In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori

References

• Stayton MM, Rudolph FB, Fromm HJ. Regulation, genetics, and properties of adenylosuccinate synthetase: a review. Curr Top Cell Regul 1983;22:103–41.
   PubMedGoogle Scholar
• Matsuda Y, Ogawa H, Fukutome S, et al. Adenylosuccinate synthetase in rat liver: the existence of two types and their regulatory roles. Biochem Biophys Res Commun 1977;78:766–71.
   PubMed Web of Science ®Google Scholar
• Honzatko RB, Stayton MM, Fromm HJ, Adenylosuccinate synthetase: recent developments. In: Purich DL, editor. Advances in enzymology and related areas of molecular biology. Hoboken (NJ): John Wiley and Sons Inc.; 1999. 57–102 p.
   Google Scholar
• Wang W, Gorrell A, Honzatko R, Fromm HJ. A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer. J Biol Chem 1997;272:7078–84.
   PubMed Web of Science ®Google Scholar
• Honzatko RB, Fromm HJ. Structure-function studies of adenylosuccinate synthetase from Escherichia coli. Arch Biochem Biophys 1999;370:1–8.
   PubMed Web of Science ®Google Scholar
• Rudolph FB, Fromm HJ. Initial rate studies of adenylosuccinate synthetase with product and competitive inhibitors. J Biol Chem 1969;244:3832–9.
   PubMed Web of Science ®Google Scholar
• Raman J, Mehrotra S, Anand RP, Balaram H. Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase. Mol Biochem Parasitol 2004;138:1–8.
   PubMed Web of Science ®Google Scholar
• Wyngaarden JB, Greenland RA. The inhibition of succinoadenylate kinosynthetase of Escherichia coli by adenosine and guanosine 5′-monophosphates. J Biol Chem 1963;238:1054–7.
   PubMed Web of Science ®Google Scholar
• Stayton MM, Fromm HJ. Guanosine 5′-diphosphate-3′-diphosphate inhibition of adenylosuccinate synthetase. J Biol Chem 1979;8:2579–81.
   Google Scholar
• Hou Z, Cashel M, Fromm HJ, Honzatko RB. Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase. J Biol Chem 1999;274:17505–10.
   PubMed Web of Science ®Google Scholar
• Hanessian S, Lu PP, Sancéau JY, et al. An enzyme-bound bisubstrate hybrid inhibitor of adenylosuccinate synthetase. Angew Chem Int Ed Engl 1999;38:3159–62.
   PubMed Web of Science ®Google Scholar
• Iancu CV, Zhou Y, Borza T, et al. Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases. Biochemistry 2006;45:11703–11.
   PubMed Web of Science ®Google Scholar
• Marshall BJ, Warren JR. Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet 1984;1:1311–5.
   PubMed Web of Science ®Google Scholar
• Talebi Bezmin Abadi A. Strategies used by Helicobacter pylori to establish persistent infection. World J Gastroenterol 2017;23:2870–82.
   PubMed Web of Science ®Google Scholar
• Miftahussurur M, Yamaoka Y, Graham DY. Helicobacter pylori as an oncogenic pathogen, revisited. Expert Rev Mol Med 2017;19:1–11.
   Web of Science ®Google Scholar
• Zamani M, Ebrahimtabar F, Zamani V, et al. Systematic review with meta-analysis: the worldwide prevalence of Helicobacter pylori infection. Aliment Pharmacol Ther 2018;47:868–76.
   PubMed Web of Science ®Google Scholar
• Peleteiro B, Bastos A, Ferro A, Lunet N. Prevalence of Helicobacter pylori infection worldwide: a systematic review of studies with national coverage. Dig Dis Sci 2014;59:1698–709.
   PubMed Web of Science ®Google Scholar
• Suzuki H, Mori H. World trends for H. pylori eradication therapy and gastric cancer prevention strategy by H. pylori test-and-treat. J Gastroenterol 2018;53:354–61.
   PubMed Web of Science ®Google Scholar
• Thung I, Aramin H, Vavinskaya V, et al. Review article: the global emergence of Helicobacter pylori antibiotic resistance. Aliment Pharmacol Ther 2016;43:514–33.
   PubMed Web of Science ®Google Scholar
• Tomb JF, White O, Kerlavage AR, et al. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 1997;389:539–47.
   PubMed Web of Science ®Google Scholar
• Doig P, de Jonge BL, Alm RA, et al. Helicobacter pylori physiology predicted from genomic comparison of two strains. Microbiol Mol Biol Rev 1999;63:675–707.
   PubMed Web of Science ®Google Scholar
• Hazell SL, Mendz GL. How Helicobacter pylori works: an overview of the metabolism of Helicobacter pylori. Helicobacter 1997;2:1–12.
   PubMed Web of Science ®Google Scholar
• el Kouni MH. Potential chemotherapeutic targets in the purine metabolism of parasites. Pharmacol Ther 2003;99:283–309.
   PubMed Web of Science ®Google Scholar
• Liechti G, Goldberg JB. Helicobacter pylori relies primarily on the purine salvage pathway for purine nucleotide biosynthesis. J Bacteriol 2012;194:839–54.
   PubMed Web of Science ®Google Scholar
• Narczyk M, Bertoša B, Papa L, et al. Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features. FEBS J 2018;285:1305–25.
   PubMed Web of Science ®Google Scholar
• Štefanić Z, Mikleušević G, Luić M, et al. Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori. Int J Biol Macromol 2017;101:518–26.
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248–54.
   PubMed Web of Science ®Google Scholar
• Hayes D, Laue T, Philo J, Program SEDNTERP: sedimentation interpretation program. Thousand Oaks (CA): Alliance Protein Laboratories; 1995.
   Google Scholar
• Gasteiger E, Hoogland C, Gattiker A, et al. Protein identification and analysis tools on the ExPASy server. In: Walker J, editor. The proteomics protocols handbook. New York (NY): Humana Press; 2005. 571–607 p.
   Google Scholar
• Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 2000;78:1606–19.
   PubMed Web of Science ®Google Scholar
• Britton HTK, Robinson RA. Universal buffer solutions and the dissociation constant of veronal. J Chem Soc 1931;0:1456–62.
   Google Scholar
• Carter CE, Cohen LH. The preparation and properties of adenylosuccinase and adenylosuccinic acid. J Biol Chem 1956;222:17–30.
   PubMed Web of Science ®Google Scholar
• Jayalakshmi R, Sumathy K, Balaram H. Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli. Protein Expr Purif 2002;25:65–72.
   PubMed Web of Science ®Google Scholar
• Kang C, Kim S, Fromm HJ. Subunit complementation of Escherichia coli adenylosuccinate synthetase. J Biol Chem 1996;271:29722–8.
   PubMed Web of Science ®Google Scholar
• Hou Z, Wang W, Fromm HJ, Honzatko RB. IMP alone organizes the active site of adenylosuccinate synthetase from Escherichia coli. J Biol Chem 2002;277:5970–6.
   PubMed Web of Science ®Google Scholar
• Ryzhova TA, Andreichuk YV, Domkin VD. Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae: purification and properties. Biochem (Mosc) 1998;63:650–6.
   PubMed Web of Science ®Google Scholar
• Barton JS. Denaturation at the optimum temperature. Biochem Educ 1979;7:13–14.
   Google Scholar
• Marshall BJ, Barret LJ, Prakash C, et al. Urea protects Helicobacter (Campylobacter) pylori from the bactericidal effect of acid. Gastroenterology 1990;99:697–702.
   PubMed Web of Science ®Google Scholar
• Mehrotra S, Balaram H. Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii. Biochemistry 2007;46:12821–32.
   PubMed Web of Science ®Google Scholar
• Kaczka EA, Gitterman CO, Dulaney EL, Folkers K. Hadacidin, a new growth-inhibitory substance in human tumor systems. Biochemistry 1962;1:340–3.
   PubMed Web of Science ®Google Scholar
• Markham GD, Reed GH. Adenylosuccinate synthetase from Azotobacter vinelandii: purification, properties and steady-state kinetics. Arch Biochem Biophys 1977;184:24–35.
   PubMed Web of Science ®Google Scholar
• Poland BW, Lee SF, Subramanian MV, et al. Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5′-phosphate, GDP, HPO42-, Mg2+, and hadacidin. Biochemistry 1996;35:15753–9.
   PubMed Web of Science ®Google Scholar
• Rudolph FB. Purification, properties, and kinetics of adenylosuccinate synthetase from Escherichia coli [PhD thesis]. Ames (IA): Iowa State University; 1971.
   Google Scholar
• Jahngen EGE, Rossomando EF. Adenylosuccinate synthetase from Dictyostelium discoideum: effects of hadacidin analogs and binding of [14C]hadacidin. Arch Biochem Biophys 1984;229:145–54.
   PubMed Web of Science ®Google Scholar
• Tibrewal N, Elliott GI. Evaluation of hadacidin analogues. Bioorg Med Chem Lett 2011;21:517–9.
   PubMed Web of Science ®Google Scholar
• Sievers F, Wilm A, Dineen DG, et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 2011;7:539–44.
   PubMed Web of Science ®Google Scholar