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Volumn 276, Issue 1, 2009, Pages 144-154

A novel inhibitor of indole-3-glycerol phosphate synthase with activity against multidrug-resistant Mycobacterium tuberculosis

Author keywords

Drug resistance; Indole 3 glycerol phosphate synthase; Inhibitor; Mycobacterium tuberculosis

Indexed keywords

ASPARAGINE; ATB 107; GLUTAMIC ACID; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE INHIBITOR; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 57649146532     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06763.x     Document Type: Article
Times cited : (30)

References (39)
  • 1
    • 0034161411 scopus 로고    scopus 로고
    • Disintegrating health services and resurgent tuberculosis in post-soviet Tajikistan: An example of structural violence
    • Keshavjee S Becerra MC (2000) Disintegrating health services and resurgent tuberculosis in post-soviet Tajikistan: an example of structural violence. JAMA 283, 1201.
    • (2000) JAMA , vol.283 , pp. 1201
    • Keshavjee, S.1    Becerra, M.C.2
  • 2
    • 39049161926 scopus 로고    scopus 로고
    • Preclinical testing of new drugs for tuberculosis: Current challenges
    • Lenaerts A, Degroote M Orme I (2008) Preclinical testing of new drugs for tuberculosis: current challenges. Trends Microbiol 16, 48 54.
    • (2008) Trends Microbiol , vol.16 , pp. 48-54
    • Lenaerts, A.1    Degroote, M.2    Orme, I.3
  • 4
    • 0035145539 scopus 로고    scopus 로고
    • Characterization of auxotrophic mutants of Mycobacterium tuberculosis and their potential as vaccine candidates
    • Smith DA, Parish T, Stoker NG Bancroft GJ (2001) Characterization of auxotrophic mutants of Mycobacterium tuberculosis and their potential as vaccine candidates. Infect Immun 69, 1142 1150.
    • (2001) Infect Immun , vol.69 , pp. 1142-1150
    • Smith, D.A.1    Parish, T.2    Stoker, N.G.3    Bancroft, G.J.4
  • 5
    • 29144495844 scopus 로고    scopus 로고
    • The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate
    • Lee CE, Goodfellow C, Javid-Majd F, Baker EN Lott JS (2006) The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate. J Mol Biol 355, 784 797.
    • (2006) J Mol Biol , vol.355 , pp. 784-797
    • Lee, C.E.1    Goodfellow, C.2    Javid-Majd, F.3    Baker, E.N.4    Lott, J.S.5
  • 6
    • 0014028006 scopus 로고
    • Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon
    • Creighton TE Yanofsky C (1966) Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J Biol Chem 241, 4616 4624.
    • (1966) J Biol Chem , vol.241 , pp. 4616-4624
    • Creighton, T.E.1    Yanofsky, C.2
  • 7
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH Rubin EJ (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48, 77 84.
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 9
    • 0032146301 scopus 로고    scopus 로고
    • Structure-based drug design
    • Amzel L (1998) Structure-based drug design. Curr Opin Biotechnol 9, 366 369.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 366-369
    • Amzel, L.1
  • 10
    • 0028297112 scopus 로고
    • Application of the three-dimensional structures of protein target molecules in structure-based drug design
    • Greer J, Erickson J, Baldwin J Varney M (1994) Application of the three-dimensional structures of protein target molecules in structure-based drug design. J Med Chem 37, 1035 1054.
    • (1994) J Med Chem , vol.37 , pp. 1035-1054
    • Greer, J.1    Erickson, J.2    Baldwin, J.3    Varney, M.4
  • 12
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese J, Smith P, Sollis SL, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL Colman PM (1998) Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 6, 735 746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.1    Smith, P.2    Sollis, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkin, J.L.6    Colman, P.M.7
  • 13
    • 0018392983 scopus 로고
    • Aromatic amino acid biosynthesis: Regulation of shikimate kinase in Escherichia coli K-12
    • Ely B Pittard J (1979) Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12. J Bacteriol 138, 933 943.
    • (1979) J Bacteriol , vol.138 , pp. 933-943
    • Ely, B.1    Pittard, J.2
  • 14
    • 0036308014 scopus 로고    scopus 로고
    • The catalytic mechanism of indole-3-glycerol phosphate synthase: Crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product
    • Hennig M, Darimont BD, Jansonius JN Kirschner K (2002) The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product. J Mol Biol 319, 757 766.
    • (2002) J Mol Biol , vol.319 , pp. 757-766
    • Hennig, M.1    Darimont, B.D.2    Jansonius, J.N.3    Kirschner, K.4
  • 16
    • 0022336792 scopus 로고
    • Calculation of protein conformations by proton-proton distance constraints: A new efficient algorithm
    • Braun W Gõ N (1985) Calculation of protein conformations by proton-proton distance constraints: a new efficient algorithm. J Mol Biol 186, 611 626.
    • (1985) J Mol Biol , vol.186 , pp. 611-626
    • Braun, W.1    Gõ, N.2
  • 18
    • 0037396345 scopus 로고    scopus 로고
    • Evolution of function in (alpha/beta)8-barrel
    • Gerlt J Raushel F (2003) Evolution of function in (alpha/beta)8-barrel. Enzymes 7, 252 264.
    • (2003) Enzymes , vol.7 , pp. 252-264
    • Gerlt, J.1    Raushel, F.2
  • 19
    • 0036701947 scopus 로고    scopus 로고
    • Simple and rapid differentiation of Mycobacterium tuberculosis H37Ra from M. tuberculosis clinical isolates through two cytochemical tests using neutral red and nile blue stains
    • Soto CY, Andreu N, Gibert I Luquin M (2002) Simple and rapid differentiation of Mycobacterium tuberculosis H37Ra from M. tuberculosis clinical isolates through two cytochemical tests using neutral red and nile blue stains. J Clin Microbiol 40, 3021 3024.
    • (2002) J Clin Microbiol , vol.40 , pp. 3021-3024
    • Soto, C.Y.1    Andreu, N.2    Gibert, I.3    Luquin, M.4
  • 20
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C, Lombardo F, Dominy B Feeney P (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 46, 3 26.
    • (2001) Adv Drug Deliv Rev , vol.46 , pp. 3-26
    • Lipinski, C.1    Lombardo, F.2    Dominy, B.3    Feeney, P.4
  • 23
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B Spoel DVD (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Mod 7, 306 317.
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Spoel, D.V.D.3
  • 25
    • 84906391926 scopus 로고
    • Temperature and size dependence for Monte Carlo simulations of TIP4P water
    • Jorgensen WL Madura JD (1985) Temperature and size dependence for Monte Carlo simulations of TIP4P water. Mol Phys 56, 1381 1392.
    • (1985) Mol Phys , vol.56 , pp. 1381-1392
    • Jorgensen, W.L.1    Madura, J.D.2
  • 28
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen H Fraaije J (1997) LINCS: a linear constraint solver for molecular simulations. J Comp Chem 18, 1463 1472.
    • (1997) J Comp Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.3    Fraaije, J.4
  • 30
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell DS Olson AJ (1990) Automated docking of substrates to proteins by simulated annealing. Proteins 8, 195 202.
    • (1990) Proteins , vol.8 , pp. 195-202
    • Goodsell, D.S.1    Olson, A.J.2
  • 32
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • Aalten DMF, Bywater R, Findlay JBC, Hendlich M, Hooft RWW Vriend G (1996) PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J Comput Aided Mol Des 10, 255 262.
    • (1996) J Comput Aided Mol des , vol.10 , pp. 255-262
    • Aalten, D.M.F.1    Bywater, R.2    Findlay, J.B.C.3    Hendlich, M.4    Hooft, R.W.W.5    Vriend, G.6
  • 33
    • 0026332547 scopus 로고
    • Eletrostatic effects in proteins: Comparison of dielectric and charge models
    • Mehler EL Solmajer T (1991) Eletrostatic effects in proteins: comparison of dielectric and charge models. Protein Eng 4, 903 910.
    • (1991) Protein Eng , vol.4 , pp. 903-910
    • Mehler, E.L.1    Solmajer, T.2
  • 34
    • 0019504490 scopus 로고
    • Evaluation of rapid radiometric method for drug susceptibility testing of Mycobacterium tuberculosis
    • Siddiqi SH, Libonati JP Middlebrook G (1981) Evaluation of rapid radiometric method for drug susceptibility testing of Mycobacterium tuberculosis. J Clin Microbiol 13, 908 912.
    • (1981) J Clin Microbiol , vol.13 , pp. 908-912
    • Siddiqi, S.H.1    Libonati, J.P.2    Middlebrook, G.3
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, McRorie RA Williams WL (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1    McRorie, R.A.2    Williams, W.L.3
  • 36
    • 0023084230 scopus 로고
    • Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli
    • Kirschner K, Szadkowski H, Jardetzky TS Hager V (1987) Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli. Methods Enzymol 142, 386 397.
    • (1987) Methods Enzymol , vol.142 , pp. 386-397
    • Kirschner, K.1    Szadkowski, H.2    Jardetzky, T.S.3    Hager, V.4
  • 37
    • 0030906459 scopus 로고    scopus 로고
    • Stability of a thermophilic TIM-barrel enzyme: Indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus
    • Anderotti G, Cubellis MV, Palo MD, Fessas D, Sannia G Marino G (1997) Stability of a thermophilic TIM-barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus. Biochem J 323, 259 264.
    • (1997) Biochem J , vol.323 , pp. 259-264
    • Anderotti, G.1    Cubellis, M.V.2    Palo, M.D.3    Fessas, D.4    Sannia, G.5    Marino, G.6
  • 38
    • 0037540410 scopus 로고    scopus 로고
    • Nonsequential unfolding of the beta/alpha barrel protein indole-3-glycerol-phosphate synthase
    • Pino MMS Fersht AR (1997) Nonsequential unfolding of the beta/alpha barrel protein indole-3-glycerol-phosphate synthase. Biochemistry 36, 5560 5565.
    • (1997) Biochemistry , vol.36 , pp. 5560-5565
    • Pino, M.M.S.1    Fersht, A.R.2
  • 39
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41, 95 98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1


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