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Journal articles on the topic 'Phosphoribosyltransferas'

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Published: 10 December 2022

Last updated: 29 January 2023

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1

Aklujkar, Muktak. "Two ATP phosphoribosyltransferase isozymes of Geobacter sulfurreducens contribute to growth in the presence or absence of histidine and under nitrogen fixation conditions." Canadian Journal of Microbiology 57, no. 7 (July 2011): 547–58. http://dx.doi.org/10.1139/w11-047.

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Bacteria of the Geobacter clade possess two distinct ATP phosphoribosyltransferases encoded by hisGL and hisGS+hisZ to catalyze the first reaction of histidine biosynthesis. This very unusual redundancy was investigated by mutational analysis. The hisGL, hisGS, and hisZ genes of Geobacter sulfurreducens were deleted, effects on growth and histidine biosynthesis gene expression were evaluated, and deficiencies were complemented with plasmid-borne genes. Both hisGL and hisGS+hisZ encode functional ATP phosphoribosyltransferases. However, deletion of hisGL resulted in no growth defect, whereas deletion of hisGS delayed growth when histidine was not provided. Both deletions increased hisZ transcript abundance, and both ΔhisGS and ΔhisZ mutations increased hisGL transcript abundance. Growth with HisGL alone (due to deletion of either hisGS or hisZ) was better under nitrogen fixation conditions than when ammonium was provided. Deletion of hisZ caused growth defects under all conditions tested, with or without exogenous sources of histidine, with different patterns of histidine biosynthesis gene expression under each condition. Taken together, the data indicate that G. sulfurreducens depends primarily on the HisGSZ isozyme as an ATP phosphoribosyltransferase in histidine biosynthesis, and for other functions when histidine is available; however, HisGL also functions as ATP phosphoribosyltransferase, particularly during nitrogen fixation.

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2

Fateev, Ilja V., Ekaterina V. Sinitsina, Aiguzel U. Bikanasova, Maria A. Kostromina, Elena S. Tuzova, Larisa V. Esipova, Tatiana I. Muravyova, Alexei L. Kayushin, Irina D. Konstantinova, and Roman S. Esipov. "Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis." Beilstein Journal of Organic Chemistry 14 (December 21, 2018): 3098–105. http://dx.doi.org/10.3762/bjoc.14.289.

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Phosphoribosyltransferases are the tools that allow the synthesis of nucleotide analogues using multi-enzymatic cascades. The recombinant adenine phosphoribosyltransferase (TthAPRT) and hypoxanthine phosphoribosyltransferase (TthHPRT) from Thermus thermophilus HB27 were expressed in E.coli strains and purified by chromatographic methods with yields of 10–13 mg per liter of culture. The activity dependence of TthAPRT and TthHPRT on different factors was investigated along with the substrate specificity towards different heterocyclic bases. The kinetic parameters for TthHPRT with natural substrates were determined. Two nucleotides were synthesized: 9-(β-D-ribofuranosyl)-2-chloroadenine 5'-monophosphate (2-Сl-AMP) using TthAPRT and 1-(β-D-ribofuranosyl)pyrazolo[3,4-d]pyrimidine-4-one 5'-monophosphate (Allop-MP) using TthНPRT.

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3

Sauer, Jørgen, and Per Nygaard. "Expression of the Methanobacterium thermoautotrophicum hpt Gene, Encoding Hypoxanthine (Guanine) Phosphoribosyltransferase, in Escherichia coli." Journal of Bacteriology 181, no. 6 (March 15, 1999): 1958–62. http://dx.doi.org/10.1128/jb.181.6.1958-1962.1999.

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ABSTRACT The hpt gene from the archaeon Methanobacterium thermoautotrophicum, encoding hypoxanthine (guanine) phosphoribosyltransferase, was cloned by functional complementation into Escherichia coli. The hpt-encoded amino acid sequence is most similar to adenine phosphoribosyltransferases, but the encoded enzyme has activity only with hypoxanthine and guanine. The synthesis of the recombinant enzyme is apparently limited by the presence of the rare arginine codons AGA and AGG and the rare isoleucine AUA codon on the hpt gene. The recombinant enzyme was purified to apparent homogeneity.

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4

OLIVEIRA, DENILSON F., HELVÉCIO M. DOS SANTOS JÚNIOR, ALEXANDRO S. NUNES, VICENTE P. CAMPOS, RENATA S. C. DE PINHO, and GIOVANNA C. GAJO. "Purification and identification of metabolites produced by Bacillus cereus and B. subtilis active against Meloidogyne exigua, and their in silico interaction with a putative phosphoribosyltransferase fromM. incognita." Anais da Academia Brasileira de Ciências 86, no. 2 (June 2014): 525–38. http://dx.doi.org/10.1590/0001-3765201402412.

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To contribute to the development of products to controlMeloidogyne exigua, the bacteria Bacillus cereus and B. subtilis were cultivated in liquid medium to produce metabolites active against this plant-parasitic nematode. Fractionation of the crude dichloromethane extracts obtained from the cultures afforded uracil, 9H-purine and dihydrouracil. All compounds were active against M. exigua, the latter being the most efficient. This substance presented a LC50 of 204 µg/mL against the nematode, while a LC50 of 260 µg/mL was observed for the commercial nematicide carbofuran. A search for protein-ligand complexes in which the ligands were structurally similar to dihydrouracil resulted in the selection of phosphoribosyltransferases, the sequences of which were used in an in silico search in the genome of M. incognita for a similar sequence of amino acids. The resulting sequence was modelled and dihydrouracil and 9H-purine were inserted in the active site of this putative phosphoribosyltransferase resulting in protein-ligand complexes that underwent molecular dynamics simulations. Calculation of the binding free-energies of these complexes revealed that the dissociation constant of dihydrouracil and 9H-purine to this protein is around 8.3 x 10-7 and 1.6 x 10-6 M, respectively. Consequently, these substances and the putative phosphoribosyltransferase are promising for the development of new products to control M. exigua.

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5

Aronov, Alex M., Narsimha R. Munagala, Irwin D. Kuntz, and Ching C. Wang. "Virtual Screening of Combinatorial Libraries across a Gene Family: in Search of Inhibitors of Giardia lamblia Guanine Phosphoribosyltransferase." Antimicrobial Agents and Chemotherapy 45, no. 9 (September 1, 2001): 2571–76. http://dx.doi.org/10.1128/aac.45.9.2571-2576.2001.

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ABSTRACT Parasitic protozoa lack the ability to synthesize purine nucleotides de novo, relying instead on purine salvage enzymes for their survival. Guanine phosphoribosyltransferase (GPRT) from the protozoan parasite Giardia lamblia is a potential target for rational antiparasitic drug design, based on the experimental evidence, which indicates the lack of interconversion between adenine and guanine nucleotide pools. The present study is a continuation of our efforts to use three-dimensional structures of parasitic phosphoribosyltransferases (PRTs) to design novel antiparasitic agents. Two micromolar phthalimide-based GPRT inhibitors were identified by screening the in-house phthalimide library. A combination of structure-based scaffold selection using virtual library screening across the PRT gene family and solid phase library synthesis led to identification of smaller (molecular weight, <300) ligands with moderate to low specificity for GPRT; the best inhibitors, GP3 and GP5, had K i values in the 23 to 25 μM range. These results represent significant progress toward the goal of designing potent inhibitors of purine salvage inGiardia parasites. As a second step in this process, altering the phthalimide moiety to optimize interactions in the guanine-binding pocket of GPRT is expected to lead to compounds with promising activity against G. lamblia PRT.

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6

Boitz, Jan M., and Buddy Ullman. "Amplification of Adenine Phosphoribosyltransferase Suppresses the Conditionally Lethal Growth and Virulence Phenotype ofLeishmania donovaniMutants Lacking Both Hypoxanthine-guanine and Xanthine Phosphoribosyltransferases." Journal of Biological Chemistry 285, no. 24 (April 2, 2010): 18555–64. http://dx.doi.org/10.1074/jbc.m110.125393.

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7

Craig, Sydney P., and Ann E. Eakin. "Purine Phosphoribosyltransferases." Journal of Biological Chemistry 275, no. 27 (May 17, 2000): 20231–34. http://dx.doi.org/10.1074/jbc.r000002200.

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8

Bollée, Guillaume, Jérôme Harambat, Albert Bensman, Bertrand Knebelmann, Michel Daudon, and Irène Ceballos-Picot. "Adenine Phosphoribosyltransferase Deficiency." Clinical Journal of the American Society of Nephrology 7, no. 9 (June 14, 2012): 1521–27. http://dx.doi.org/10.2215/cjn.02320312.

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9

Kadziola, A., K. S. Jensen, A. Mølgaard, J. C. N. Poulsen, and K. F. Jensen. "Sulfolobus solfataricusadenine phosphoribosyltransferase." Acta Crystallographica Section A Foundations of Crystallography 67, a1 (August 22, 2011): C786—C787. http://dx.doi.org/10.1107/s0108767311080093.

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10

Chander, Preethi, Kari M. Halbig, Jamie K. Miller, Christopher J. Fields, Heather K. S. Bonner, Gail K. Grabner, Robert L. Switzer, and Janet L. Smith. "Structure of the Nucleotide Complex of PyrR, the pyr Attenuation Protein from Bacillus caldolyticus, Suggests Dual Regulation by Pyrimidine and Purine Nucleotides." Journal of Bacteriology 187, no. 5 (March 1, 2005): 1773–82. http://dx.doi.org/10.1128/jb.187.5.1773-1782.2005.

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ABSTRACT PyrR is a protein that regulates the expression of genes and operons of pyrimidine nucleotide biosynthesis (pyr genes) in many bacteria. PyrR acts by binding to specific sequences on pyr mRNA and causing transcriptional attenuation when intracellular levels of uridine nucleotides are elevated. PyrR from Bacillus subtilis has been purified and extensively studied. In this work, we describe the purification to homogeneity and characterization of recombinant PyrR from the thermophile Bacillus caldolyticus and the crystal structures of unliganded PyrR and a PyrR-nucleotide complex. The B. caldolyticus pyrR gene was previously shown to restore normal regulation of the B. subtilis pyr operon in a pyrR deletion mutant. Like B. subtilis PyrR, B. caldolyticus PyrR catalyzes the uracil phosphoribosyltransferase reaction but with maximal activity at 60°C. Crystal structures of B. caldolyticus PyrR reveal a dimer similar to the B. subtilis PyrR dimer and, for the first time, binding sites for nucleotides. UMP and GMP, accompanied by Mg2+, bind specifically to PyrR active sites. Nucleotide binding to PyrR is similar to other phosphoribosyltransferases, but Mg2+ binding differs. GMP binding was unexpected. The protein bound specific sequences of pyr RNA 100 to 1,000 times more tightly than B. subtilis PyrR, depending on the RNA tested and the assay method; uridine nucleotides enhanced RNA binding, but guanosine nucleotides antagonized it. The new findings of specific GMP binding and its antagonism of RNA binding suggest cross-regulation of the pyr operon by purines.

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11

Munagala, Narsimha, Anne E. Sarver, and Ching C. Wang. "Converting the Guanine Phosphoribosyltransferase fromGiardia lambliato a Hypoxanthine-guanine Phosphoribosyltransferase." Journal of Biological Chemistry 275, no. 47 (September 6, 2000): 37072–77. http://dx.doi.org/10.1074/jbc.m007239200.

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12

Nishida, Y., and T. Miyamoto. "Simple Screening Methods for Hypoxanthine-Guanine Phosphoribosyltransferase and Adenine Phosphoribosyltransferase Deficiencies Using Dried Blood Spots on Filter Paper." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 23, no. 5 (September 1986): 529–32. http://dx.doi.org/10.1177/000456328602300507.

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Simple methods for the detection of hypoxanthine-guanine phosphoribosyltransferase and/or adenine phosphoribosyltransferase deficiencies using dried filter paper blood spots were studied. Enzyme activities in the eluate from dried filter paper blood spots stored for 4 weeks at room conditions were shown to be quite stable. Autoradiographs prepared from dried filter paper blood spots and DE-81 papers soaked with enzyme reaction mixtures containing 14C-hypoxanthine and/or 14C-adenine showed sharp radioactive spots in normal subjects. No activity was evident in the cases of the Lesch-Nyhan syndrome and/or adenine phosphoribosyltransferase deficiency. The methods seem to be suitable for screening.

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13

CURTO, Raul, O. Eberhard VOIT, and Marta CASCANTE. "Analysis of abnormalities in purine metabolism leading to gout and to neurological dysfunctions in man." Biochemical Journal 329, no. 3 (February 1, 1998): 477–87. http://dx.doi.org/10.1042/bj3290477.

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A modelling approach is used to analyse diseases associated with purine metabolism in man. The specific focus is on deficiencies in two enzymes, hypoxanthine:guanine phosphoribosyltransferase and adenylosuccinate lyase. These deficiencies can lead to a number of symptoms, including neurological dysfunctions and mental retardation. Although the biochemical mechanisms of dysfunctions associated with adenylosuccinate lyase deficiency are not completely understood, there is at least general agreement in the literature about possible causes. Simulations with our model confirm that accumulation of the two substrates of the enzyme can lead to significant biochemical imbalance. In hypoxanthine:guanine phosphoribosyltransferase deficiency the biochemical mechanisms associated with neurological dysfunctions are less clear. Model analyses support some old hypotheses but also suggest new indicators for possible causes of neurological dysfunctions associated with this deficiency. Hypoxanthine:guanine phosphoribosyltransferase deficiency is known to cause hyperuricaemia and gout. We compare the relative importance of this deficiency with other known causes of gout in humans. The analysis suggests that defects in the excretion of uric acid are more consequential than defects in uric acid synthesis such as hypoxanthine:guanine phosphoribosyltransferase deficiency.

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14

Jardim, Armando, Susan E. Bergeson, Sarah Shih, Nicola Carter, Randall W. Lucas, Gilles Merlin, Peter J. Myler, Kenneth Stuart, and Buddy Ullman. "Xanthine Phosphoribosyltransferase fromLeishmania donovani." Journal of Biological Chemistry 274, no. 48 (November 26, 1999): 34403–10. http://dx.doi.org/10.1074/jbc.274.48.34403.

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15

Pittelli, Maria, Laura Formentini, Giuseppe Faraco, Andrea Lapucci, Elena Rapizzi, Francesca Cialdai, Giovanni Romano, Gloriano Moneti, Flavio Moroni, and Alberto Chiarugi. "Inhibition of Nicotinamide Phosphoribosyltransferase." Journal of Biological Chemistry 285, no. 44 (August 19, 2010): 34106–14. http://dx.doi.org/10.1074/jbc.m110.136739.

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16

OLESEN, UFFE HØGH, NINA HASTRUP, and MAXWELL SEHESTED. "Expression patterns of nicotinamide phosphoribosyltransferase and nicotinic acid phosphoribosyltransferase in human malignant lymphomas." APMIS 119, no. 4-5 (March 25, 2011): 296–303. http://dx.doi.org/10.1111/j.1600-0463.2011.02733.x.

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17

Santiago, Manuel F., and Thomas P. West. "Control of pyrimidine formation in Pseudomonas putida ATCC 17536." Canadian Journal of Microbiology 48, no. 12 (December 1, 2002): 1076–81. http://dx.doi.org/10.1139/w02-110.

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The regulation of de novo pyrimidine biosynthesis in Pseudomonas putida ATCC 17536 by pyrimidines was explored. The pathway enzyme activities were higher in glucose-grown cells than in succinate-grown cells, indicating catabolite repression by succinate. In P. putida cells grown on succinate as a carbon source, only aspartate transcarbamoylase activity was greatly diminished by uracil supplementation. When glucose was the carbon source, orotic acid supplementation significantly decreased orotate phosphoribosyltransferase and orotidine 5'-monophosphate (OMP) decarboxylase activities. Uracil auxotrophs, deficient for dihydroorotase activity or with reduced phosphoribosyltransferase activity, were isolated. After pyrimidine limitation of both auxotrophs, the greatest derepression of enzyme activity was observed for OMP decarboxylase independent of carbon source. Orotic acid induced both phosphoribosyltransferase and decarboxylase activities in glucose-grown cells of the dihydroorotase-deficient strain. Regulation at the transcriptional level of de novo pyrimidine biosynthetic enzyme synthesis in P. putida ATCC 17536 was observed, which contrasts with previous observations.Key words: pyrimidine biosynthesis, regulation, auxotrophs, induction, Pseudomonas.

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18

Davidson, B. L., M. Pashmforoush, W. N. Kelley, and T. D. Palella. "Human Hypoxanthine-Guanine Phosphoribosyltransferase Deficiency." Journal of Biological Chemistry 264, no. 1 (January 1989): 520–25. http://dx.doi.org/10.1016/s0021-9258(17)31289-9.

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19

Takahashi, Ryo, Shota Nakamura, Takuya Yoshida, Yuji Kobayashi, and Tadayasu Ohkubo. "Crystallization of human nicotinamide phosphoribosyltransferase." Acta Crystallographica Section F Structural Biology and Crystallization Communications 63, no. 5 (April 6, 2007): 375–77. http://dx.doi.org/10.1107/s1744309107006069.

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20

Árnadóttir, Margrét. "Febuxostat in Adenosine Phosphoribosyltransferase Deficiency." American Journal of Kidney Diseases 64, no. 2 (August 2014): 316. http://dx.doi.org/10.1053/j.ajkd.2014.04.026.

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21

Raman, Jayalakshmi, Chethan S. Ashok, Sujay I.N. Subbayya, Ranjith P. Anand, Senthamizh T. Selvi, and Hemalatha Balaram. "Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase." FEBS Journal 272, no. 8 (March 29, 2005): 1900–1911. http://dx.doi.org/10.1111/j.1742-4658.2005.04620.x.

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22

Scapin, Giovanna, Charles Grubmeyer, and James C. Sacchettini. "Crystal Structure of Orotate Phosphoribosyltransferase." Biochemistry 33, no. 6 (February 15, 1994): 1287–94. http://dx.doi.org/10.1021/bi00172a001.

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23

Vos, Siska, John de Jersey, and Jennifer L. Martin. "Crystal Structure ofEscherichia coliXanthine Phosphoribosyltransferase†." Biochemistry 36, no. 14 (April 1997): 4125–34. http://dx.doi.org/10.1021/bi962640d.

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24

Torres, R. J., S. Puente, A. Menendez, and N. Fernandez-Garcia. "Unapparent hypoxanthine-guanine phosphoribosyltransferase deficiency." Clinica Chimica Acta 472 (September 2017): 136–38. http://dx.doi.org/10.1016/j.cca.2017.08.002.

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25

LAXDAL, THRÖSTUR, and TÓMAS Á. JÓNASSON. "Adenine Phosphoribosyltransferase Deficiency in Iceland." Acta Medica Scandinavica 224, no. 6 (April 24, 2009): 621–26. http://dx.doi.org/10.1111/j.0954-6820.1988.tb19635.x.

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26

Harambat, Jérôme, Guillaume Bollée, Michel Daudon, Irène Ceballos-Picot, and Albert Bensman. "Adenine phosphoribosyltransferase deficiency in children." Pediatric Nephrology 27, no. 4 (January 3, 2012): 571–79. http://dx.doi.org/10.1007/s00467-011-2037-0.

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27

Izadpanah, A., and J. Rappaport. "Nicotinamide phosphoribosyltransferase in wound healing." American Journal of the Medical Sciences 365 (February 2023): S70. http://dx.doi.org/10.1016/s0002-9629(23)00139-8.

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28

Ikeda, Kazumasa, Harudo Suzuki, and Shigeki Nakagawa. "Human brain hypoxanthine guanine phosphoribosyltransferase: Structural and functional comparison with erythrocyte hypoxanthine guanine phosphoribosyltransferase." International Journal of Biochemistry 18, no. 7 (January 1986): 575–81. http://dx.doi.org/10.1016/0020-711x(86)90236-3.

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29

Syed, Danyal B., and Donald L. Sloan. "Orotate phosphoribosyltransferase and hypoxanthine/guanine phosphoribosyltransferase from yeast: Kinetic analysis with chromium(III) pyrophosphate." Journal of Inorganic Biochemistry 38, no. 2 (February 1990): 127–38. http://dx.doi.org/10.1016/0162-0134(90)84021-g.

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30

Cerna, David, Hongyun Li, Siobhan Flaherty, Naoko Takebe, C. Norman Coleman, and Stephen S. Yoo. "Inhibition of Nicotinamide Phosphoribosyltransferase (NAMPT) Activity by Small Molecule GMX1778 Regulates Reactive Oxygen Species (ROS)-mediated Cytotoxicity in a p53- and Nicotinic Acid Phosphoribosyltransferase1 (NAPRT1)-dependent Manner." Journal of Biological Chemistry 287, no. 26 (May 8, 2012): 22408–17. http://dx.doi.org/10.1074/jbc.m112.357301.

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31

Allen, Thomas, Eugene V. Henschel, Terry Coons, Laura Cross, Joseph Conley, and Buddy Ullman. "Purification and characterization of the adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase activities from Leishmania donovani." Molecular and Biochemical Parasitology 33, no. 3 (March 1989): 273–81. http://dx.doi.org/10.1016/0166-6851(89)90089-3.

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32

Shackelford, R. E., K. Mayhall, N. M. Maxwell, E. Kandil, and D. Coppola. "Nicotinamide Phosphoribosyltransferase in Malignancy: A Review." Genes & Cancer 4, no. 11-12 (October 30, 2013): 447–56. http://dx.doi.org/10.1177/1947601913507576.

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33

Foster, Alan C., William C. Zinkand, and Robert Schwarcz. "Quinolinic Acid Phosphoribosyltransferase in Rat Brain." Journal of Neurochemistry 44, no. 2 (February 1985): 446–54. http://dx.doi.org/10.1111/j.1471-4159.1985.tb05435.x.

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34

Runolfsdottir, Hrafnhildur Linnet, Runolfur Palsson, Inger M. Agustsdottir, Olafur S. Indridason, and Vidar O. Edvardsson. "Kidney Disease in Adenine Phosphoribosyltransferase Deficiency." American Journal of Kidney Diseases 67, no. 3 (March 2016): 431–38. http://dx.doi.org/10.1053/j.ajkd.2015.10.023.

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35

Grubmeyer, C., E. Segura, and R. Dorfman. "Active site lysines in orotate phosphoribosyltransferase." Journal of Biological Chemistry 268, no. 27 (September 1993): 20299–304. http://dx.doi.org/10.1016/s0021-9258(20)80728-5.

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36

Tao, Wen, Charles Grubmeyer, and John S. Blanchard. "Transition State Structure ofSalmonella typhimuriumOrotate Phosphoribosyltransferase†." Biochemistry 35, no. 1 (January 1996): 14–21. http://dx.doi.org/10.1021/bi951898l.

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37

Williamson, D. J., M. L. Hooper, and D. W. Melton. "Mouse models of hypoxanthine phosphoribosyltransferase deficiency." Journal of Inherited Metabolic Disease 15, no. 4 (July 1992): 665–73. http://dx.doi.org/10.1007/bf01799622.

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38

Chiba, P., K. Zwiauer, and M. M. Müller. "Characterization of an adenine phosphoribosyltransferase deficiency." Clinica Chimica Acta 172, no. 2-3 (March 1988): 141–47. http://dx.doi.org/10.1016/0009-8981(88)90318-x.

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39

Wang, Pei, Yun-Feng Guan, Wen-Lin Li, Guo-Cai Lu, Jian-Min Liu, and Chao-Yu Miao. "Nicotinamide Phosphoribosyltransferase Facilitates Post-Stroke Angiogenesis." CNS Neuroscience & Therapeutics 21, no. 5 (March 9, 2015): 475–77. http://dx.doi.org/10.1111/cns.12388.

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40

Campillo, Nuria, Hampapathalu A. Nagarajaram, and Indira Ghosh. "Phosphoribosyltransferase superfamily: A comparative structural analysis." Journal of Molecular Modeling 7, no. 4 (May 2001): 80–89. http://dx.doi.org/10.1007/s008940000001.

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41

Colombo, G., D. G. Ribaldone, G. P. Caviglia, A. Genazzani, and C. Travelli. "P072 The involvement of extracellular Nicotinamide Phosphoribosyltransferase (eNAMPT) and Nicotinate Phosphoribosyltransferase (eNAPRT) in inflammatory bowel disease." Journal of Crohn's and Colitis 15, Supplement_1 (May 1, 2021): S175—S176. http://dx.doi.org/10.1093/ecco-jcc/jjab076.201.

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Abstract Background Nicotinamide phosphoribosyltrasferase (NAMPT) is a pleiotropic enzyme which catalyses the first and rate-limiting step in the biosynthesis of NAD. It is present in two different forms: an intracellular form, called iNAMPT, (Chiarugi et al., 2012), and an extracellular form, eNAMPT. eNAMPT is considered an important factor for granulocyte-colony stimulating factor-(G-CSF)-induced myeloid differentiation, with paracrine and autocrine effects on different cell types (i.e. immune and cancer cells), binding TLR4. NAMPT is structurally and functionally related to the enzyme nicotinate phosphoribosyltransferase (iNAPRT), which is rate-limiting in the NAD salvage pathway that starts from nicotinic acid. The NAD biosynthetic pathways controlled by NAMPT and NAPRT are closely interconnected and can compensate for each other. Also, NAPRT is identified as an extracellular ligand (eNAMPRT) for TLR4 and a mediator of inflammation (Managò et al., 2020). Importantly, iNAMPT and eNAMPT levels are increased in several pathologies, included inflammatory bowel disease (IBD). It has been reported that serum eNAMPT levels correlate with the stage of the pathology: in an active state of the disease the levels of NAMPT are very high, however its levels are partially reduced in a remission stage (Moschen et al., 2007). Methods First, we investigated the role of eNAMPT and eNAPRT in murine IBD models (especially in DNBS and DSS model). We took into account phenotypic effect as weight loss and colon shortening, but also the reduction of mRNA of inflammatory genes with RT-PCR, tissue damage with H&E and IHC analysis and systemic and local production through colon explant. Secondly, we determined serum eNAMPT and eNAPRT levels in a cohort of adult IBD patients. Results Both eNAMPT and eNAPRT have been found elevated in 180 IBD patients, as proinflammatory marker of the pathologies. These levels are also elevated in serum and colonic explant of DSS and DNBS preclinical models, associated to an active state of the disease, as a pro-inflammatory response developed locally and systemically. Moreover, we performed ELISA analysis on sera of 100 IBD patients, eligible for anti-TNF treatment, both pediatric and adults. Serum eNAMPT levels are increased before the treatment, responsive patients verified a reduction of these levels, while no-responsive ones verified higher levels. Conclusion eNAMPT and eNAPRT could be considered pro-inflammatory markers of IBD and possible druggable targets.

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42

Dush, M. K., J. M. Sikela, S. A. Khan, J. A. Tischfield, and P. J. Stambrook. "Nucleotide sequence and organization of the mouse adenine phosphoribosyltransferase gene: presence of a coding region common to animal and bacterial phosphoribosyltransferases that has a variable intron/exon arrangement." Proceedings of the National Academy of Sciences 82, no. 9 (May 1, 1985): 2731–35. http://dx.doi.org/10.1073/pnas.82.9.2731.

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43

Gonzalez, Jose E., and Ronald L. Somerville. "The anthranilate aggregate of Escherichia coli: kinetics of inhibition by tryptophan of phosphoribosyltransferase." Biochemistry and Cell Biology 64, no. 7 (July 1, 1986): 681–91. http://dx.doi.org/10.1139/o86-094.

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The kinetic mechanism of the phosphoribosyltransferase reaction is shown to be rapid equilibrium random bi bi with an enzyme–anthranilate–pyrophosphate abortive complex. We present a rate equation that not only predicts the observed kinetic patterns but also accomodates the fact that feedback inhibition is partial, even though tryptophan (Ki = 0.5 μM) and phosphoribosylpyrophosphate (Km = 50 μM) are competitive. Neither ligand completely abolishes the effect of the other. Instead, the binding of one ligand leads to a mutual elevation in the dissociation constant of the opposing ligand by a factor of two to three. Tryptophan inhibition is noncompetitive with respect to anthranilate (Km = 0.58 μM) and does not diminish the rate of interconversion of ternary complexes. Tryptophan cooperativity, with respect to the inhibition of phosphoribosyltransferase, conforms to the concerted Monod–Wyman–Changeux formulation (kinetic Hill coefficient = 2), whereas tryptophan as an inhibitor of anthranilate synthase more closely conforms to a Koshland model of sequential cooperativity with a kinetic Hill coefficient of 1.4. The aggregrate contains only one class of tryptophan sites. Thus the first tryptophan molecule bound to the aggregate maximally inhibits both phosphoribosyltransferase active centers and one of the two anthranilate synthase catalytic sites. The remaining anthranilate synthase subunit thereupon is converted into a form with less (but not zero) affinity for chorismate and a greater affinity for a second molecule of tryptophan.

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Aldritt, S. M., P. Tien, and C. C. Wang. "Pyrimidine salvage in Giardia lamblia." Journal of Experimental Medicine 161, no. 3 (March 1, 1985): 437–45. http://dx.doi.org/10.1084/jem.161.3.437.

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We have found that the anaerobic protozoan parasite Giardia lamblia is incapable of de novo pyrimidine metabolism, as shown by its inability to incorporate orotate, bicarbonate, and aspartate into the pyrimidine nucleotide pool. Results from high performance liquid chromatography of pyrimidine and pyrimidine nucleoside pulse-labeled nucleotide pools and enzyme assays suggest that the parasite satisfies its pyrimidine nucleotide needs predominantly through salvage of uracil by a cytoplasmic uracil phosphoribosyltransferase. Exogenous uridine and cytidine are primarily converted to uracil by the action of uridine hydrolase and cytidine deaminase before incorporation into nucleotide pools. Direct salvage of cytosine occurs to a relatively limited extent via cytosine phosphoribosyltransferase. G. lamblia relies on salvage of exogenous thymidine for ribosylthymine monophosphate (TMP) synthesis, accomplished primarily through the action of a 100,000 g-pelletable thymidine phosphotransferase.

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Pettersson, Jonas, Merry E. Schrumpf, Sandra J. Raffel, Stephen F. Porcella, Cyril Guyard, Kevin Lawrence, Frank C. Gherardini, and Tom G. Schwan. "Purine Salvage Pathways among Borrelia Species." Infection and Immunity 75, no. 8 (May 14, 2007): 3877–84. http://dx.doi.org/10.1128/iai.00199-07.

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ABSTRACT Genome sequencing projects on two relapsing fever spirochetes, Borrelia hermsii and Borrelia turicatae, revealed differences in genes involved in purine metabolism and salvage compared to those in the Lyme disease spirochete Borrelia burgdorferi. The relapsing fever spirochetes contained six open reading frames that are absent from the B. burgdorferi genome. These genes included those for hypoxanthine-guanine phosphoribosyltransferase (hpt), adenylosuccinate synthase (purA), adenylosuccinate lyase (purB), auxiliary protein (nrdI), the ribonucleotide-diphosphate reductase alpha subunit (nrdE), and the ribonucleotide-diphosphate reductase beta subunit (nrdF). Southern blot assays with multiple Borrelia species and isolates confirmed the presence of these genes in the relapsing fever group of spirochetes but not in B. burgdorferi and related species. TaqMan real-time reverse transcription-PCR demonstrated that the chromosomal genes (hpt, purA, and purB) were transcribed in vitro and in mice. Phosphoribosyltransferase assays revealed that, in general, B. hermsii exhibited significantly higher activity than did the B. burgdorferi cell lysate, and enzymatic activity was observed with adenine, hypoxanthine, and guanine as substrates. B. burgdorferi showed low but detectable phosphoribosyltransferase activity with hypoxanthine even though the genome lacks a discernible ortholog to the hpt gene in the relapsing fever spirochetes. B. hermsii incorporated radiolabeled hypoxanthine into RNA and DNA to a much greater extent than did B. burgdorferi. This complete pathway for purine salvage in the relapsing fever spirochetes may contribute, in part, to these spirochetes achieving high cell densities in blood.

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INAGAKI, Kenjiroh, Akihiro MURAOKA, Itsuo SUEHIRO, Masatoshi FUJII, Hirohisa UENO, Tetsuya HOSOOKA, Kazuhisa KIDA, and Keiji MURAKAMI. "Partial Adenine Phosphoribosyltransferase Deficiency Detected by Ureterolithiasis." Internal Medicine 37, no. 1 (1998): 69–72. http://dx.doi.org/10.2169/internalmedicine.37.69.

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Bollée, Guillaume. "Adenine phosphoribosyltransferase deficiency: Leave no stone unturned." World Journal of Clinical Urology 3, no. 3 (2014): 218. http://dx.doi.org/10.5410/wjcu.v3.i3.218.

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Cho, Yoonsang, Vivek Sharma, and James C. Sacchettini. "Crystal Structure of ATP Phosphoribosyltransferase fromMycobacterium tuberculosis." Journal of Biological Chemistry 278, no. 10 (January 2, 2003): 8333–39. http://dx.doi.org/10.1074/jbc.m212124200.

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Grolla, Ambra A., Cristina Travelli, Armando A. Genazzani, and Jaswinder K. Sethi. "Extracellular nicotinamide phosphoribosyltransferase, a new cancer metabokine." British Journal of Pharmacology 173, no. 14 (June 2, 2016): 2182–94. http://dx.doi.org/10.1111/bph.13505.

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Galli, Ubaldina, Cristina Travelli, Alberto Massarotti, Gohar Fakhfouri, Reza Rahimian, Gian Cesare Tron, and Armando A. Genazzani. "Medicinal Chemistry of Nicotinamide Phosphoribosyltransferase (NAMPT) Inhibitors." Journal of Medicinal Chemistry 56, no. 16 (May 31, 2013): 6279–96. http://dx.doi.org/10.1021/jm4001049.

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