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Volumn 2, Issue 8, 2016, Pages 579-591

Structure of the Essential Mtb FadD32 Enzyme: A Promising Drug Target for Treating Tuberculosis

Author keywords

FadD32; fatty acyl AMP ligase; Mycobacterium tuberculosis; mycolic acid biosynthesis

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIAL ENZYME; LIGAND; MYCOBACTERIUM TUBERCULOSIS FADD32 PROTEIN; UNCLASSIFIED DRUG;

EID: 85006210861     PISSN: None     EISSN: 23738227     Source Type: Journal    
DOI: 10.1021/acsinfecdis.6b00082     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 85006183839 scopus 로고    scopus 로고
    • WHO | Tuberculosismortality nearly halved since 1990. (accessed May 11)
    • WHO | Tuberculosismortality nearly halved since 1990. http://www.who.int/mediacentre/news/releases/2015/tuberculosis-mortality/en/ (accessed May 11, 2016).
    • (2016)
  • 2
    • 84923172431 scopus 로고    scopus 로고
    • Heterogeneity in tuberculosis pathology, microenvironments and therapeutic responses
    • Lenaerts, A., Barry, C. E., and Dartois, V. (2015) Heterogeneity in tuberculosis pathology, microenvironments and therapeutic responses Immunol. Rev. 264, 288-307 10.1111/imr.12252
    • (2015) Immunol. Rev. , vol.264 , pp. 288-307
    • Lenaerts, A.1    Barry, C.E.2    Dartois, V.3
  • 3
    • 84894068321 scopus 로고    scopus 로고
    • The path of anti-tuberculosis drugs: From blood to lesions to mycobacterial cells
    • Dartois, V. (2014) The path of anti-tuberculosis drugs: from blood to lesions to mycobacterial cells Nat. Rev. Microbiol. 12, 159-67 10.1038/nrmicro3200
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 159-167
    • Dartois, V.1
  • 5
    • 85006203346 scopus 로고    scopus 로고
    • WHO | Antimicrobial resistance: globalreport on surveillance 2014. (accessed May 11)
    • WHO | Antimicrobial resistance: globalreport on surveillance 2014. http://www.who.int/drugresistance/documents/surveillancereport/en/ (accessed May 11, 2016).
    • (2016)
  • 6
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama, K., Wang, C., and Besra, G. S. (2005) Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis Clin. Microbiol. Rev. 18, 81-101 10.1128/CMR.18.1.81-101.2005
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 7
    • 84892635980 scopus 로고    scopus 로고
    • Mycolic acids: Structures, biosynthesis, and beyond
    • Marrakchi, H., Lanéelle, M.-A., and Daffé, M. (2014) Mycolic acids: structures, biosynthesis, and beyond Chem. Biol. 21, 67-85 10.1016/j.chembiol.2013.11.011
    • (2014) Chem. Biol. , vol.21 , pp. 67-85
    • Marrakchi, H.1    Lanéelle, M.-A.2    Daffé, M.3
  • 9
    • 84904720893 scopus 로고    scopus 로고
    • New approaches to target the mycolic acid biosynthesis pathway for the development of tuberculosis therapeutics
    • North, E. J., Jackson, M., and Lee, R. E. (2014) New approaches to target the mycolic acid biosynthesis pathway for the development of tuberculosis therapeutics Curr. Pharm. Des. 20, 4357-78 10.2174/1381612819666131118203641
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 4357-4378
    • North, E.J.1    Jackson, M.2    Lee, R.E.3
  • 10
    • 80052716471 scopus 로고    scopus 로고
    • Fatty acyl-AMP ligases and polyketide synthases are unique enzymes of lipid biosynthetic machinery in Mycobacterium tuberculosis
    • Mohanty, D., Sankaranarayanan, R., and Gokhale, R. S. (2011) Fatty acyl-AMP ligases and polyketide synthases are unique enzymes of lipid biosynthetic machinery in Mycobacterium tuberculosis Tuberculosis 91, 448-455 10.1016/j.tube.2011.04.006
    • (2011) Tuberculosis , vol.91 , pp. 448-455
    • Mohanty, D.1    Sankaranarayanan, R.2    Gokhale, R.S.3
  • 11
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • Trivedi, O. A., Arora, P., Sridharan, V., Tickoo, R., Mohanty, D., and Gokhale, R. S. (2004) Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria Nature 428, 441-5 10.1038/nature02384
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 12
    • 15744389881 scopus 로고    scopus 로고
    • The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: Identification of the carboxylation product and determination of the acyl-CoA carboxylase componen
    • Portevin, D., de Sousa-D'Auria, C., Montrozier, H., Houssin, C., Stella, A., Lanéelle, M.-A., Bardou, F., Guilhot, C., and Daffé, M. (2005) The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase componen J. Biol. Chem. 280, 8862-74 10.1074/jbc.M408578200
    • (2005) J. Biol. Chem. , vol.280 , pp. 8862-8874
    • Portevin, D.1    De Sousa-D'Auria, C.2    Montrozier, H.3    Houssin, C.4    Stella, A.5    Lanéelle, M.-A.6    Bardou, F.7    Guilhot, C.8    Daffé, M.9
  • 15
    • 84856437600 scopus 로고    scopus 로고
    • Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis
    • Goyal, A., Verma, P., Anandhakrishnan, M., Gokhale, R. S., and Sankaranarayanan, R. (2012) Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis J. Mol. Biol. 416, 221-38 10.1016/j.jmb.2011.12.031
    • (2012) J. Mol. Biol. , vol.416 , pp. 221-238
    • Goyal, A.1    Verma, P.2    Anandhakrishnan, M.3    Gokhale, R.S.4    Sankaranarayanan, R.5
  • 17
    • 60749090908 scopus 로고    scopus 로고
    • Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains
    • Buchholz, T. J., Geders, T. W., Bartley, F. E., Reynolds, K. A., Smith, J. L., and Sherman, D. H. (2009) Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains ACS Chem. Biol. 4, 41-52 10.1021/cb8002607
    • (2009) ACS Chem. Biol. , vol.4 , pp. 41-52
    • Buchholz, T.J.1    Geders, T.W.2    Bartley, F.E.3    Reynolds, K.A.4    Smith, J.L.5    Sherman, D.H.6
  • 18
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • Portevin, D., De Sousa-D'Auria, C., Houssin, C., Grimaldi, C., Chami, M., Daffé, M., and Guilhot, C. (2004) A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms Proc. Natl. Acad. Sci. U. S. A. 101, 314-9 10.1073/pnas.0305439101
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3    Grimaldi, C.4    Chami, M.5    Daffé, M.6    Guilhot, C.7
  • 19
    • 79961085853 scopus 로고    scopus 로고
    • Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach
    • Carroll, P., Faray-Kele, M.-C., and Parish, T. (2011) Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach Appl. Environ. Microbiol. 77, 5040-3 10.1128/AEM.02880-10
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 5040-5043
    • Carroll, P.1    Faray-Kele, M.-C.2    Parish, T.3
  • 20
    • 84885957426 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of phenyl-substituted coumarins with anti-tubercular activity that target FadD32
    • Kawate, T., Iwase, N., Shimizu, M., Stanley, S. A., Wellington, S., Kazyanskaya, E., and Hung, D. T. (2013) Synthesis and structure-activity relationships of phenyl-substituted coumarins with anti-tubercular activity that target FadD32 Bioorg. Med. Chem. Lett. 23, 6052-9 10.1016/j.bmcl.2013.09.035
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 6052-6059
    • Kawate, T.1    Iwase, N.2    Shimizu, M.3    Stanley, S.A.4    Wellington, S.5    Kazyanskaya, E.6    Hung, D.T.7
  • 22
  • 23
    • 84949024177 scopus 로고    scopus 로고
    • Crystal structure of FadD32, an enzyme essential for mycolic acid biosynthesis in mycobacteria
    • Li, W., Gu, S., Fleming, J., and Bi, L. (2015) Crystal structure of FadD32, an enzyme essential for mycolic acid biosynthesis in mycobacteria Sci. Rep. 5, 15493 10.1038/srep15493
    • (2015) Sci. Rep. , vol.5 , pp. 15493
    • Li, W.1    Gu, S.2    Fleming, J.3    Bi, L.4
  • 24
    • 70350140439 scopus 로고    scopus 로고
    • Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase
    • Gulick, A. M. (2009) Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase ACS Chem. Biol. 4, 811-27 10.1021/cb900156h
    • (2009) ACS Chem. Biol. , vol.4 , pp. 811-827
    • Gulick, A.M.1
  • 26
    • 84880070725 scopus 로고    scopus 로고
    • Structures of Mycobacterium tuberculosis FadD10 protein reveal a new type of adenylate-forming enzyme
    • Liu, Z., Ioerger, T. R., Wang, F., and Sacchettini, J. C. (2013) Structures of Mycobacterium tuberculosis FadD10 protein reveal a new type of adenylate-forming enzyme J. Biol. Chem. 288, 18473-83 10.1074/jbc.M113.466912
    • (2013) J. Biol. Chem. , vol.288 , pp. 18473-18483
    • Liu, Z.1    Ioerger, T.R.2    Wang, F.3    Sacchettini, J.C.4
  • 27
    • 79251595133 scopus 로고    scopus 로고
    • Structural and functional studies of fatty acyl adenylate ligases from E. Coli and L. Pneumophila
    • Zhang, Z., Zhou, R., Sauder, J. M., Tonge, P. J., Burley, S. K., and Swaminathan, S. (2011) Structural and functional studies of fatty acyl adenylate ligases from E. coli and L. pneumophila J. Mol. Biol. 406, 313-24 10.1016/j.jmb.2010.12.011
    • (2011) J. Mol. Biol. , vol.406 , pp. 313-324
    • Zhang, Z.1    Zhou, R.2    Sauder, J.M.3    Tonge, P.J.4    Burley, S.K.5    Swaminathan, S.6
  • 28
    • 84861993618 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase: Structural basis for housing lipid substrates longer than the enzyme
    • Andersson, C. S., Lundgren, C. A. K., Magnúsdóttir, A., Ge, C., Wieslander, A., Martinez Molina, D., and Högbom, M. (2012) The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase: structural basis for housing lipid substrates longer than the enzyme Structure 20, 1062-7 10.1016/j.str.2012.03.012
    • (2012) Structure , vol.20 , pp. 1062-1067
    • Andersson, C.S.1    Lundgren, C.A.K.2    Magnúsdóttir, A.3    Ge, C.4    Wieslander, A.5    Martinez Molina, D.6    Högbom, M.7
  • 29
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May, J. J., Kessler, N., Marahiel, M. A., and Stubbs, M. T. (2002) Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases Proc. Natl. Acad. Sci. U. S. A. 99, 12120-5 10.1073/pnas.182156699
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12120-12125
    • May, J.J.1    Kessler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 32
    • 77951518283 scopus 로고    scopus 로고
    • Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv
    • Malen, H., Pathak, S., Søfteland, T., de Souza, G. A., and Wiker, H. G. (2010) Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv BMC Microbiol. 10, 132 10.1186/1471-2180-10-132
    • (2010) BMC Microbiol. , vol.10 , pp. 132
    • Malen, H.1    Pathak, S.2    Søfteland, T.3    De Souza, G.A.4    Wiker, H.G.5
  • 33
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • Gu, S., Chen, J., Dobos, K. M., Bradbury, E. M., Belisle, J. T., and Chen, X. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain Mol. Cell. Proteomics 2, 1284 10.1074/mcp.M300060-MCP200
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1284
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 34
    • 48649093119 scopus 로고    scopus 로고
    • Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase
    • Reger, A. S., Wu, R., Dunaway-Mariano, D., and Gulick, A. M. (2008) Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase Biochemistry 47, 8016-25 10.1021/bi800696y
    • (2008) Biochemistry , vol.47 , pp. 8016-8025
    • Reger, A.S.1    Wu, R.2    Dunaway-Mariano, D.3    Gulick, A.M.4
  • 35
    • 37249085564 scopus 로고    scopus 로고
    • Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: Coenzyme a ligase for expanded substrate range
    • Wu, R., Reger, A. S., Cao, J., Gulick, A. M., and Dunaway-Mariano, D. (2007) Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range Biochemistry 46, 14487-99 10.1021/bi701609w
    • (2007) Biochemistry , vol.46 , pp. 14487-14499
    • Wu, R.1    Reger, A.S.2    Cao, J.3    Gulick, A.M.4    Dunaway-Mariano, D.5
  • 36
    • 0037790957 scopus 로고    scopus 로고
    • A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles
    • Millard, C. S., Stols, L., Quartey, P., Kim, Y., Dementieva, I., and Donnelly, M. I. (2003) A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles Protein Expression Purif. 29, 311-20 10.1016/S1046-5928(03)00063-9
    • (2003) Protein Expression Purif. , vol.29 , pp. 311-320
    • Millard, C.S.1    Stols, L.2    Quartey, P.3    Kim, Y.4    Dementieva, I.5    Donnelly, M.I.6
  • 37
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri, L. E., Weinreb, P. H., Lei, M., Nakano, M. M., Zuber, P., and Walsh, C. T. (1998) Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases Biochemistry 37, 1585-95 10.1021/bi9719861
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 38
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures Protein Expression Purif. 41, 207-34 10.1016/j.pep.2005.01.016
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 39
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes Acta Crystallogr., Sect. D: Biol. Crystallogr. 62, 859-66 10.1107/S0907444906019949
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 43
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6, 458-63 10.1038/8263
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 44
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr., Sect. D: Biol. Crystallogr. 55, 191-205 10.1107/S0907444998006684
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 46
    • 69249123826 scopus 로고    scopus 로고
    • A critical electrostatic interaction mediates inhibitor recognition by human asparagine synthetase
    • Ikeuchi, H., Meyer, M. E., Ding, Y., Hiratake, J., and Richards, N. G. J. (2009) A critical electrostatic interaction mediates inhibitor recognition by human asparagine synthetase Bioorg. Med. Chem. 17, 6641-50 10.1016/j.bmc.2009.07.071
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 6641-6650
    • Ikeuchi, H.1    Meyer, M.E.2    Ding, Y.3    Hiratake, J.4    Richards, N.G.J.5


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