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Volumn 712, Issue 1-2, 2011, Pages 33-39

Sequence and structural characterization of tbnat gene in isoniazid-resistant Mycobacterium tuberculosis: Identification of new mutations

Author keywords

Drug resistance; Molecular modeling; Mutation; Mycobacterium tuberculosis; Structure function; Tbnat Polymorphism

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; ISONIAZID;

EID: 79957684830     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2011.03.017     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 0000652832 scopus 로고    scopus 로고
    • Genetics of drug resistance in Mycobacterium tuberculosis
    • ASM Press, Washington DC, G.F. Hatfull, W.R. Jacobs (Eds.)
    • Zhang Y., Telenti A. Genetics of drug resistance in Mycobacterium tuberculosis. Molecular Genetics of Mycobacteria 2000, 235-253. ASM Press, Washington DC. G.F. Hatfull, W.R. Jacobs (Eds.).
    • (2000) Molecular Genetics of Mycobacteria , pp. 235-253
    • Zhang, Y.1    Telenti, A.2
  • 2
    • 33750699963 scopus 로고    scopus 로고
    • Mechanisms of action of isoniazid
    • Timmins G.S., Deretic V. Mechanisms of action of isoniazid. Mol. Microbiol. 2006, 62:1220-1227.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1220-1227
    • Timmins, G.S.1    Deretic, V.2
  • 4
    • 0030868749 scopus 로고    scopus 로고
    • Analysis do ahpC gene mutations in isoniazid-reistant clinical isolates of Mycobacterium tuberculosis
    • Kelley C.L., Rouse D.A., Morris S.L. Analysis do ahpC gene mutations in isoniazid-reistant clinical isolates of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 1997, 41:2057-2058.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2057-2058
    • Kelley, C.L.1    Rouse, D.A.2    Morris, S.L.3
  • 6
    • 0034958063 scopus 로고    scopus 로고
    • Novel mutations in ndh in isoniazid-resistant Mycobacterium tuberculosis isolates
    • Lee A.S.G., Teo A.S.M., Wong S.Y. Novel mutations in ndh in isoniazid-resistant Mycobacterium tuberculosis isolates. Antimicrob. Agents Chemother. 2001, 45:2157-2159.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2157-2159
    • Lee, A.S.G.1    Teo, A.S.M.2    Wong, S.Y.3
  • 11
    • 0041332754 scopus 로고    scopus 로고
    • Mycobacterial efflux pumps and chemotherapeutic implications
    • Viveiros M., Leandro C., Amaral L. Mycobacterial efflux pumps and chemotherapeutic implications. Int. J. Antimicrob. Agents 2003, 22:274-278.
    • (2003) Int. J. Antimicrob. Agents , vol.22 , pp. 274-278
    • Viveiros, M.1    Leandro, C.2    Amaral, L.3
  • 12
    • 0034761725 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism
    • Upton A.M., Mushtaq A., Victor T.C., Sampson S.L., Sandy J., Smith D.M., van Helden P.D., Sim E. Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism. Mol. Microbiol. 2001, 42:309-317.
    • (2001) Mol. Microbiol. , vol.42 , pp. 309-317
    • Upton, A.M.1    Mushtaq, A.2    Victor, T.C.3    Sampson, S.L.4    Sandy, J.5    Smith, D.M.6    van Helden, P.D.7    Sim, E.8
  • 14
    • 23944518412 scopus 로고    scopus 로고
    • Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines
    • Sandy J., Mushtaq A., Holton S.J., Schartau P., Noble M.E.M., Sim E. Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines. Biochem. J. 2005, 390:115-123.
    • (2005) Biochem. J. , vol.390 , pp. 115-123
    • Sandy, J.1    Mushtaq, A.2    Holton, S.J.3    Schartau, P.4    Noble, M.E.M.5    Sim, E.6
  • 16
    • 36348945257 scopus 로고    scopus 로고
    • Divergence of cofator recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase
    • Fullam E., Westwood I.M., Anderton M.C., Lowe E.D., Sim E., Noble M.E. Divergence of cofator recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase. J. Mol. Biol. 2008, 375:178-191.
    • (2008) J. Mol. Biol. , vol.375 , pp. 178-191
    • Fullam, E.1    Westwood, I.M.2    Anderton, M.C.3    Lowe, E.D.4    Sim, E.5    Noble, M.E.6
  • 17
    • 0033759301 scopus 로고    scopus 로고
    • An update on genetic, structural and functional studies of arylamine N-acetyltransferase in eucaryotes and prokaryotes
    • Sim E., Payton M., Noble M., Minchin R. An update on genetic, structural and functional studies of arylamine N-acetyltransferase in eucaryotes and prokaryotes. Hum. Mol. Genet. 2000, 9:2435-2441.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2435-2441
    • Sim, E.1    Payton, M.2    Noble, M.3    Minchin, R.4
  • 18
    • 0036042103 scopus 로고    scopus 로고
    • The structure of arylamine N-acetyltranferase from Mycobacterium smegmatis-an enzyme which inactivates the anti-tubercular drug, isoniazid
    • Sandy J., Mushtaq A., Kawamura A., Sinclair J., Sim E., Noble M. The structure of arylamine N-acetyltranferase from Mycobacterium smegmatis-an enzyme which inactivates the anti-tubercular drug, isoniazid. J. Mol. Biol. 2002, 318:1071-1083.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1071-1083
    • Sandy, J.1    Mushtaq, A.2    Kawamura, A.3    Sinclair, J.4    Sim, E.5    Noble, M.6
  • 19
    • 0033019777 scopus 로고    scopus 로고
    • Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance
    • Payton M., Auty R., Delgoda R., Everett M., Sim E. Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance. J. Bacteriol. 1999, 181:1343-1347.
    • (1999) J. Bacteriol. , vol.181 , pp. 1343-1347
    • Payton, M.1    Auty, R.2    Delgoda, R.3    Everett, M.4    Sim, E.5
  • 21
    • 0014622610 scopus 로고
    • Advancesin techniques of testing mycobacterial drug sensivity, and the use of sensivity tests in tuberculosis control programmes
    • Canetti G., Fox W., Khomenko A., Mahler H.T., Menom N.K., Mitchison D.A., Rist N., Smeley N.A. Advancesin techniques of testing mycobacterial drug sensivity, and the use of sensivity tests in tuberculosis control programmes. Bull. WHO 1969, 41:21-43.
    • (1969) Bull. WHO , vol.41 , pp. 21-43
    • Canetti, G.1    Fox, W.2    Khomenko, A.3    Mahler, H.T.4    Menom, N.K.5    Mitchison, D.A.6    Rist, N.7    Smeley, N.A.8
  • 22
    • 0035992072 scopus 로고    scopus 로고
    • Resazurin microtiter assay plate: simple and inexpensive meted for detection of drug resistance in Mycobacterium tuberculosis
    • Palomino J.C., Martin A., Camacho M., Guerra H., Swings J., Portaels F. Resazurin microtiter assay plate: simple and inexpensive meted for detection of drug resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 2002, 46:2720-2722.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2720-2722
    • Palomino, J.C.1    Martin, A.2    Camacho, M.3    Guerra, H.4    Swings, J.5    Portaels, F.6
  • 24
    • 0031057723 scopus 로고    scopus 로고
    • Genotypic assessment of isoniazid and rifampin resistance in Mycobacterium tuberculosis: a blind study at reference laboratory level
    • Telenti A., Honoré N., Bernasconi C., March J., Ortega A., Heym B., Takiff H.E., Cole S.T. Genotypic assessment of isoniazid and rifampin resistance in Mycobacterium tuberculosis: a blind study at reference laboratory level. J. Clin. Microbiol. 1997, 35:719-723.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 719-723
    • Telenti, A.1    Honoré, N.2    Bernasconi, C.3    March, J.4    Ortega, A.5    Heym, B.6    Takiff, H.E.7    Cole, S.T.8
  • 28
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen M.Y., Sali A. Statistical potential for assessment and prediction of protein structures. Protein Sci. 2006, 15:2507-2512.
    • (2006) Protein Sci. , vol.15 , pp. 2507-2512
    • Shen, M.Y.1    Sali, A.2
  • 30
    • 77954584856 scopus 로고    scopus 로고
    • Thrombin allosteric modulation revisited: a molecular dynamics study
    • de Amorim H.L., Netz P.A., Guimarães J.A. Thrombin allosteric modulation revisited: a molecular dynamics study. J. Mol. Model. 2010, 16:725-735.
    • (2010) J. Mol. Model. , vol.16 , pp. 725-735
    • de Amorim, H.L.1    Netz, P.A.2    Guimarães, J.A.3
  • 31
    • 0031943169 scopus 로고    scopus 로고
    • Differentiation of Mycobacterium ulcerans, M. marinum, and M. haemophilum: mapping of their relationships to M. tuberculosis by fatty acid profile analysis, DNA-DNA hybridization, and 16S rRNA gene sequence analysis
    • Tonjum T., Welty D.B., Jantzen E., Small P.L. Differentiation of Mycobacterium ulcerans, M. marinum, and M. haemophilum: mapping of their relationships to M. tuberculosis by fatty acid profile analysis, DNA-DNA hybridization, and 16S rRNA gene sequence analysis. J. Clin. Microbiol. 1998, 36:918-925.
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 918-925
    • Tonjum, T.1    Welty, D.B.2    Jantzen, E.3    Small, P.L.4
  • 32
    • 70349454045 scopus 로고    scopus 로고
    • Comparison of the arylamine N-acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis
    • Fullam E., Kawamura A., Wilkinson H., Abuhammad A., Westwood I., Sim E. Comparison of the arylamine N-acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis. Protein J. 2009, 28:281-293.
    • (2009) Protein J. , vol.28 , pp. 281-293
    • Fullam, E.1    Kawamura, A.2    Wilkinson, H.3    Abuhammad, A.4    Westwood, I.5    Sim, E.6
  • 33
    • 14144256365 scopus 로고    scopus 로고
    • Binding of the anti-tubercular drug isoniazid to the arilamine N-acetyltransferase protein from Mycobacterium smegmatis
    • Sandy J., Holton S., Fullam E., Sim E., Noble M. Binding of the anti-tubercular drug isoniazid to the arilamine N-acetyltransferase protein from Mycobacterium smegmatis. Protein Sci. 2005, 14:775-782.
    • (2005) Protein Sci. , vol.14 , pp. 775-782
    • Sandy, J.1    Holton, S.2    Fullam, E.3    Sim, E.4    Noble, M.5
  • 35
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie J.U., Luthy R., Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science 1991, 253:164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 36
    • 0027180507 scopus 로고
    • Verification of protein structures: patterns of nonbonded atomic interactions
    • Colovos C., Yeates T.O. Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 1993, 2:1511-1519.
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 38
    • 0037023704 scopus 로고    scopus 로고
    • The COOH terminus of arylamine N-acetyltransferase from Salmonella typhimurium controls enzymic activity
    • Mushtaq A., Payton M., Sim E. The COOH terminus of arylamine N-acetyltransferase from Salmonella typhimurium controls enzymic activity. J. Biol. Chem. 2002, 277:12175-12181.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12175-12181
    • Mushtaq, A.1    Payton, M.2    Sim, E.3
  • 39
    • 33745619224 scopus 로고    scopus 로고
    • Public health impact of isoniazid-resistant Mycobacterium tuberculosis strains with a mutation at amino-acid position 315 of katG: a decade of experience in The Netherlands
    • van Doorn H.R., de Haas P.E.W., Kremer K., Vandenbroucke-Grauls C.M.J., Borgdorff M.W., van Soolingen D. Public health impact of isoniazid-resistant Mycobacterium tuberculosis strains with a mutation at amino-acid position 315 of katG: a decade of experience in The Netherlands. Clin. Microbiol. Infect. 2006, 12:769-775.
    • (2006) Clin. Microbiol. Infect. , vol.12 , pp. 769-775
    • van Doorn, H.R.1    de Haas, P.E.W.2    Kremer, K.3    Vandenbroucke-Grauls, C.M.J.4    Borgdorff, M.W.5    van Soolingen, D.6
  • 40
    • 53249149273 scopus 로고    scopus 로고
    • Kinetic and chemical mechanism of arylamine n-acetyltransferase from Mycobacterium tuberculosis
    • Sikora A.L., Frankel B.A., Blanchard J.S. Kinetic and chemical mechanism of arylamine n-acetyltransferase from Mycobacterium tuberculosis. Biochemistry 2008, 47:10781-10789.
    • (2008) Biochemistry , vol.47 , pp. 10781-10789
    • Sikora, A.L.1    Frankel, B.A.2    Blanchard, J.S.3
  • 41
    • 33646227714 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis complex genetic diversity: mining the fourth international spoligotyping database (SpolDB4) for classification, population genetics and epidemiology
    • Brudey K., Driscoll J.R., Rilgouts L., Prodinger W.N., Gori A., Al-Hajoi S.A., Allix C., Aristimuno L., et al. Mycobacterium tuberculosis complex genetic diversity: mining the fourth international spoligotyping database (SpolDB4) for classification, population genetics and epidemiology. BMC Microbiol. 2006, 6.
    • (2006) BMC Microbiol. , vol.6
    • Brudey, K.1    Driscoll, J.R.2    Rilgouts, L.3    Prodinger, W.N.4    Gori, A.5    Al-Hajoi, S.A.6    Allix, C.7    Aristimuno, L.8
  • 42
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. 1991, 47:392-400.
    • (1991) Acta Crystallogr. , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2


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