarbamoylase Mutant and the Investigation of Its Growth Characteristics, Pyrimidine Biosynthetic Enzyme Activities, and Virulence Factor Production (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>

    … 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 for expression in <em>Escherichia …

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

    Pyrimidine nucleotides play a central role in cellular regulation. Most cells have two pathways to fulfill their pyrimidine nucleotide pools: the de novo and the salvage pathway. The de novo pyrimidine pathway begins with glutamine, ATP and bicarbonate, and through six-enzymatic steps yields …

    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)

  5. Identification and Characterization of Drug Targets in the Pyrimidine and Purine Pathways of Trypanosoma brucei

    … characterize novel drug targets in the parasite pyrimidine and purine pathways. The pyrimidine de novo biosynthetic pathway has been well characterized, however little work had been done to evaluate the importance of pyrimidine salvage enzymes. Specifically, my research validates the essentiality …

    utswmed Repository record for Identification and Characterization of Drug Targets in the Pyrimidine and Purine Pathways of Trypanosoma brucei (opens in a new tab)

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

    The regulation of pyrimidine biosynthesis was studied in Pseudomonas putida. The biosynthetic and salvage pathways provide pyrimidine nucleotides for RNA, DNA, cell membrane and cell wall biosynthesis. Pyrimidine metabolism is intensely studied because many of its enzymes are targets for …

    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)

  7. Effector Response of the Aspartate Transcarbamoylase From Wild Type Pseudomonas Putida and a Mutant with 11 Amino Acids Deleted at the N-terminus of PyrB.

    Like its enteric counterpart, aspartate transcarbamoylase (ATCase) from Pseudomonas putida is a dodecamer of two different polypeptides. Unlike the enterics, the Pseudomonas ATCase lacks regulatory polypeptides but employs instead inactive dihydroorotases for an active dodecamer. Previous work …

    unt Repository record for Effector Response of the Aspartate Transcarbamoylase From Wild Type Pseudomonas Putida and a Mutant with 11 Amino Acids Deleted at the N-terminus of PyrB. (opens in a new tab)

  8. Pyrimidine Enzyme Specific Activity at Four Different Phases of Growth in Minimal and Rich Media, and Concomitant Virulence Factors Evaluation in Pseudomonas aeruginosa

    … is the first comprehensive report of the pyrimidine biosynthetic pathway for all phases of growth in minimal and rich media coupled with the evaluation of virulence factor production of P. aeruginosa in comparison to four other bacterial species (Pseudomonas putida, Pseudomonas …

    unt Repository record for Pyrimidine Enzyme Specific Activity at Four Different Phases of Growth in Minimal and Rich Media, and Concomitant Virulence Factors Evaluation in Pseudomonas aeruginosa (opens in a new tab)