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Showing 1 to 20 of 21 for “"ATCase"”.

  1. Fluorescence Study of Aspartate Transcarbamylase (Atcase)

    Made available in DSpace on 2014-12-10T23:01:41Z (GMT). No. of bitstreams: 1 7411977.pdf: 2535470 bytes, checksum: 120bad7a4f835b974e087ffcad7f970a (MD5) Previous issue date: 1973

    uiuc Repository record for Fluorescence Study of Aspartate Transcarbamylase (Atcase) (opens in a new tab)

  2. Purification and Characterization of Proteolytic Aspartate Transcarbamoylase (ATCase) from Burkholderia cepacia 25416 and Construction of a pyrB1 Knock-out Mutant

    … patients. The pyrB gene encoding ATCase was cloned and ATCase was purified by the glutathione S-transferase gene fusion system. The ATCase in B. cepacia has been previously classified as a class A enzyme by Bethell and Jones. ATCase activity gels showed that B. cepacia contained a …

    unt Repository record for Purification and Characterization of Proteolytic Aspartate Transcarbamoylase (ATCase) from Burkholderia cepacia 25416 and Construction of a pyrB1 Knock-out Mutant (opens in a new tab)

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

    An aspartate transcarbamoylase (ATCase) gene from Bordetella pertussis was amplified by PCR and ligated into pT-ADV for expression in Escherichia coli. This particular ATCase (pyrB) was an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was …

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

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

    … (CPTase), 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 …

    greenwich

  5. 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)

  6. Degradation of Aspartate Transcarbamylase in Growing and Starved Bacillus Subtilis Cells

    Aspartate transcarbamylase (ATCase) is degraded upon starvation of Bacillus subtilis cells for carbon or nitrogen. The rate of ATCase degradation in exponentially growing B. subtilis cells was determined by measurement of enzyme activity after the addition of uridine to repress further enzyme …

    uiuc Repository record for Degradation of Aspartate Transcarbamylase in Growing and Starved Bacillus Subtilis Cells (opens in a new tab)

  7. Oxidative Inactivation of Bacillus Subtilis Aspartate Transcarbamylase in Vitro

    Aspartate transcarbamylase (ATCase) is stable in growing Bacillus subtilis cells, but it is rapidly and selectively inactivated in stationary cells. It has been demonstrated that the inactivation requires the continuous generation of metabolic energy, but not nucleic acid or protein synthesis. …

    uiuc Repository record for Oxidative Inactivation of Bacillus Subtilis Aspartate Transcarbamylase in Vitro (opens in a new tab)

  8. Characterization of Moraxella bovis Aspartate Transcarbamoylase

    Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious …

    unt Repository record for Characterization of Moraxella bovis Aspartate Transcarbamoylase (opens in a new tab)

  9. 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.

    … 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 showed that …

    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)

  10. BioInformatics, Phylogenetics, and Aspartate Transcarbamoylase

    … using the enzyme aspartate transcarbamoylase (ATCase) as the model enzyme. The first portion of this research focuses on the use of bioinformatics. A partial sequence of the pyrB gene found in Enterococcus faecalis was submitted to GenBank and was analyzed against the contiguous sequence from …

    unt Repository record for BioInformatics, Phylogenetics, and Aspartate Transcarbamoylase (opens in a new tab)

  11. Cassette Systems for Creating Intergeneric Hybrid ATCases

    Cassette systems for creating intergeneric hybrid ATCases were constructed. An MluI restriction enzyme site was introduced at the carbamoylphosphate binding site within the pyrB genes of both Pseudomonas putida and Escherichia coli. Two hybrids, E. coli pyrB polar domain fused with P. putida pyrB …

    unt Repository record for Cassette Systems for Creating Intergeneric Hybrid ATCases (opens in a new tab)

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

    … (DHOase) and aspartate transcarbamoylase (ATCase) of <em>Bacillus anthracis</em> (<em>B. anthracis</em>) were cloned for expression in <em>Escherichia coli</em> (<em>E. coli</em>). The proteins were purified by affinity chromatography and the enzymatic activity was determined by enzyme …

    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)

  13. Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis

    The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 …

    unt Repository record for Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis (opens in a new tab)

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

    … of the pathway, aspartate transcarbamoylase (ATCase), was created. Assays for pyrimidine intermediates, and virulence factors were performed. Results showed that the production of pigments, haemolysin, and rhamnolipids were significantly decreased from PAO1. Elastase and casein protease …

    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)

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

    … of Pseudomonas aspartate transcarbamoylase (ATCase), its allosteric regulation and how it is assembled. The E. coli ATCase is a dodecamer of two different polypeptides, encoded by pyrBI. Six regulatory (PyrI) and six catalytic (PyrB) polypeptides assemble from two preformed trimers (B3) and …

    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)

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

    … growth, including the production of two forms of ATCase in the late log phase in P. aeruginosa. This finding may be explained by the displacement of the inactive PyrC' by the active PyrC or PyrC2 to form a new and larger pyrBC encoded ATCase. Pseudomonas aeruginosa wild-type appears to produce by …

    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)

  17. A continuous spectrophotometric assay for phosphate releasing enzymes

    … reported continuous assay devised for measuring ATCase activity using the nucleoside analogue methylthioguanosine as the linking substrate. In contrast to MESG, m$\sp7$Ino is easily and inexpensively synthesized and is also commercially available. The spectrophotometric signal at 291 nm, produced …

    concordia Repository record for A continuous spectrophotometric assay for phosphate releasing enzymes (opens in a new tab)

  18. A Study of the Pyrimidine Biosynthesis Pathway and its Regulation in Two Distinct Organisms: Methanococcus jannaschii and Pseudomonas aeruginosa

    … genes encoding the aspartate transcarbamoylase (ATCase) catalytic (PyrB) and regulatory (PyrI) polypeptides were found. Unlike Escherichia coli where the above genes are expressed from a biscistronic operon the two genes in M. jannaschii are separated by 200-kb stretch of genome. Previous …

    unt Repository record for A Study of the Pyrimidine Biosynthesis Pathway and its Regulation in Two Distinct Organisms: Methanococcus jannaschii and Pseudomonas aeruginosa (opens in a new tab)

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