Relevant bibliographies by topics / Pyrimidine nucleotides

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Academic literature on the topic 'Pyrimidine nucleotides'

Author: Grafiati
Published: 4 June 2021
Last updated: 21 February 2023

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Journal articles on the topic "Pyrimidine nucleotides"

1

Tomlinson, Patricia Tolson, and Carol J. Lovatt. "Nucleotide Metabolism in ‘Washington’ Navel Orange Fruit: I. Pathways of Synthesis and Catabolism." Journal of the American Society for Horticultural Science 112, no. 3 (May 1987): 529–35. http://dx.doi.org/10.21273/jashs.112.3.529.

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Abstract The capacity of ‘Washington’ navel orange fruit [Citrus sinensis (L.) Osbeck] to synthesize and catabolize purines and pyrimidines was assessed. De novo biosynthesis of purine nucleotide was demonstrated by [14C] bicarbonate incorporation into purine nucleotides, blockage of this process by four known inhibitors, and assimilation of radiolabeled carbon from formate, both carbons of glycine, and carbon-3 of serine into the adenine ring. De novo synthesis of pyrimidines via the orotate pathway in young fruit was demonstrated by incorporation of [14C] bicarbonate and [6-14C]orotic acid into uridine nucleotides, release of 14CO2 from [7-14C]orotic acid, and blockage of these processes by 6-azauridine. Synthesis of purine and pyrimidine nucleotides via salvage reactions was demonstrated by incorporation of radiolabeled bases and ribonucleosides into nucleotides and into nucleic acids. Release of 14CO2 from radiolabeled adenine, adenosine, hypoxanthine, and xanthine, uric acid, urea (purines), uracil, and uridine (pyrimidines) provided evidence the pathways for catabolism (degradation) of purines and pyrimidines in navel orange fruit are similar to those found in microorganisms and animal tissues. To the best of our knowledge, this report is the first to assess the capacity of anabolic and catabolic pathways of purine and pyrimidine nucleotide metabolism in fruit of any species. De novo synthetic activities in orange fruit permit increases in the pools of purine and pyrimidine nucleotides using simple precursors. Further, the patterns of salvage and catabolism suggest riboside pools are reused predominantly as nucleotides, while the majority of base pools are degraded to permit recycling of carbon and nitrogen into other metabolites.
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Weetall, Marla, Kensuke Kojima, Sujan Piya, Christopher Trotta, John Baird, Kylie O'Keefe, Bansri Furia, Gautam M. Borthakur, and Robert Spiegel. "Inhibition of De Novo Pyrimidine Nucleotide Synthesis By the Novel DHODH Inhibitor PTC299 Induces Differentiation and/or Death of AML Cells." Blood 134, Supplement_1 (November 13, 2019): 5152. http://dx.doi.org/10.1182/blood-2019-124569.

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Background: Pyrimidine nucleotides are generated either by de novo synthesis or the salvage pathway in which pyrimidine nucleotides are obtained from the diet. Resting cells typically acquire adequate pyrimidine nucleotides from the salvage pathway. Rapidly proliferating cells, however, are dependent on the de novo synthesis of pyrimidine nucleotides. PTC299 is an inhibitor of dihydroorotate dehydrogenase (DHODH), a rate limiting enzyme for de novo pyrimidine nucleotide synthesis that had previously been in clinical trials for treatment of solid tumors. Results: Using 15N-labelled glutamine, we show that PTC299 reduces de novo pyrimidine nucleotide synthesis in PTC299-sensitive AML cell lines resulting in a depletion of total pyrimidine nucleotides. In parallel to reduction in pyrimidine nucleotides, PTC 299 leads to accumulation of DHO, the substrate of DHODH and unexpectedly, an accumulation of N-carbamoyl aspartate the metabolite above DHO in the de novo pyrimidine nucleotide synthesis pathway. PTC299 was broadly active against leukemia and lymphoma lines, with 80% of the AML lines tested showing sensitivity. Treatment of AML cell lines with PTC299 induced differentiation as shown by increased CD14 and/or reduced proliferation. Using isogenic AML lines, we show that PTC299 reduces the proliferation of both p53 wildtype and p53 deficient leukemia calls with similar potency as measured by the concentration of PTC299 required to reduce cell number by 50% (CC50). In cells expressing wildtype p53, PTC299 increases p53 activation. However, p53- wildtype cells undergo increased apoptosis whereas p53-deficience cells undergo necrosis. PTC299 induced a G1/S cell cycle arrest, also independent of p53 status. PTC299 increased H2A.X (a marker of double stranded DNA breaks) in both p53 wildtype and p53 deficient cells. These data suggest that the depletion of nucleotides results in stalling at the replication fork, and subsequent DNA-breaks. Conclusion: De novo pyrimidine nucleotide synthesis is critical for AML survival and proliferation. Depletion of nucleotides results in reduced proliferation, triggering either differentiation and/or cell death. Disclosures Weetall: PTC Therapeutics: Employment. Trotta:PTC Therapeutics: Employment. Baird:PTC Therapeutics: Employment. O'Keefe:PTC Therapeutics: Employment. Furia:PTC Therapeutics: Employment. Borthakur:PTC Therapeutics: Consultancy; Janssen: Research Funding; AbbVie: Research Funding; Argenx: Membership on an entity's Board of Directors or advisory committees; NKarta: Consultancy; AstraZeneca: Research Funding; Xbiotech USA: Research Funding; Incyte: Research Funding; GSK: Research Funding; Oncoceutics, Inc.: Research Funding; Novartis: Research Funding; Agensys: Research Funding; BMS: Research Funding; Oncoceutics: Research Funding; Cantargia AB: Research Funding; Bayer Healthcare AG: Research Funding; Eisai: Research Funding; FTC Therapeutics: Membership on an entity's Board of Directors or advisory committees; BioTheryX: Membership on an entity's Board of Directors or advisory committees; Polaris: Research Funding; Merck: Research Funding; Cyclacel: Research Funding; Eli Lilly and Co.: Research Funding; BioLine Rx: Consultancy, Membership on an entity's Board of Directors or advisory committees, Research Funding; Arvinas: Research Funding; Tetralogic Pharmaceuticals: Research Funding; Strategia Therapeutics: Research Funding. Spiegel:PTC Therapeutics: Consultancy.
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Li, Wentao, Ogun Adebali, Yanyan Yang, Christopher P. Selby, and Aziz Sancar. "Single-nucleotide resolution dynamic repair maps of UV damage in Saccharomyces cerevisiae genome." Proceedings of the National Academy of Sciences 115, no. 15 (March 26, 2018): E3408—E3415. http://dx.doi.org/10.1073/pnas.1801687115.

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We have adapted the eXcision Repair-sequencing (XR-seq) method to generate single-nucleotide resolution dynamic repair maps of UV-induced cyclobutane pyrimidine dimers and (6-4) pyrimidine–pyrimidone photoproducts in the Saccharomyces cerevisiae genome. We find that these photoproducts are removed from the genome primarily by incisions 13–18 nucleotides 5′ and 6–7 nucleotides 3′ to the UV damage that generate 21- to 27-nt-long excision products. Analyses of the excision repair kinetics both in single genes and at the genome-wide level reveal strong transcription-coupled repair of the transcribed strand at early time points followed by predominantly nontranscribed strand repair at later stages. We have also characterized the excision repair level as a function of the transcription level. The availability of high-resolution and dynamic repair maps should aid in future repair and mutagenesis studies in this model organism.
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Satterwhite, Christina M., Angela M. Farrelly, and Michael E. Bradley. "Chemotactic, mitogenic, and angiogenic actions of UTP on vascular endothelial cells." American Journal of Physiology-Heart and Circulatory Physiology 276, no. 3 (March 1, 1999): H1091—H1097. http://dx.doi.org/10.1152/ajpheart.1999.276.3.h1091.

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Endothelial cells express receptors for ATP and UTP, and both UTP and ATP elicit endothelial release of vasoactive compounds such as prostacyclin and nitric oxide; however, the distinction between purine and pyrimidine nucleotide signaling is not known. We hypothesized that UTP plays a more important role in endothelial mitogenesis and chemotaxis than does ATP and that UTP is angiogenic. In cultured endothelial cells from guinea pig cardiac vasculature (CEC), both UTP and vascular endothelial growth factor (VEGF) were significant mitogenic and chemotactic factors; in contrast, ATP demonstrated no significant chemotaxis in CEC. In chick chorioallantoic membranes (CAM), UTP and VEGF treatments produced statistically significant increases in CAM vascularity compared with controls. These findings are the first evidence of chemotactic or angiogenic effects of pyrimidines; they suggest a role for pyrimidine nucleotides that is distinct from those assumed by purine nucleotides and provide for the possibility that UTP serves as an extracellular signal for processes such as endothelial repair and angiogenesis.
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Tomlinson, Patricia Tolson, and Carol J. Lovatt. "Nucleotide Metabolism in ‘Washington’ Navel Orange Fruit: II. Pathway Capacities During Development." Journal of the American Society for Horticultural Science 112, no. 3 (May 1987): 535–39. http://dx.doi.org/10.21273/jashs.112.3.535.

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Abstract Changes in the capacity of ‘Washington’ navel orange [Citrus sinensis (L.) Osbeck] fruit to synthesize (de novo or by salvage) pyrimidine nucleotides, but not purine nucleotides, appears to be related to the stage of fruit development. De novo pyrimidine synthesis in whole-fruit tissue increased 6-fold during Stage I of development (cell division phase), from 10 nmol [14C]bicarbonate incorporated into uridine nucleotides during 5 hr per g dry weight whole-fruit tissue from ovaries harvested at flower petal drop to 57 nmol for 2-month-old fruit. Capacity of peel tissue to synthesize pyrimidine nucleotides de novo decreased following completion of Stage I, from 43 nmol [14C]bicarbonate incorporated into uridine nucleotides during 5 hr per g dry weight of peel tissue from 2-month-old fruit to 11 nmol for 5-month-old (Stage II) fruit. This decrease was not offset by increased salvage of uridine. Capacity of whole-fruit tissue to synthesize purines de novo increased 3-fold during Stage I. Synthetic capacity of peel tissue from Stage I fruit was half that observed for whole-fruit tissue and did not decrease significantly during Stages II (cell enlargement phase) and III (maturation phase). These observations suggest purine synthetic capacity may not be related to stage of development. Changes in protein or glucose contents, or respiratory activity of peel tissue, could not account for the observed reduction in pyrimidine synthetic capacity. Thus, the reduction observed in synthetic activity was specific for pyrimidine nucleotides. The capacity of fast-growing, 1-month-old fruit (high potential to set) to synthesize or catabolize either pyrimidine or purine nucleotides did not differ from that of slow-growing fruit (low potential to set), suggesting that nucleotide synthesis is not limiting to growth.
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Szondy, Z., and E. A. Newsholme. "The effect of glutamine concentration on the activity of carbamoyl-phosphate synthase II and on the incorporation of [3H]thymidine into DNA in rat mesenteric lymphocytes stimulated by phytohaemagglutinin." Biochemical Journal 261, no. 3 (August 1, 1989): 979–83. http://dx.doi.org/10.1042/bj2610979.

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The maximum catalytic activities of carbamoyl-phosphate synthase II, a limiting enzyme for pyrimidine nucleotide synthesis, are very much less than those of glutaminase, a limiting enzyme for glutamine utilization, in lymphocytes and macrophages; and the flux through the pathway for pyrimidine formation de novo is only about 0.4% of the rate of glutamine utilization by lymphocytes. The Km of synthase II for glutamine is about 16 microM and the concentration of glutamine necessary to stimulate lymphocyte proliferation half-maximally is about 21 microM. This agreement suggests that the importance of glutamine for these cells is provision of nitrogen for biosynthesis of pyrimidine nucleotides (and probably purine nucleotides). However, the glutamine concentration necessary for half-maximal stimulation of glutamine utilization (glutaminolysis) by the lymphocytes is 2.5 mM. The fact that the rate of glutamine utilization by lymphocytes is markedly in excess of the rate of the pathway for pyrimidine nucleotide synthesis de novo and that the Km and ‘half-maximal concentration’ values are so different, suggests that the glutaminolytic pathway is independent of the use of glutamine nitrogen for pyrimidine synthesis.
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Amici, Adolfo, Monica Emanuelli, Giulio Magni, Nadia Raffaelli, and Silverio Ruggieri. "Pyrimidine nucleotidases from human erythrocyte possess phosphotransferase activities specific for pyrimidine nucleotides." FEBS Letters 419, no. 2-3 (December 15, 1997): 263–67. http://dx.doi.org/10.1016/s0014-5793(97)01464-6.

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Bhat, B. M., H. A. Brady, and W. S. Wold. "Virus deletion mutants that affect a 3' splice site in the E3 transcription unit of adenovirus 2." Molecular and Cellular Biology 5, no. 9 (September 1985): 2405–13. http://dx.doi.org/10.1128/mcb.5.9.2405-2413.1985.

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Five viable virus mutants were constructed with deletions near a 3' splice site located at nucleotide 2157 in the E3 transcription unit of adenovirus 2. The mutants were examined for splicing activity at the 2157 3' splice site in vivo by nuclease-gel analysis of steady-state cytoplasmic mRNA. Splicing was not prevented by an exon deletion (dl719) that leaves 16 5'-proximal exon nucleotides intact or by intron deletions that leave 34 (dl717, dl712) or 18 (dl716) 3'-proximal intron nucleotides intact. The sequences deleted in one of these intron mutants (dl716) include the putative branchpoint site used in lariat formation during splicing. Thus, a surrogate branchpoint site apparently can be used for splicing. Another intron mutant (dl714) has a deletion that leaves 15 3'-proximal intron nucleotides intact; remarkably, this deletion virtually abolished splicing, even though the deletion is only 3 nucleotides closer to the splice site than is the deletion in dl716 which splices normally. The three nucleotides deleted in dl714 that are retained by dl716 are the sequence TGT. The TGT sequence is located on the 5' boundary of the pyrimidine-rich region upstream of the nucleotide 2157 3' splice site. Such pyrimidine-rich regions are ubiquitous at 3' splice sites. Most likely, the TGT is required for splicing at the nucleotide 2157 3' splice site. The TGT may be important because of its specific sequence or because it forms the 5' boundary of the pyrimidine-rich region.
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Bhat, B. M., H. A. Brady, and W. S. Wold. "Virus deletion mutants that affect a 3' splice site in the E3 transcription unit of adenovirus 2." Molecular and Cellular Biology 5, no. 9 (September 1985): 2405–13. http://dx.doi.org/10.1128/mcb.5.9.2405.

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Five viable virus mutants were constructed with deletions near a 3' splice site located at nucleotide 2157 in the E3 transcription unit of adenovirus 2. The mutants were examined for splicing activity at the 2157 3' splice site in vivo by nuclease-gel analysis of steady-state cytoplasmic mRNA. Splicing was not prevented by an exon deletion (dl719) that leaves 16 5'-proximal exon nucleotides intact or by intron deletions that leave 34 (dl717, dl712) or 18 (dl716) 3'-proximal intron nucleotides intact. The sequences deleted in one of these intron mutants (dl716) include the putative branchpoint site used in lariat formation during splicing. Thus, a surrogate branchpoint site apparently can be used for splicing. Another intron mutant (dl714) has a deletion that leaves 15 3'-proximal intron nucleotides intact; remarkably, this deletion virtually abolished splicing, even though the deletion is only 3 nucleotides closer to the splice site than is the deletion in dl716 which splices normally. The three nucleotides deleted in dl714 that are retained by dl716 are the sequence TGT. The TGT sequence is located on the 5' boundary of the pyrimidine-rich region upstream of the nucleotide 2157 3' splice site. Such pyrimidine-rich regions are ubiquitous at 3' splice sites. Most likely, the TGT is required for splicing at the nucleotide 2157 3' splice site. The TGT may be important because of its specific sequence or because it forms the 5' boundary of the pyrimidine-rich region.
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Froschauer, Elisabeth M., Nicole Rietzschel, Melanie R. Hassler, Markus Binder, Rudolf J. Schweyen, Roland Lill, Ulrich Mühlenhoff, and Gerlinde Wiesenberger. "The mitochondrial carrier Rim2 co-imports pyrimidine nucleotides and iron." Biochemical Journal 455, no. 1 (September 13, 2013): 57–65. http://dx.doi.org/10.1042/bj20130144.

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Mitochondrial iron uptake is of key importance both for organelle function and cellular iron homoeostasis. The mitochondrial carrier family members Mrs3 and Mrs4 (homologues of vertebrate mitoferrin) function in organellar iron supply, yet other low efficiency transporters may exist. In Saccharomyces cerevisiae, overexpression of RIM2 (MRS12) encoding a mitochondrial pyrimidine nucleotide transporter can overcome the iron-related phenotypes of strains lacking both MRS3 and MRS4. In the present study we show by in vitro transport studies that Rim2 mediates the transport of iron and other divalent metal ions across the mitochondrial inner membrane in a pyrimidine nucleotide-dependent fashion. Mutations in the proposed substrate-binding site of Rim2 prevent both pyrimidine nucleotide and divalent ion transport. These results document that Rim2 catalyses the co-import of pyrimidine nucleotides and divalent metal ions including ferrous iron. The deletion of RIM2 alone has no significant effect on mitochondrial iron supply, Fe–S protein maturation and haem synthesis. However, RIM2 deletion in mrs3/4Δ cells aggravates their Fe–S protein maturation defect. We conclude that under normal physiological conditions Rim2 does not play a significant role in mitochondrial iron acquisition, yet, in the absence of the main iron transporters Mrs3 and Mrs4, this carrier can supply the mitochondrial matrix with iron in a pyrimidine-nucleotide-dependent fashion.
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Dissertations / Theses on the topic "Pyrimidine nucleotides"

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Eguae, Samuel Iyamu. "Pyrimidine nucleotide metabolism in Rhizobium meliloti: purification of aspartate transcarbamoylase from a pyrimidine auxotroph." Thesis, University of North Texas, 1990. https://digital.library.unt.edu/ark:/67531/metadc332674/.

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Rhizobium aspartate transcarbamoylase (ATCase; EC 2.1.3.2) was previously believed to be similar to the Pseudomonas ATCase which has been studied extensively. To facilitate the study of the Rhizobium ATCase a pyrimidine-requiring mutant of R. meliloti was isolated and used in the purification of the enzyme.
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Stewart, John E. B. (John Edward Bakos). "Characterization of Aspartate Transcarbamoylase in the Archaebacterium Methanococcus Jannaschii." Thesis, University of North Texas, 1996. https://digital.library.unt.edu/ark:/67531/metadc935724/.

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Asparate transcarbamoylase catalyzes the first committed step in the de novo synthesis of pyrmidine nucleotides UMP, UDP, UTP, and CTP. The archetype enzyme found in Escherichia coli (310 kDa) exhibits sigmodial substrate binding kinetics with positive control by ATP and negative control with CTP and UTP. The ATCase characterized in this study is from the extreme thermophilic Archaebacterium, Methanococcus jannaschii. The enzyme was very stable at elevated temperatures and possessed activity from 20 degrees Celsius to 90 degrees Celsius. M. Jannaschii ATCase retained 75% of its activity after incubation at 100 degrees Celsius for a period of 90 minutes. No sigmodial allosteric response to substrate for the enzyme was observed. Velocity substrate plots gave Michaelis-Menten (hyperbolic) kinetics. The Km for aspartate was 7 mM at 30 degrees Celsius and the KM for carbamoylphosphate was .125 mM. The enzyme from M. jannaschii had a broad pH response with an optimum above pH 9. Kinetic measurements were significantly affected by changes in pH and temperature. The enzyme catalyzed reaction had an energy of activation of 10,300 calories per mole. ATCase from M. jannaschii was partially purified. The enzyme was shown to have a molecular weight of 110,000 Da., with a subunit molecular weight of 37,000 Da. The enzyme was thus a trimer composed of three identical subunits. The enzyme did not possess any regulatory response and no evidence for a regulatory polypeptide was found, DNA from M. jannaschii did hybridize to probes corresponding to genes for both the catalytic and regulatory subunits from E. coli. Analysis of DNA sequences for the M. jannaschii ATCase genes showed that the gene for the catalytic subunits shares significant homology with the pyrB genes from E. coli, and maximum homology amongst known ATCase genes to pyrB from Bacillus. An unlinked gene homologous to E. coli pyrl encoding the regulatory subunit was identified, though its expression and true function remain uncharacterized.
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So, Ngar-chung Nellie. "Pyrimidine nucleotide biosynthesis in adult angiostrongylus Cantonensis (Nematoda : Metastrongyloidea) /." [Hong Kong : University of Hong Kong], 1993. http://sunzi.lib.hku.hk/hkuto/record.jsp?B13637745.

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蘇雅頌 and Ngar-chung Nellie So. "Pyrimidine nucleotide biosynthesis in adult angiostrongylus Cantonensis (Nematoda : Metastrongyloidea)." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1993. http://hub.hku.hk/bib/B3123320X.

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Brichta, Dayna Michelle. "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." Thesis, University of North Texas, 2003. https://digital.library.unt.edu/ark:/67531/metadc4344/.

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The ability to synthesize pyrimidine nucleotides is essential for most organisms. Pyrimidines are required for RNA and DNA synthesis, as well as cell wall synthesis and the metabolism of certain carbohydrates. Recent findings, however, indicate that the pyrimidine biosynthetic pathway and its intermediates maybe more important for bacterial metabolism than originally thought. Maksimova et al., 1994, reported that a P. putida M, pyrimidine 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 genes (pyrC and pyrC2), both of which encode active DHOase enzymes. The pyrC gene was inactivated by gene replacement with a truncated form of the gene. Next, the pyrC2 gene was insertionally inactivated with the aacC1 gentamicin resistance gene, isolated from pCGMW. The resulting pyrimidine auxotroph produced significantly less pyoverdin than did the wild type. In addition, the mutant produced 40% less of the phenazine antibiotic, pyocyanin, than did the wild type. As both of these compounds have been reported to be vital to the virulence response of P. aeruginosa, we decided to test the ability of the DHOase mutant strain to produce other virulence factors as well. Here we report that a block in the conversion of carbamoyl aspartate (CAA) to dihydroorotate significantly impairs the ability of P. aeruginosa to affect virulence. We believe that the accumulation of CAA in the cell is the root cause of this observed defect. This research demonstrates a potential role for pyrimidine intermediates in the virulence response of P. aeruginosa and may lead to novel targets for chemotherapy against P. aeruginosa infections.
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Entezampour, Mohammad. "Characterization of pyrimidine biosynthesis in Acinetobacter calcoaceticus using wild type and mutant strains." Thesis, University of North Texas, 1992. https://digital.library.unt.edu/ark:/67531/metadc798038/.

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Pyrimidine nucleotide biosynthesis was studies in Acinetobacter calcoaceticus ADP-1. Pyrimidine auxotrophic mutants were isolated and characterized for this purpose. One such Pyr mutant, strain ADP-1-218 was chosen for further study.
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Vickrey, John F. (John Fredrick) 1959. "Isolation and Characterization of the Operon Containing Aspartate Transcarbamoylase and Dihydroorotase from Pseudomonas aeruginosa." Thesis, University of North Texas, 1993. https://digital.library.unt.edu/ark:/67531/metadc278859/.

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The Pseudomonas aeruginosa ATCase was cloned and sequenced to determine the correct size, subunit composition and architecture of this pivotal enzyme in pyrimidine biosynthesis. During the course of this work, it was determined that the ATCase of Pseudomonas was not 360,000 Da but rather present in a complex of 484,000 Da consisting of two different polypeptides (36,000 Da and 44,000 Da) with an architecture similar to that of E. coli ATCase, 2(C3):3(r2). However, there was no regulatory polypeptide found in the Pseudomonas ATCase.
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AsFour, Hani. "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." Thesis, University of North Texas, 2002. https://digital.library.unt.edu/ark:/67531/metadc3163/.

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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 showed that PyrB contains not only the active site but also the effector binding sites for ATP, UTP and CTP at its N-terminus. In this work, 11 amino acids were deleted from the N-terminus of PyrB and the ATCase with the truncated protein was expressed in E. coli pyrB- and purified. The wild type enzyme was similarly treated. Velocity-substrate plots without effectors gave Michaelis-Menten kinetics in all cases. Deleting 11 amino acids did not affect dodecameric assembly but altered effector responses. When carbamoylphosphate was varied, the mutant enzyme was inhibited by UTP while the wild type enzyme was activated 2-fold. When the aspartate was varied, CTP had no effect on the mutant enzyme but strongly inhibited the wild type enzyme.
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Kumar, Alan P. "Structure-Function Studies on Aspartate Transcarbamoylase and Regulation of Pyrimidine Biosynthesis by a Positive Activator Protein, PyrR in Pseudomonas putida." Thesis, University of North Texas, 2003. https://digital.library.unt.edu/ark:/67531/metadc4362/.

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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 chemotheraphy. Four aspects of pyrimidine regulation are described in this dissertation. Chapter I compares the salvage pathways of Escherichia coli and P. putida. Surprisingly, P. putida lacks several salvage enzymes including nucleoside kinases, uridine phosphorylase and cytidine deaminase. Without a functional nucleoside kinase, it was impossible to feed exogenous uridine to P. putida. To obviate this problem, uridine kinase was transferred to P. putida from E. coli and shown to function in this heterologous host. Chapter II details the enzymology 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 three preformed regulatory dimers (I2) in the conserved 2B3:3I2 molecular structure. The Pseudomonas ATCase also assembles from two different polypeptides encoded by pyrBC'. However, a PyrB polypeptide combines with a PyrC. polypeptide to form a PyrB:PyrC. protomer; six of these assemble into a dodecamer 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 of ways. This includes orotate transport for use as pyrimidine, carbon and nitrogen sources. Orotate is important because it interacts with PyrR in repressing the pyr genes. Chapter IV describes PyrR, the positive activator of the pyrimidine pathway. As with other positive activator proteins, when pyrimidine nucleotides are depleted, PyrR binds to DNA thereby enhancing expression of pyrD, pyrE and pyrF genes. When pyrimidine nucleotides are in excess, the PyrR apoprotein binds to orotate, its co-repressor, to shut down all the pyrimidine genes. Like many positive activators, PyrR is subject to autoregulation and has catalytic activity for uracil phosphoribosyltransferase inducible by orotate.
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Hammerstein, Heidi Carol. "Isolation of a Pseudomonas aeruginosa Aspartate Transcarbamoylase Mutant and the Investigation of Its Growth Characteristics, Pyrimidine Biosynthetic Enzyme Activities, and Virulence Factor Production." Thesis, University of North Texas, 2004. https://digital.library.unt.edu/ark:/67531/metadc4704/.

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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 produce virulence factors. In this work an organism with a mutation in the second step 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 production were also moderately decreased. In the Caenorhabditis elegans infection model the nematodes fed the ATCase mutant had increased mortality, as compared to nematodes fed wild type bacteria. These findings lend support to the hypothesis that changes in the pyrimidine biosynthetic pathway contribute to the organism's ability to effect pathogenicity.
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Books on the topic "Pyrimidine nucleotides"

1

Pharmacology of purine and pyrimidine receptors. San Diego, CA: Elsevier, 2011.

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2

Wilkinson, Yvonne Annette. Nucleotide pool changes resulting from purine and pyrimidine salrage pathway deficiency in Friend erythroleukaemia cells. [s.l: The Author], 1989.

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1951-, Lusty James R., Wearden Peter, and Moreno Virtudes, eds. CRC handbook of nucleobase complexes: Transition metal complexes of naturally occuring nucleobases and their derivatives. Boca Raton, Fla: CRC Press, 1990.

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Jacobson, Kenneth A., and Joel Linden. Pharmacology of Purine and Pyrimidine Receptors. Elsevier Science & Technology Books, 2011.

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Jensen, Christine May. Vitamin B-6 and pyrimidine deoxynucleoside metabolism in the rat. 1989.

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Jensen, Christine May. Vitamin B-6 and pyrimidine deoxynucleoside metabolism in the rat. 1989.

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Stebbins, Jeffrey W. Catalysis, regulation and relationship to structure of Escherichia coli aspartate transcarbamoylase: By Jeffrey William Stebbins. 1990.

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Ulbricht, T. L. V., and Robert Robinson. Purines, Pyrimidines and Nucleotides and the Chemistry of Nucleic Acids. Elsevier Science & Technology Books, 2016.

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Ulbricht, T. L. V. Purines, Pyrimidines and Nucleotides: And the Chemistry of Nucleic Acids. Elsevier Science & Technology Books, 2013.

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Lusty, James R., and Peter Wearden. Handbook of Nucleobase Complexes: Transition Metal Complexes of the Naturally Occurring Nucleobases and Their Derivative. CRC Press, 1991.

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Book chapters on the topic "Pyrimidine nucleotides"

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Ueda, Tohru. "Synthesis and Reaction of Pyrimidine Nucleosides." In Chemistry of Nucleosides and Nucleotides, 1–112. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0995-6_1.

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Sulkowska, Anna. "Association of pyrimidine nucleotides with unfolded albumin." In Spectroscopy of Biological Molecules: New Directions, 267–68. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4479-7_117.

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Connolly, G. P. "Uridine and Pyrimidine Nucleotides in Cell Function." In Purinergic and Pyrimidinergic Signalling I, 403–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-09604-8_14.

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Rudolph, Frederick B., William C. Fanslow, Anil D. Kulkarni, Sulabha S. Kulkarni, and Charles T. Van Buren. "Effect of Dietary Nucleotides on Lymphocyte Maturation." In Purine and Pyrimidine Metabolism in Man V, 497–501. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_83.

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Peters, Godefridus J. "Therapy Related Disturbances in Nucleotides in Cancer Cells." In Purine and Pyrimidine Metabolism in Man VIII, 95–107. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_24.

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Havel, Michael, Werner Monl, Gerhard Schopf, and Mathias M. Müller. "Purine Nucleotides in Human Hearts During Open Heart Surgery." In Purine and Pyrimidine Metabolism in Man V, 529–33. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_82.

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Nuki, G., K. Astrini, D. Brenton, M. Cruikshank, J. Lever, and J. E. Seegmiller. "Purine and Pyrimidine Nucleotides in Some Mutant Human Lymphoblasts." In Ciba Foundation Symposium 48 - Purine and Pyrimidine Metabolism, 127–42. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720301.ch9.

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Lin, Tai-Shun, and Mao-Chin Liu. "Synthesis and Anticancer and Antiviral Activity of Certain Pyrimidine Nucleoside Analogues." In Nucleosides and Nucleotides as Antitumor and Antiviral Agents, 177–201. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2824-1_10.

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Edwards, N. Lawrence, Annette M. Zaytoun, and Gail A. Renard. "Separate Mechanisms for Cellular uptake of Purine Nucleotides by B- and T-Lymphoblasts." In Purine and Pyrimidine Metabolism in Man V, 463–65. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_72.

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Grune, Tilman, and David Perrett. "Rapid Simultaneous Measurement of Nucleotides, Nucleosides and Bases in Tissues by Capillary Electrophoresis." In Purine and Pyrimidine Metabolism in Man VIII, 805–10. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_169.

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Conference papers on the topic "Pyrimidine nucleotides"

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Šimák, Ondřej, Petr Pachl, Tomáš Jandušík, Jiří Brynda, Miloš Buděšínský, and Ivan Rosenberg. "Bi-substrate inhibitors of human pyrimidine 5’-nucleotidases." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414381.

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Chudinov, A. V., O. S. Volkova, V. E. Kuznetsova, V. E. Shershov, and S. A. Lapa. "Application of PCR for simultaneous modification of DNA by various pyrimidine nucleotide derivatives." In MODERN SYNTHETIC METHODOLOGIES FOR CREATING DRUGS AND FUNCTIONAL MATERIALS (MOSM2020): PROCEEDINGS OF THE IV INTERNATIONAL CONFERENCE. AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0068928.

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Ghazaly, Essam A., Magdalena Slusarczyk, Christopher McGuigan, David Harrison, and Sarah P. Blagden. "Abstract B46: NUC-3373: A novel pyrimidine nucleotide analogue that overcomes key cancer drug resistance limiting patient survival." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-b46.

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Matherly, Larry H., Xin Zhang, Adrianne Wallace, Zhanjun Hou, Christina George, Xilin Zhou, and Aleem Gangjee. "Abstract 4481: Tumor-targeting with novel 6-substituted thienoyl[2,3-d]pyrimidine antifolates via cellular uptake by folate receptor α, and inhibition of de novopurine nucleotide biosynthesis." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4481.

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Cherian, Christina, Yiqiang Wang, Shermaine Mitchell-Ryan, Steven Orr, Zhanjun Hou, Aleem Gangjee, and Larry H. Matherly. "Abstract 5493: Tumor-targeting with novel non-benzoyl 6-substituted pyrrolo[2,3-d]pyrimidine antifolates via cellular uptake by folate receptor α and inhibition ofde novopurine nucleotide biosynthesis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5493.

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Mitchell-Ryan, Shermaine K., Lei Wang, Steven Orr, Sita Kugel, Christina Cherian, Aleem Gangjee, and Larry H. Matherly. "Abstract 5494: Novel 6-substituted pyrrolo[2,3-d]pyrimidine thienoyl antifolate regioisomers target folate receptor alpha positive ovarian cancer cells via inhibition of de novo purine nucleotide biosynthesis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5494.

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Wallace-Povirk, Adrianne, Nian Tong, Carrie O'Connor, Zhanjun Hou, Aleem Gangjee, Larry Matherly, and Xilin Zhou. "Abstract 3983: Tumor-targeting with novel dual-targeted 6-substituted thieno[2,3-d]pyrimidine antifolates via cellular uptake by folate receptor α, and inhibition of de novo purine nucleotide biosynthesis." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3983.

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Mitchell-Ryan, Shermaine K., Yiqiang Wang, Christina Cherian, Erika Etnyre, Zhanjun Hou, Aleem Gangjee, and Larry H. Matherly. "Abstract 3822: A tumor-targeted 5-pyrrolo[2,3-d]pyrimidine antifolate is a selective substrate for folate receptor ≤ and potent inhibitor of 5-amino-4-carboxamide formyltransferase inde novopurine nucleotide biosynthesis." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3822.

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Cherian, Christina, Lei Wang, Adrianne Wallace, Steven Orr, Zhanjun Hou, Aleem Gangjee, and Larry H. Matherly. "Abstract 2706: Tumor-targeting with novel pyridyl 6-substituted pyrrolo[2,3-d]pyrimidine antifolates via cellular uptake by folate receptor (FR) α and the proton-coupled folate transporter (PCFT) and inhibition ofde novopurine nucleotide biosynthesis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2706.

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