Synthesis and biochemical evaluation of selective inhibitors of class II fructose bisphosphate aldolases: Towards new synthetic antibiotics

Chemistry - A European Journal

Volumn 14, Issue 28, 2008, Pages 8521-8529

  Fonvielle, Matthieu ^a   Coinçon, Mathieu ^b   Daher, Racha ^a   Desbenoit, Nicolas ^a   Kosieradzka, Katarzyna ^a   Barilone, Nathalie ^c   Gicquel, Brigitte ^c   Sygusch, Jurgen ^b   Jackson, Mary ^c   Therisod, Michel ^a  

^a UNIVERSITÉ PARIS SUD   (France)

^b UNIVERSITÉ DE MONTRÉAL   (Canada)

^c INSTITUT PASTEUR   (France)

Author keywords

Aldolases; Antibiotics; Bioorganic chemistry; Enzyme inhibitors

Indexed keywords

CRYSTALLOGRAPHY; FRUCTOSE; MINERALOGY; ZINC;

ALDOLASES; ANTIBIOTICS; BIOORGANIC CHEMISTRY; ENZYME INHIBITORS;

COMPLEXATION;

ANTIINFECTIVE AGENT; ENZYME INHIBITOR; FRUCTOSE BISPHOSPHATE ALDOLASE;

ARTICLE; CHEMICAL STRUCTURE; CRYSTALLOGRAPHY; DRUG ANTAGONISM; DRUG EFFECT; MICROBIOLOGICAL EXAMINATION; MYCOBACTERIUM TUBERCULOSIS; SYNTHESIS;

ANTI-BACTERIAL AGENTS; CRYSTALLOGRAPHY; ENZYME INHIBITORS; FRUCTOSE-BISPHOSPHATE ALDOLASE; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS;

EID: 53849138071     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200800857     Document Type: Article

References (39)

1. P. Lochhead, E. M. El-Omar, Best Pract. Res. Clin. Gastroenterol. 2007, 21, 281-297.
2. a) Global Alliance for TB Drug Development Scientific Blueprint for TB Drug Development. Tuberculosis 2001, 81, 1-52;
3. b) WHO web site: http://www.who.int/.
4. M.-A. Alberti. J. R. Haanstra, V. Hannaert. J. van Roy, F. Opperdoes, B. M. Bakker, P. A. Michels, J. Biol. Chem. 2005, 280, 28306-28315.
5. D. J. Lewis, G. Lowe, J. Chem. Soc. Chem. Commun. 1973, 713-715.
6. S. Y. Gerdes, M. D. Scholle, J. W. Campbell, G. Balázsi, E. Ravasz, M. D. Daugherty, A. L. Somera. N. C. Kyrpides. I. Anderson. M. S. Gelfand. A. Bhattacharya, V. Kapatral, M. D'Souza, M. V. Baev, Y. Grechkin, F. Mseeh, M. Y. Fonstein, R. Overbeek, A.-L. Barabási, Z. N. Oltvai, A. L. Osterman, J. Bacteriol. 2003, 185, 5673-5684.
7. U. F. Wehmeier, FEMS Microbiol. Lett. 2001, 197, 53-58.
8. M. Singer, P. Rossmiessl, B. M. Cali, H. Liebke, C. A. Gross, J. Bacteriol. 1991, 173, 6242-6248.
9. M. Singer, W. A. Walter, B. M. Cali, P. Rouviere, H. H. Liebke, R. L. Gourse, C. A. Gross, J. Bacterial. 1991, 173, 6249-6257.
10. N. J. Bai, M. R. Pai, P. S. Murthy, T. A. Venkilasubramanian. FEBS Lett. 1974, 45, 68-70.
11. N. J. Bai, M. R. Pai, P. S. Murthy. T. A. Venkitasubramanian, Methods Enzymol. 1982, 90, 241-250.
12. P. C. Ramsaywak, G. Labbé, S. Siemann, G. I. Dmitrienko, J. G. Guillemelte, Protein Expression Purif. 2004, 37, 220-228.
13. I. Rosenkrands, R. A. Slayden, J. Crawford, C. Aagaard, C. E. Barry. III, P. Andersen, J. Bacteriol. 2002, 184, 3485-3491.
14. T. Gefflaut, C. Blonski, J. Perie. M. Willson, Prog. Biophys. Mol. Biol. 1995, 63, 301 -340.
15. K. D. Collins, J. Biol. Chem. 1974, 249, 136-142.
16. M. K. Dreyer. G. E. Schulz. J. Mol. Biol. 1996, 259, 458-466.
17. M. Fonvielle, P. Weber, K. Dabkowska, M. Therisod, Bioorg. Med. Chem. Lett. 2004, 14, 2923-2926.
18. D. R. Hall, G. A. Leonard, C. D. Reed, C. I. Walt, A. Berry, W. N. Hunter, J. Mol. Biol. 1999, 287, 383-394.
19. D. R. Hall, L. E. Kemp, G. A. Leonard, K. M. Arshal, A. Berry, W. N. Hunter. Acta Crystallogr. Sect. D 2003, 59, 611 -614.
20. The structure of PGH bound to H. pylori Fba was determined to 2.3 Å resolution (see Supporting Information) and is structurally isomorphous with that of the H. pylori Fba complex formed with 2 (RMSD 0.26 Å based on superposition of all Cα atoms)
21. G. T. Marks, T. K. Harris, M. A. Massiah, A. S. Mildvan, Biochemistry 2001, 40, 6805-6818.
22. Z. Zhang, S. Sugio, E. A. Komives, K. D. Liu, J. R. Knowles, G. A. Petsko, D. Ringe. Biochemistry 1994, 33, 2830-2837.
23. A. Martin, M. Camacho, F. Portaels, J.-C. Palomino. Antimicrob. Agents Chemother. 2003, 47, 3616-3619.
24. W. L. DeLano, 2004, DeLano Scientific, LLC, San Carlos, CA.
25. C. F. Midelfort, R. K. Gupta, I. A. Rose, Biochemistry 1976, 15, 2178-2185.
26. M. St. -Jean, J. Lafrance-Vanasse, B. Liotard, J. Sygusch J. Biol. Chem. 2005, 280, 27262-27270.
27. N. S. Blom, S. Tétrault, R. Coulombe, J. Sygusch. Nat. Struct. Biol. 1996, 3, 856-862.
28. Z. Otwinowski, W. Minor. Methods Mol. Med. Methods. Enzymol. 1997, 276, 307-326.
29. J. Navaza. Acta Crystalogr. Sect D. 2001, 57, 1367-1372.
30. A. Fiser, R. K. Do, A. Sali, Prot. Sci. 2000, 9, 1753-1773.
31. T. Izard, J. Sygusch, J. Biol. Chem. 2004, 279, 11825-11833.
32. A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, N. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson, G. L. Warren, Acta Crystallogr. Sect. A 1998, 54, 905-921.
33. T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. Sect. A 1991, 47, 110-119.
34. P. D. Adams, R. W. Grosse-Kunstleve, L.-W. Hung, T. R. lorger, A. J. McCoy, N. W. Moriarty, R. J. Read, J. C. Sacchetini, N. K. Sauter, T. C. Acta Crystallogr., Sect D. 2002, 58, 1948-1954.
35. P. Emsley, K. Cowtan, Acta Crystallogr. Sect. A 2004, 60, 2126-2132.
36. S. C. Lowell, I. W. Davis, W. B. Arendall, III, P. I. W. de Bakker, J. M. Word, M. G. Prisant, J. S. Richardson, D. C. Richardson. Proteins Struct. Funct. Bioinf. 2003, 50, 437-450.
37. R. A. Laskowski, M. W. McArthur, D. S. Moss, J. M. Thornton J. Appl. Crystalog. E. 1993, 26, 283-291.
38. Protein Data Bank, research collaboratory for structural bioinformatics. Rutgers University, New Brunswick, NJ; http://www.rcsb.org/
39. W. J. Ruller, J. R. Hunsley, Methods Enzymol. 1966, 9, 480-486.