Potent inhibitors of a shikimate pathway enzyme from Mycobacterium tuberculosis: Combining mechanism- and modeling-based design

Journal of Biological Chemistry

Volumn 286, Issue 18, 2011, Pages 16197-16207

  Reichau, Sebastian ^a   Jiao, Wanting ^a   Walker, Scott R ^a   Hutton, Richard D ^a   Baker, Edward N ^b   Parker, Emily J ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; CATALYTIC MECHANISMS; CONFORMATIONAL CHANGE; ENZYME REACTION; GLOBAL HEALTH; INHIBITOR COMPLEX; INHIBITORY CONSTANTS; M. TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS; NANOMOLAR RANGE; POTENT INHIBITOR; RESISTANT STRAINS; SHIKIMATE PATHWAY; SYNTHASES; TETRAHEDRAL INTERMEDIATES; WATER MOLECULE;

BIOCHEMISTRY; CATALYSIS; CONDENSATION REACTIONS; CRYSTAL STRUCTURE; ENZYMES; HEALTH RISKS;

REACTION INTERMEDIATES;

3 DEOXY 7 PHOSPHOHEPTULONATE SYNTHASE; ENZYME INHIBITOR; PHOSPHOENOLPYRUVATE; SHIKIMIC ACID;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SYNTHESIS; MOLECULAR MODEL; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

ALCOHOL OXIDOREDUCTASES; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; ENZYME INHIBITORS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, TERTIARY; SHIKIMIC ACID; STRUCTURE-ACTIVITY RELATIONSHIP; TUBERCULOSIS;

MYCOBACTERIUM TUBERCULOSIS;

EID: 79955527616     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.211649     Document Type: Article

References (49)

1. Sharma, S. K., and Mohan, A. (2006) Chest 130, 261-272
2. Meya, D. B., and McAdam, K. P. (2007) J. Intern. Med. 261, 309-329
3. World Health Organization (2009). Global Tuberculosis Control: Epidemiology, Strategy, and Financing, WHO Report 2009, pp. 6-33, WHO Press, Geneva
4. Barry, C. E., 3rd, and Blanchard, J. S. (2010) Curr. Opin. Chem. Biol. 14, 456-466
5. Campbell, S. A., Richards, T. A., Mui, E. J., Samuel, B. U., Coggins, J. R., McLeod, R., and Roberts, C. W. (2004) Int. J. Parasitol. 34, 5-13
6. Roberts, F., Roberts, C. W., Johnson, J. J., Kyle, D. E., Krell, T., Coggins, J. R., Coombs, G. H., Milhous, W. K., Tzipori, S., Ferguson, D. J., Chakrabarti, D., and McLeod, R. (1998) Nature 393, 801-805
7. Bentley, R. (1990) Crit. Rev. Biochem. Mol. Biol. 25, 307-384
8. Sikorski, J. A., and Gruys, K. J. (1997) Acc. Chem. Res. 30, 2-8
9. Schönbrunn, E., Eschenburg, S., Shuttleworth, W. A., Schloss, J. V., Amrhein, N., Evans, J. N., and Kabsch, W. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 1376-1380
10. Parish, T., and Stoker, N. G. (2002) Microbiology 148, 3069-3077
11. Schofield, L. R., Anderson, B. F., Patchett, M. L., Norris, G. E., Jameson, G. B., and Parker, E. J. (2005) Biochemistry 44, 11950-11962
12. Williamson, R. M., Pietersma, A. L., Jameson, G. B., and Parker, E. J. (2005) Bioorg. Med. Chem. Lett. 15, 2339-2342
13. DeLeo, A. B., Dayan, J., and Sprinson, D. B. (1973) J. Biol. Chem. 248, 2344-2353
14. Shumilin, I. A., Bauerle, R., and Kretsinger, R. H. (2003) Biochemistry 42, 3766-3776
15. Wagner, T., Shumilin, I. A., Bauerle, R., and Kretsinger, R. H. (2000) J. Mol. Biol. 301, 389-399
16. König, V., Pfeil, A., Braus, G. H., and Schneider, T. R. (2004) J. Mol. Biol. 337, 675-690
17. Ray, P. H. (1980) J. Bacteriol. 141, 635-644
18. Kona, F., Xu, X., Martin, P., Kuzmic, P., and Gatti, D. L. (2007) Biochemistry 46, 4532-4544
19. Kona, F., Tao, P., Martin, P., Xu, X., and Gatti, D. L. (2009) Biochemistry 48, 3610-3630
20. Ahn, M., Pietersma, A. L., Schofield, L. R., and Parker, E. J. (2005) Org. Biomol. Chem. 3, 4046-4049
21. Webby, C. J., Baker, H. M., Lott, J. S., Baker, E. N., and Parker, E. J. (2005) J. Mol. Biol. 354, 927-939
22. Webby, C. J., Jiao, W., Hutton, R. D., Blackmore, N. J., Baker, H. M., Baker, E. N., Jameson, G. B., and Parker, E. J. (2010) J. Biol. Chem. 285, 30567-30576
23. Webby, C. J., Lott, J. S., Baker, H. M., Baker, E. N., and Parker, E. J. (2005) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61, 403-406
24. Hartmann, M., Schneider, T. R., Pfeil, A., Heinrich, G., Lipscomb, W. N., and Braus, G. H. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 862-867
25. Webby, C. J., Patchett, M. L., and Parker, E. J. (2005) Biochem. J. 390, 223-230
26. Sasso, S., Okvist, M., Roderer, K., Gamper, M., Codoni, G., Krengel, U., and Kast, P. (2009) EMBO J. 28, 2128-2142
27. Walker, S. R., Cumming, H., and Parker, E. J. (2009) Org. Biomol. Chem. 7, 3031-3035
28. Walker, S. R., and Parker, E. J. (2006) Bioorg. Med. Chem. Lett. 16, 2951-2954
29. Grison, C., Petek, S., Finance, C., and Coutrot, P. (2005) Carbohydr. Res. 340, 529-537
30. Collaborative Computational Project Number 4 (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
31. Schüttelkopf, A. W., and van Aalten, D. M. F. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363
32. Schoner, R., and Herrmann, K. M. (1976) J. Biol. Chem. 251, 5440-5447
33. Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) Anal. Biochem. 100, 95-97
34. Schrödinger, LLC (2005) MacroModel, Version 9.1, Schrödinger, LLC, New York
35. Schrödinger, LLC (2005) Maestro, Version 7.5, Schrödinger, LLC, New York
36. Schrödinger, LLC (2005) Schrödinger Suite 2006 Induced Fit Protocol, Prime version 1.5, Schrödinger, LLC, New York
37. Schrödinger, LLC (2005) Glide, Version 4.0, Schrodinger, LLC, New York
38. Armarego, W. L., and Chai, C. (2003). Purification of Laboratory Chemicals, 5th Ed., Butterworth-Heinemann, Oxford
39. Dess, D. B., and Martin, J. C. (1991) J. Am. Chem. Soc. 113, 7277-7287
40. Ireland, R. E., and Liu, L. (1993) J. Org. Chem. 58, 2899-2899
41. Grison, C., Coutrot, F., Comoy, C., Lemilbeau, C., and Coutrot, P. (2000) Tetrahedron Lett. 41, 6571-6574
42. Petit, Y., and Larcheveque, M. (1998) Org. Synth. 75, 37-44
43. Friis, G. J., and Bundgaard, H. (1996) Eur. J. Pharm. Sci. 4, 49-59
44. Schultz, C. (2003) Bioorg. Med. Chem. 11, 885-898
45. Hecker, S. J., and Erion, M. D. (2008) J. Med. Chem. 51, 2328-2345
46. Wang, J., Duewel, H. S., Woodard, R. W., and Gatti, D. L. (2001) Biochemistry 40, 15676-15683
47. Shumilin, I. A., Bauerle, R., Wu, J., Woodard, R. W., and Kretsinger, R. H. (2004) J. Mol. Biol. 341, 455-466
48. McPhillips, T. M., McPhillips, S. E., Chiu, H. J., Cohen, A. E., Deacon, A. M., Ellis, P. J., Garman, E., Gonzalez, A., Sauter, N. K., Phizackerley, R. P., Soltis, S. M., and Kuhn, P. (2002) J. Synchrotron Rad. 9, 401-406
49. Walker, S. R., Jiao, W., and Parker, E. J. (2011) Bioorg. Med. Chem. Lett., 10:10.1016/j.bmcl.2011.03.071