Relevant bibliographies by topics / Pyrimidines – Metabolism

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  2. Dissertations / Theses
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  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Pyrimidines – Metabolism'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Pyrimidines – Metabolism"

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Nerkar, A. G., S. A. Ghone, and A. K. Thaker. "In SilicoScreening of the Library of Pyrimidine Derivatives as Thymidylate Synthase Inhibitors for Anticancer Activity." E-Journal of Chemistry 6, no. 3 (2009): 665–72. http://dx.doi.org/10.1155/2009/352717.

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We here report the virtual screening of several series of pyrimidine derivatives forin silicoThymidylate Synthase (TS) inhibition to arrive at possible potential inhibitors of TS with acceptable pharmacokinetic or ADME (Absorption, Distribution, Metabolism and Excretion) properties. Library of the molecules was constructed based upon structural modifications of pyrimidines nucleus. Structural modifications in descending order were performed for the series of pyrimidines,vizfrom pyrimidines with five membered heterocyclic ring to pyrimidines with four membered heterocyclic ring to simple pyrimindine carboxylates in an order to arrive at pyrimidines with better inhibition scores (G-Scores) as compared with Raltitrexed (RTX) and active metabolite of 5-Fluorouracil (5-FUMP). The molecules with betterG-Scores were subjected to predict pharmacokinetic or ADME properties. The molecules with acceptable ADME properties and betterG-Scores were prioritized for synthesis and anticancer evaluation. Three molecules from pyrimidine carboxylate series PIC1-31were found acceptable withG-Scores and pharmacokinetic properties. Thus a library of pyrimidine derivatives was constructed based upon the feasibility of synthesis and in silico screened to prioritize the molecules and to obtain potential lead molecules as TS inhibitors.
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Stentoft, Charlotte, Betina Amdisen Røjen, Søren Krogh Jensen, Niels B. Kristensen, Mogens Vestergaard, and Mogens Larsen. "Absorption and intermediary metabolism of purines and pyrimidines in lactating dairy cows." British Journal of Nutrition 113, no. 4 (January 26, 2015): 560–73. http://dx.doi.org/10.1017/s0007114514004000.

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About 20 % of ruminal microbial N in dairy cows derives from purines and pyrimidines; however, their intermediary metabolism and contribution to the overall N metabolism has sparsely been described. In the present study, the postprandial patterns of net portal-drained viscera (PDV) and hepatic metabolism were assessed to evaluate purine and pyrimidine N in dairy cows. Blood was sampled simultaneously from four veins with eight hourly samples from four multi-catheterised Holstein cows. Quantification of twenty purines and pyrimidines was performed with HPLC–MS/MS, and net fluxes were estimated across the PDV, hepatic tissue and total splanchnic tissue (TSP). Concentration differences between veins of fifteen purine and pyrimidine nucleosides (NS), bases (BS) and degradation products (DP) were different from zero (P≤ 0·05), resulting in the net PDV releases of purine NS (0·33–1·3 mmol/h), purine BS (0·0023–0·018 mmol/h), purine DP (7·0–7·8 mmol/h), pyrimidine NS (0·30–2·8 mmol/h) and pyrimidine DP (0·047–0·77 mmol/h). The hepatic removal of purine and pyrimidine was almost equivalent to the net PDV release, resulting in no net TSP release. One exception was uric acid (7·9 mmol/h) from which a large net TSP release originated from the degradation of purine NS and BS. A small net TSP release of the pyrimidine DP β-alanine and β-aminoisobutyric acid ( − 0·032 to 0·37 mmol/h) demonstrated an outlet of N into the circulating N pool. No effect of time relative to feeding was observed (P>0·05). These data indicate that considerable amounts of N are lost in the dairy cow due to prominent intermediary degradation of purines, but that pyrimidine N is reusable to a larger extent.
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Borzenko, Berta, Elena Bakurova, and Ksenia Mironova. "Disorders of purines and pyrimidines metabolism in human gastrointestinal tract cancer." Current Issues in Pharmacy and Medical Sciences 26, no. 4 (December 30, 2013): 369–71. http://dx.doi.org/10.12923/j.2084-980x/26.4/a.02.

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Deng, Wei-Wei, Riko Katahira, and Hiroshi Ashihara. "Short Term Effect of Caffeine on Purine, Pyrimidine and Pyridine Metabolism in Rice (Oryza sativa) Seedlings." Natural Product Communications 10, no. 5 (May 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000510.

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As part of our studies on the physiological and ecological function of caffeine, we investigated the effect of exogenously supplied caffeine on purine, pyrimidine and pyridine metabolism in rice seedlings. We examined the effect of 1 mM caffeine on the in situ metabolism of 14C-labelled adenine, guanine, inosine, uridine, uracil, nicotinamide and nicotinic acid. The segments of 4-day-old dark-grown seedlings were incubated with these labelled compounds for 6 h. For purines, the incorporation of radioactivity from [8-14C]adenine and [8-14C]guanine into nucleotides was enhanced by caffeine; in contrast, incorporation into CO2 were reduced. The radioactivity in ureides (allantoin and allantoic acid) from [8-14C]guanine and [8-14C]inosine was increased by caffeine. For pyrimidines, caffeine enhanced the incorporation of radioactivity from [2-14C]uridine into nucleotides, which was accompanied by a decrease in pyrimidine catabolism. Such difference was not found in the metabolism of [2-14C]uracil. Caffeine did not influence the pyridine metabolism of [carbonyl-14C]-nicotinamide and [2-14C]nicotinic acid. The possible control steps of caffeine on nucleotide metabolism in rice are discussed.
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Liu, Xianxian, and Rebecca E. Parales. "Bacterial Chemotaxis to Atrazine and Related s-Triazines." Applied and Environmental Microbiology 75, no. 17 (July 6, 2009): 5481–88. http://dx.doi.org/10.1128/aem.01030-09.

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ABSTRACT Pseudomonas sp. strain ADP utilizes the human-made s-triazine herbicide atrazine as the sole nitrogen source. The results reported here demonstrate that atrazine and the atrazine degradation intermediates N-isopropylammelide and cyanuric acid are chemoattractants for strain ADP. In addition, the nonmetabolized s-triazine ametryn was also an attractant. The chemotactic response to these s-triazines was not specifically induced during growth with atrazine, and atrazine metabolism was not required for the chemotactic response. A cured variant of strain ADP (ADP M13-2) was attracted to s-triazines, indicating that the atrazine catabolic plasmid pADP-1 is not necessary for the chemotactic response and that atrazine degradation and chemotaxis are not genetically linked. These results indicate that atrazine and related s-triazines are detected by one or more chromosomally encoded chemoreceptors in Pseudomonas sp. strain ADP. We demonstrated that Escherichia coli is attracted to the s-triazine compounds N-isopropylammelide and cyanuric acid, and an E. coli mutant lacking Tap (the pyrimidine chemoreceptor) was unable to respond to s-triazines. These data indicate that pyrimidines and triazines are detected by the same chemoreceptor (Tap) in E. coli. We showed that Pseudomonas sp. strain ADP is attracted to pyrimidines, which are the naturally occurring structures closest to triazines, and propose that chemotaxis toward s-triazines may be due to fortuitous recognition by a pyrimidine chemoreceptor in Pseudomonas sp. strain ADP. In competition assays, the presence of atrazine inhibited chemotaxis of Pseudomonas sp. strain ADP to cytosine, and cytosine inhibited chemotaxis to atrazine, suggesting that pyrimidines and s-triazines are detected by the same chemoreceptor.
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Uchida, Michihiko, Ken-Ichi Kamiya, Teruo Yoshimura, Kin-Ya Sasaki, Hiroshi Tsutani, Takanori Ueda, and Toru Nakamura. "163 Transport and intracel lular metabolism of fluorinated pyrimidines." Pediatric Research 24, no. 1 (July 1988): 138. http://dx.doi.org/10.1203/00006450-198807000-00187.

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Martinussen, J., P. S. Andersen, and K. Hammer. "Nucleotide metabolism in Lactococcus lactis: salvage pathways of exogenous pyrimidines." Journal of Bacteriology 176, no. 5 (1994): 1514–16. http://dx.doi.org/10.1128/jb.176.5.1514-1516.1994.

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SASAMOTO, HAMAKO, KOSHI SAITO, and HIROSHI ASHIHARA. "Metabolism of Pyrimidines in Protoplasts from Cultured Catharanthus roseus Cells*." Annals of Botany 60, no. 4 (October 1987): 417–20. http://dx.doi.org/10.1093/oxfordjournals.aob.a087462.

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Ito, Tetsuya, André B. P. van Kuilenburg, Albert H. Bootsma, Anja J. Haasnoot, Arno van Cruchten, Yoshiro Wada, and Albert H. van Gennip. "Rapid Screening of High-Risk Patients for Disorders of Purine and Pyrimidine Metabolism Using HPLC-Electrospray Tandem Mass Spectrometry of Liquid Urine or Urine-soaked Filter Paper Strips." Clinical Chemistry 46, no. 4 (April 1, 2000): 445–52. http://dx.doi.org/10.1093/clinchem/46.4.445.

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Abstract Background: A rapid and specific screening method for patients at risk of inherited disorders of purine and pyrimidine metabolism is desirable because symptoms are varied and nonspecific. The aim of this study was to develop a rapid and specific method for screening with use of liquid urine samples or urine-soaked filter paper strips. Methods: Reverse-phase HPLC was combined with electrospray ionization (ESI), tandem mass spectrometry (MS/MS), and detection performed by multiple reaction monitoring. Transitions and instrument settings were established for 17 purines or pyrimidines. Stable-isotope-labeled reference compounds were used as internal standards when available. Results: Total analysis time of this method was 15 min, approximately one-third that of conventional HPLC with ultraviolet detection. Recoveries were 96–107% in urine with added analyte, with two exceptions (hypoxanthine, 64%; xanthine, 79%), and 89–110% in urine-soaked filter paper strips, with three exceptions (hypoxanthine, 65%; xanthine, 77%; 5-hydroxymethyluracil, 80%). The expected abnormalities were easily found in samples from patients with purine nucleoside phosphorylase deficiency, ornithine transcarbamylase deficiency, molybdenum cofactor deficiency, adenylosuccinase deficiency, or dihydropyrimidine dehydrogenase deficiency. Conclusions: HPLC-ESI MS/MS of urine allows rapid screening for disorders of purine and pyrimidine metabolism. The filter paper strips offer the advantage of easy collection, transport, and storage of the urine samples.
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Sirakanyan, Samuel N., Victor G. Kartsev, Athina Geronikaki, Domenico Spinelli, Anthi Petrou, Elmira K. Hakobyan, Jasmina Glamoclij, Manija Ivanov, Marina Sokovic, and Anush A. Hovakimyan. "Synthesis and Evaluation of Antimicrobial Activity and Molecular Dock - ing of New N-1,3-thiazol-2-ylacetamides of Condensed Pyrido[3',2':4,5] furo(thieno)[3,2-d]pyrimidines." Current Topics in Medicinal Chemistry 20, no. 24 (November 2, 2020): 2192–209. http://dx.doi.org/10.2174/1568026620666200628145308.

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Background: From the literature it is known that many derivatives of fused thienopyrimidines and furopyrimidines possess broad spectrum of biological activity. Objectives: The current studies describe the synthesis and evaluation of antimicrobial activity of some new N-1,3-thiazol-2-ylacetamides of pyrido[3',2':4,5]furo(thieno)[3,2-d]pyrimidines. Methods: By cyclocondensation of ethyl 1-aminofuro(thieno)[2,3-b]pyridine-2-carboxylates 1with formamide were converted to the pyrido[3',2':4,5]furo(thieno)[3,2-d]pyrimidin-7(8)-ones 2.Alkylation of compound 2 with 2-chloro-N-1,3-thiazol-2-ylacetamide led to the aimed N-1,3-thiazol-2-ylaceta-mides of pyrido[3',2':4,5]furo(thieno)[3,2-d]pyrimidines 3. Starting from compound 2 the relevant S-alkylated derivatives of pyrido[3',2':4,5]furo(thieno)[3,2-d]pyrimidines 6 were also synthesized. Results: All the compounds showed antibacterial activity to non-resistant strains. Compounds 3a-3m showed antibacterial activity with MIC/MBC at 0.08-2.31 mg/mL/0.11-3.75 mg/mL .The two most active compounds, 3j and 6b, appeared to be more active towards MRSA than the reference drugs. Half of the tested compounds appeared to be equipotent/more potent than ketoconazole and more potent than bifonazole. The docking analysis provided useful information about the interactions occurring between the tested compounds and the different enzymes. Conclusion: Gram-negative and Gram-positive bacteria and fungi showed different response towards tested compounds, indicating that different substituents may lead to different modes of action or that the metabolism of some bacteria/fungi was better able to overcome the effect of the compounds or adapt to it.
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Dissertations / Theses on the topic "Pyrimidines – Metabolism"

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Ibrahim, Mohamed M. "Pyrimidine Metabolism in Rhizobium: Physiological Aspects of Pyrimidine Salvage." Thesis, University of North Texas, 1989. https://digital.library.unt.edu/ark:/67531/metadc330907/.

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The objective of this research was to study the pyrimidine salvage pathways of Rhizobium. Three approaches were used to define the pyrimidine salvage pathways operative in two species of Rhizobium, R. meliloti and R. leguminosarum . The first approach was to ascertain the pyrimidine bases and nucleosides that could satisfy the pyrimidine requirement of pyrimidine auxotrophs. Uracil, cytosine, uridine or cytidine all satisfied the absolute pyrimidine requirement. The second approach was to select for mutants resistant to 5-fluoropyrimidine analogues which block known steps in the interconversion of the pyrimidine bases and nucleosides. Mutants resistant to 5-fluorouracil lacked the enzyme uracil phosphoribosyltransferase (upp ) and could no longer use uracil to satisfy their pyrimidine requirement. Mutants resistant to 5-fluorocytosine, while remaining sensitive to 5- fluorouracil, lacked cytosine deaminase (cod) and thus could no longer use cytosine to satisfy their pyrimidine auxotrophy. The third approach used a reversed phase HPLC column to identify the products that accumulated when cytidine, uridine or cytosine was incubated with cell extracts of wild type and analogue resistant mutants of Rhizobium. When cytidine was incubated with cell extracts of Rhizobium wild type, uridine, uracil and cytosine were produced. This Indicated that Rhizobium had an active cytidine deaminase (cdd) and either uridine phosphorylase or uridine hydrolase. By dialyzing the extract and reincubating it with cytidine, uridine and uracil still appeared. This proved that it was a hydrolase ( nuh ) rather than a phosphorylase that degraded the nucleoside. Thus, Rhizobium was found to contain an active cytidine deaminase and cytosine deaminase with no uridine phosphorylase present. The nucleoside hydrolase was active with cytidine, uridine and to a far lesser extent with purines, adenosine and inosine. When high concentrations of cytidine were added to mutants devoid of hydrolase, cytosine was produced from cytidine - 5-monophosphate by the sequential action of uridine ( cytidine ) kinase and nucleoside monophosphate glycosylase. Both ft meliloti and ft leguminosarum had identical salvage pathways.
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Hughes, Lee E. (Lee Everette). "Pyrimidine Metabolism in Streptomyces griseus." Thesis, University of North Texas, 1994. https://digital.library.unt.edu/ark:/67531/metadc278710/.

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Salvage of pyrimidine nucleosides and bases by S. griseus and the regulation of aspartate transcarbamoylase (ATCase) were studied. The velocity-substrate curve for S. griseus ATCase was hyperbolic for both aspartate and carbamoylphosphate. The enzyme activity was diminished in the presence of ATP, CTP, or UTP. The synthesis of ATCase was repressed in cells grown in the presence of exogenous uracil. The specific activity of cells grown with uracil was 43 percent of that for cells grown in minimal medium only. Maximal ATCase and dihydroorotase activities were found in the same column fraction after size-exclusion chromatography, suggesting that both activities could reside in the same polypeptide. The pyrimidine salvage enzymes cytosine deaminase and uridine phosphorylase were identified in S. griseus using HPLC reversed-phase chromatography.
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Patel, Monal V. "The regulatory roles of PyrR and Crc in pyrimidine metabolism in Pseudomonas aeruginosa." Thesis, University of North Texas, 2001. https://digital.library.unt.edu/ark:/67531/metadc2875/.

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The regulatory gene for pyrimidine biosynthesis has been identified and designated pyrR. The pyrR gene product was purified to homogeneity and found to have a monomeric molecular mass of 19 kDa. The pyrR gene is located directly upstream of the pyrBC' genes in the pyrRBC' operon. Insertional mutagenesis of pyrR led to a 50- 70% decrease in the expression of pyrBC', pyrD, pyrE and pyrF while pyrC was unchanged. This suggests that PyrR is a positive activator. The upstream regions of the pyrD, pyrE and pyrF genes contain a common conserved 9 bp sequence to which the purified PyrR protein is proposed to bind. This consensus sequence is absent in pyrC but is present, as an imperfect inverted repeat separated by 11 bp, within the promoter region of pyrR. Gel retardation assays using upstream DNA fragments proved PyrR binds to the DNA of pyrD, pyrE, pyrF as well as pyrR. This suggests that expression of pyrR is autoregulated; moreover, a stable stem-loop structure was determined in the pyrR promoter region such that the SD sequence and the translation start codon for pyrR is sequestered. β-galactosidase activity from transcriptional pyrR::lacZ fusion assays, showed a two-fold in increase when expressed in a pyrR- strain compared to the isogenic pyrR+ strain. Thus, pyrR is negatively regulated while the other pyr genes (except pyrC) are positively activated by PyrR. That no regulation was seen for pyrC is in keeping with the recent discovery of a second functional pyrC that is not regulated in P. aeruginosa. Gel filtration chromatography shows the PyrR protein exists in a dynamic equilibrium, and it is proposed that PyrR functions as a monomer in activating pyrD, pyrE and pyrF and as a dimeric repressor for pyrR by binding to the inverted repeat. A related study discovered that the catabolite repression control (Crc) protein was indirectly involved in pyr gene regulation, and shown to negatively regulate expression of PyrR at the posttranscriptional level.
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Black, Duncan Arthur. "Aspects of purine and pyrimidine metabolism." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/26590.

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In Chapter 1 a review of the literature concerning aspects of erythrocyte membrane transport and metabolism, and purine and pyrimidine metabolism is presented. The effects of pH, pO₂ and inorganic phosphate (Pi) on the uptake and metabolism of hypoxanthine by erythrocytes has been studied in Chapter 2. Uptake of hypoxanthine and accumulation of inosine 5'-monophosphate (IMP) were markedly increased at acid pH, high external phosphate concentrations, and low pO₂. Release of accumulated IMP as hypoxanthine occurred at alkaline pH values and low external phosphate concentrations. Conditions favouring IMP accumulation gave rise, in the absence of hypoxanthine, to a corresponding increase in 5'-phosphoribosyl-1-pyrophosphate (PRPP). Intracellular phosphate concentrations were markedly pH dependent and a model is presented whereby hypoxanthine uptake and release are controlled by intracellular concentrations of inorganic phosphate and 2,3- bisphosphoglycerate (2,3-DPG). These allosteric effectors influence, in opposing ways, two enzymes governing IMP accumulation, namely PRPP synthetase and 5'-nucleotidase. These metabolic properties suggest that the erythrocyte could play a role in the removal of hypoxanthine from anoxic tissue. In Chapter 3 the kinetics and mechanism of transport of orotate across the human erythrocyte membrane and the effect of pH and inorganic phosphate on its metabolism (in the erythrocyte) have been studied. It has been shown that orotate enters erythrocytes with non-saturable kinetics and with a capacity of 190 μmoles/1 packed cells/min at a concentration of 4-6 mmolar. The presence of competition for transport by a number of anions and the lack of competition by uridine is indicative of transport by a general anion transporter, with the ability for concentrative uptake in the absence of other external anions being compatible with transport via a ping-pong mechanism. Inhibition of transport by the specific band 3 inhibitors DIDS and CHCA confirm that transport is via the band 3 anion transporter. This explains the lack of significant uptake of orotate by most differentiated tissues which lack the intact band 3 protein. However, the demonstration of band 3 in rat hepatocytes (Cheng and Levy, 1980) provides a mechanism for the orotate transport which has been observed in liver (Handschumacher and Coleridge, 1979). Changes in pH and inorganic phosphate (Pi) concentrations have been shown to have marked effects on the relative quantities of metabolic products produced by the erythrocyte from orotate. There was an increase in orotate metabolised with increasing Pi, an effect augmented by lowering the pH, and most easily explained by the allosteric activation of PRPP synthetase by Pi. The increase in UTP levels with decreasing pH may be the consequence of both increased PRPP availability for the formation of uridine nucleotide from orotate, and decreased conversion of UMP to uridine by pyrimidine 5'-nucleotidase, which is known to be inhibited by phosphate. The accumulation of UDP sugars is optimal at a phosphate concentration of 10 mmolar, which is unexplained but would be compatible with an inhibitory effect of Pi on CTP synthetase. A PRPP wasting cycle at alkaline pH values is proposed to explain the apparent paradox where no PRPP was observed to accumulate in erythrocytes (Chapter 2) at pH values of 7.6 and above in the presence of 10 mmolar phosphate and no added hypoxanthine, yet the metabolism of orotate, which is a PRPP utilising reaction, at alkaline pH values was readily demonstrable here. This (apparent paradox) can be resolved if one assumes that even in the absence of added hypoxanthine and demonstrable intracellular IMP there are sufficient quantities of hypoxanthine and/or IMP to maintain a PRPP wasting cycle at alkaline pH values. The cycle is interrupted at acidic pH values as phosphate levels rise and inhibit 5'-nucleotidase, an effect augmented by the decreasing levels of 2,3-DPG which accompany decreasing pH. This wasting cycle has recently been confirmed by P. Berman (unpublished). The kinetics of orotate uptake by erythrocytes and its eventual release as uridine provides a role for the erythrocyte in the transport and distribution of pyrimidines to peripheral tissues. A model is proposed and involves the de novo production of orotate in the liver. In the next step erythrocytes take up the orotate secreted by the liver into the circulation, convert it into an intermediate buffer store of uridine nucleotides, whose distribution is a function of pH and phosphate concentration, and eventually release it as uridine, which is a readily available form of pyrimidine for utilisation by peripheral nucleated cells. The enhancement of uptake of labelled orotate into nucleic acids of cultured cells is demonstrated here. The degradative half of the cycle proposes that uracil and palanine are the predominant degradative forms of pyrimidines produced by peripheral cells, and their ultimate metabolic fate is complete catabolism in the liver to CO₂ and water. In the final chapter the possible role of the human erythrocyte in the prevention of reperfusion injury has been investigated. The development of a model of renal ischaemia in the rat is described. The ability of human erythrocytes, "primed" by preincubating in acid medium of high Pi concentration and low pO₂, to take up hypoxanthine in a concentrative manner when perfused through ischaemic rat kidney is demonstrated. Attempts to demonstrate improved survival and renal function in rats with "primed" human erythrocytes prior to reperfusion were, however, unsuccessful. It is further demonstrated that "unprimed" human erythrocytes, resident in ischaemic rat kidney for 3 hours, take up hypoxanthine and convert it to IMP. that erythrocytes could play a physiological prevention of reperfusion injury.
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Scott, Allelia Worrall. "Pyrimidine Nucleoside Metabolism in Pseudomonads and Enteric Bacteria." Thesis, University of North Texas, 1991. https://digital.library.unt.edu/ark:/67531/metadc500941/.

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Metabolic differences in the strategies used for pyrimidine base and nucleoside salvage were studied in the pseudomonads and enteric bacteria. Fluoro--analogs were used to select mutant strains of E. coli, S. typhimurium, P. putida, and P. aeruginosa blocked in one or more of the uracil and uridine salvage enzymes. HPLC analysis of cell-free extracts from wild-type and mutant strains examined the effectiveness of the selections. Evidence was found for cytidine kinase in Pseudomonas and for an activity that converted uracil compounds to cytosine compounds. Using media supplemented with 150 μg of orotic acid per ml, P. putida SOC 1, a Pyr, upp mutant which utilizes orotic acid as a pyrimidine source was isolated for the first time in any study.
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Farajallah, Azizeh M. "Focused chemical libraries targeting pyrimidine metabolism in Plasmodium falciparum /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/8652.

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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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Lee, Yick-Shun. "Pyrimidine Metabolism in Bacteria: Physiological Properties of Nucleoside Hydrolase and Uridine Kinase." Thesis, University of North Texas, 1991. https://digital.library.unt.edu/ark:/67531/metadc798309/.

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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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Léger, Dominique. "L'aspartate transcarbamylase, enzyme clef de la regulation du metabolisme des pyrimidines." Paris 6, 1987. http://www.theses.fr/1987PA066181.

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Books on the topic "Pyrimidines – Metabolism"

1

International Symposium on Human Purine and Pyrimidine Metabolism (6th 1988 Hakone-machi, Japan). Purine and pyrimidine metabolism in man VI. New York: Plenum Press, 1989.

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1926-, Nyhan William L., Thompson L. F. 1947-, Watts R. W. E, and Seegmiller J. E, eds. Purine and pyrimidine metabolism in man V. New York: Plenum Press, 1986.

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International Symposium on Purine and Pyrimidine Metabolism in Man (7th 1991 Bournemouth, England). Purine and pyrimidine metabolism in man VII. New York: Plenum Press, 1991.

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Nyhan, W. L., L. F. Thompson, and R. W. E. Watts, eds. Purine and Pyrimidine Metabolism in Man V. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2.

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Harkness, R. Angus, Gertrude B. Elion, and Nepomuk Zöllner, eds. Purine and Pyrimidine Metabolism in Man VII. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4899-2638-8.

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Mikanagi, Kiyonobu, Kusuki Nishioka, and William N. Kelley, eds. Purine and Pyrimidine Metabolism in Man VI. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5673-8.

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Mikanagi, Kiyonobu, Kusuki Nishioka, and William N. Kelley, eds. Purine and Pyrimidine Metabolism in Man VI. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5676-9.

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Nyhan, W. L., L. F. Thompson, and R. W. E. Watts, eds. Purine and Pyrimidine Metabolism in Man V. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7.

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Zoref-Shani, Esther, and Oded Sperling, eds. Purine and Pyrimidine Metabolism in Man X. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/b113056.

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Harkness, R. Angus, Gertrude B. Elion, and Nepomuk Zöllner, eds. Purine and Pyrimidine Metabolism in Man VII. New York, NY: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-7703-4.

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Book chapters on the topic "Pyrimidines – Metabolism"

1

Harley, E. H., S. Sacks, P. Berman, L. Cohen, H. A. Simmonds, L. D. Fairbanks, and D. Black. "Source and Fate of Circulating Pyrimidines." In Purine and Pyrimidine Metabolism in Man V, 109–13. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_17.

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Larovere, Laura, Alexandra Latini, Catalina Depetris-Boldini, Carlos E. Coronel, and Raquel Dodelson De Kremer. "Cerebrospinal Fluid Purines, Pyrimidines, Organic Acids and Amino Acids in Neonatal Citrullinaemia." In Purine and Pyrimidine Metabolism in Man X, 97–101. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46843-3_19.

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Uchida, Michihiko, Dah Hsi W. Ho, Ken-ichi Kamiya, Teruo Yoshimura, Kin-ya Sasaki, Hiroshi Tsutani, and Toru Nakamura. "Transport and Intracellular Metabolism of Fluorinated Pyrimidines in Cultured Cell Lines." In Advances in Experimental Medicine and Biology, 321–26. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5676-9_47.

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Lazzarino, Giuseppe, Angela Maria Amorini, Valentina Di Pietro, and Barbara Tavazzi. "HPLC Analysis for the Clinical–Biochemical Diagnosis of Inborn Errors of Metabolism of Purines and Pyrimidines." In Methods in Molecular Biology, 99–117. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-61737-985-7_5.

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Löffler, Monika, Elizabeth A. Carrey, and Elke Zameitat. "Essential Role of Mitochondria in Pyrimidine Metabolism." In Tumor Cell Metabolism, 287–311. Vienna: Springer Vienna, 2015. http://dx.doi.org/10.1007/978-3-7091-1824-5_13.

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Switzer, Robert L., Howard Zalkin, and Hans Henrik Saxild. "Purine, Pyrimidine, and Pyridine Nucleotide Metabolism." In Bacillus subtilis and Its Closest Relatives, 255–69. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555817992.ch19.

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van den Berghe, Georges, M. Françoise Vincent, and Sandrine Marie. "Disorders of Purine and Pyrimidine Metabolism." In Inborn Metabolic Diseases, 433–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/978-3-540-28785-8_35.

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Van den Berghe, G., and M. F. Vincent. "Disorders of Purine and Pyrimidine Metabolism." In Inborn Metabolic Diseases, 289–302. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-03147-6_26.

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van den Berghe, G., M. F. Vincent, and S. Marie. "Disorders of Purine and Pyrimidine Metabolism." In Inborn Metabolic Diseases, 354–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-662-04285-4_31.

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Rogosa, Morrison, Micah I. Krichevsky, and Rita R. Colwell. "Amine, Amide, Lactam, Purine, Pyrimidine Metabolism." In Springer Series in Microbiology, 187–90. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4612-4986-3_32.

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Conference papers on the topic "Pyrimidines – Metabolism"

1

Tong, Nian, Khushbu Shah, Aleem Gangjee, Carrie O’Connor, Adrianne W. Porvirk, Aamod Dekhne, Zhanjun Hou, and Larry H. Matherly. "Abstract 789: Multi-targeted novel 5-substituted pyrrolo[3,2-d]pyrimidines with tumor-selective targeting and inhibition of cytosolicde novopurine biosynthesis and mitochondrial one-carbon metabolism." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-789.

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Tong, Nian, Khushbu Shah, Aleem Gangjee, Carrie O’Connor, Adrianne W. Porvirk, Aamod Dekhne, Zhanjun Hou, and Larry H. Matherly. "Abstract 789: Multi-targeted novel 5-substituted pyrrolo[3,2-d]pyrimidines with tumor-selective targeting and inhibition of cytosolicde novopurine biosynthesis and mitochondrial one-carbon metabolism." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-789.

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Doshi, Arpit, Adrianne Wallace-Povirk, Carrie O'Connor, Zhanjun Hou, Larry Matherly, and Aleem Gangjee. "Abstract 511: Targeted one-carbon (1C) metabolism inhibitors: Design, synthesis and biological evaluation of novel 5-substituted pyrrolo[3,2-d]pyrimidines with pyridyl- andortho-fluoropyridyl glutamate side chains as selective folate receptors substrates." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-511.

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Imanishi, Satoshi, Tomohiro Umezu, Chiaki Kobayashi, Kazuma Ohyashiki, and Junko Ohyashiki. "Abstract 5627: Involvement of pyrimidine metabolism pathway in 5-azacytidine resistance." 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.am2013-5627.

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Zurlo, Giada, Jeremy Simon, Cheng Fan, Adam Robinson, Javier Rodriguez Martinez, Alex Kriegsheim, Jason Locasale, Charles Perou, and Qing Zhang. "Abstract B18: ADSL controls pyrimidine metabolism and triple-negative breast tumorigenesis." In Abstracts: AACR Special Conference: Advances in Breast Cancer Research; October 7-10, 2017; Hollywood, CA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1557-3125.advbc17-b18.

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Gokare, Prashanth Ravishankar, Niklas Finnberg, Jenny Dai, and Wafik El-Deiry. "Abstract PR03: P53 inhibits the expression of the pyrimidine catabolic gene Dihydropyrimidine dehydrogenase (DPYD)." In Abstracts: AACR Special Conference: Metabolism and Cancer; June 7-10, 2015; Bellevue, WA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.metca15-pr03.

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Dekhne, Aamod, Khushbu Shah, Gregory S. Ducker, Md Junayed Nayeen, Jade M. Katinas, Jennifer Wong, Arpit Doshi, et al. "Abstract 2992: Cellular pharmacodynamics of mitochondrial one-carbon metabolism-targeting 5-substituted pyrrolo[3,2-d]pyrimidine antifolates." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2992.

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Dekhne, Aamod, Khushbu Shah, Gregory S. Ducker, Md Junayed Nayeen, Jade M. Katinas, Jennifer Wong, Arpit Doshi, et al. "Abstract 2992: Cellular pharmacodynamics of mitochondrial one-carbon metabolism-targeting 5-substituted pyrrolo[3,2-d]pyrimidine antifolates." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2992.

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Mozgovaya, E., S. Bedina, A. Trofimenko, and I. Zborovskaya. "AB0187 The association between activity of purine and pyrimidine metabolism enzymes and disease activity in systemic scleroderma patients." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.4743.

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Mozgovaya, Elena, Svetlana Bedina, Andrew Trofimenko, Irina Zborovskaya, Maria Mamus, and Ekaterina Tikhomirova. "AB0216 THE IMBALANCE OF ACTIVITIES OF PURINE AND PYRIMIDINE METABOLISM ENZYMES IN RED BLOOD CELLS OF SYSTEMIC SCLERODERMA PATIENTS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.2125.

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