An overview of mechanism and chemical inhibitors of shikimate kinase

References

• Arcuri, H. A., Canduri, F., Pereira, J. H., da Silveira, N. J., Camera Júnior, J. C., de Oliveira, J. S., Basso, L. A., Palma, M. S., Santos, D. S., & de Azevedo Júnior, W. F. (2004). Molecular models for shikimate pathway enzymes of Xylella fastidiosa. Biochemical and Biophysical Research Communications, 320(3), 979–991. https://doi.org/10.1016/j.bbrc.2004.05.220
   PubMed Web of Science ®Google Scholar
• Arora, K., Ochoa-Montaño, B., Tsang, P. S., Blundell, T. L., Dawes, S. S., Mizrahi, V., Bayliss, T., Mackenzie, C. J., Cleghorn, L. A., Ray, P. C., Wyatt, P. G., Uh, E., Lee, J., Barry, C. E., 3rd., & Boshoff, H. I. (2014). Respiratory flexibility in response to inhibition of cytochrome C oxidase in Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy, 58(11), 6962–6965. https://doi.org/10.1128/AAC.03486-14
   PubMed Web of Science ®Google Scholar
• Badger, J., Sauder, J. M., Adams, J. M., Antonysamy, S., Bain, K., Bergseid, M. G., et al. (2005). Proteins, 60, 787–796. https://doi.org/10.2210/pdb1VIA/pdb
   PubMed Web of Science ®Google Scholar
• Ballell, L., Bates, R. H., Young, R. J., Alvarez-Gomez, D., Alvarez-Ruiz, E., Barroso, V., Blanco, D., Crespo, B., Escribano, J., González, R., Lozano, S., Huss, S., Santos-Villarejo, A., Martín-Plaza, J. J., Mendoza, A., Rebollo-Lopez, M. J., Remuiñan-Blanco, M., Lavandera, J. L., Pérez-Herran, E., … Cammack, N. (2013). Fueling open-source drug discovery: 177 small-molecule leads against tuberculosis. ChemMedChem, 8(2), 313–321. https://doi.org/10.1002/cmdc.201200428
   PubMed Web of Science ®Google Scholar
• Bentley, R., & Haslam, E. (1990). The shikimate pathway–a metabolic tree with many branches. Critical Reviews in Biochemistry and Molecular Biology, 25(5), 307–384. https://doi.org/10.3109/10409239009090615
   PubMed Web of Science ®Google Scholar
• Biava, M., Porretta, G. C., Poce, G., Supino, S., Deidda, D., Pompei, R., Molicotti, P., Manetti, F., & Botta, M. (2006). Antimycobacterial agents. Novel diarylpyrrole derivatives of BM212 endowed with high activity toward Mycobacterium tuberculosis and low cytotoxicity. Journal of Medicinal Chemistry, 49(16), 4946–4952. https://doi.org/10.1021/jm0602662
   PubMed Web of Science ®Google Scholar
• Blanco, B., Prado, V., Lence, E., Otero, J. M., Garcia-Doval, C., van Raaij, M. J., Llamas-Saiz, A. L., Lamb, H., Hawkins, A. R., & González-Bello, C. (2013). Mycobacterium tuberculosis shikimate kinase inhibitors: Design and simulation studies of the catalytic turnover. Journal of the American Chemical Society, 135(33), 12366–12376. https://doi.org/10.1021/ja405853p
   PubMed Web of Science ®Google Scholar
• Brief history of tuberculosis. (2020). https://www.cdc.gov/tb/worldtbday/history.htm
   Google Scholar
• Brown-Elliott, B. A., Rubio, A., & Wallace, R. J. Jr (2018). In Vitro susceptibility testing of a novel benzimidazole, SPR719, against nontuberculous mycobacteria. Antimicrobial Agents and Chemotherapy, 62(11), e01503-18. https://doi.org/10.1128/AAC.01503-18
   PubMed Web of Science ®Google Scholar
• Chadha, V. K. (2009). Progress towards millennium development goals for TB control in seven Asian countries. The Indian Journal of Tuberculosis, 56(1), 30–43. https://pubmed.ncbi.nlm.nih.gov/19402270/
   PubMedGoogle Scholar
• Chaisson, R. E., Schecter, G. F., Theuer, C. P., Rutherford, G. W., Echenberg, D. F., & Hopewell, P. C. (1987). Tuberculosis in patients with the acquired immunodeficiency syndrome. Clinical features, response to therapy, and survival. American Review of Respiratory Disease, 136(3), 570–574. https://doi.org/10.1164/ajrccm/136.3.570
   PubMed Web of Science ®Google Scholar
• Chellat, M. F., & Riedl, R. (2017). Pseudouridimycin: The first nucleoside analogue that selectively inhibits bacterial RNA polymerase. Angewandte Chemie (International ed. in English), 56(43), 13184–13186. https://doi.org/10.1002/anie.201708133
   PubMed Web of Science ®Google Scholar
• Cheng, W. C., Chang, Y. N., & Wang, W. C. (2005). Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase. Journal of Bacteriology, 187, 8156–8163. https://doi.org/10.1128/JB.187.23.8156-8163.2005
   PubMed Web of Science ®Google Scholar
• Cheng, W. C., Chen, Y. F., Wang, H. J., Hsu, K. C., Lin, S. C., Chen, T. J., Yang, J. M., & Wang, W. C. (2010). Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism. PLoS One, 7, e33481–e33481. https://doi.org/10.1371/journal.pone.0033481
   Web of Science ®Google Scholar
• Cheng, Franklin, M. C., Cheung, J., Rudolph, M. J., Burshteyn, F., Cassidy, M., Gary, E., Hillerich, B., Yao, Z. K., Carlier, P. R., Totrov, M., & Love, J. D. (2011). Structural genomics for drug design against the pathogen Coxiella burnetii. Proteins, 83, 2124–2136. https://doi.org/10.1002/prot.24841
   Google Scholar
• Chirke, S. S., Krishna, J. S., Rathod, B. B., Bonam, S. R., Khedkar, V. M., Rao, B. V., Sampath Kumar, H. M., & Shetty, P. R. (2017). Synthesis of triazole derivatives of 9-ethyl-9H-carbazole and dibenzo[b,d]furan and evaluation of their antimycobacterial and immunomodulatory activity. ChemistrySelect, 2(24), 7309–7318. https://doi.org/10.1002/slct.201701377
   Web of Science ®Google Scholar
• Curtidor, H., Arevalo-Pinzon, G., Bermudez, A., Calderon, D., Vanegas, M., Patino, L. C., Patarroyo, M. A., & Patarroyo, M. E. (2012). Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins. Amino Acids, 43, 365–378. https://doi.org/10.1007/s00726-011-1087-8
   PubMed Web of Science ®Google Scholar
• Dadlani, V. G., Chhabhaiya, H., Somani, R. R., & Tripathi, P. K. (2022). Synthesis, molecular docking, and biological evaluation of novel 1,2,4-triazole-isatin derivatives as potential Mycobacterium tuberculosis shikimate kinase inhibitors. Chemical Biology & Drug Design, 100(2), 230–244. https://doi.org/10.1111/cbdd.14060
   PubMed Web of Science ®Google Scholar
• Debnath, J., Siricilla, S., Wan, B., Crick, D. C., Lenaerts, A. J., Franzblau, S. G., & Kurosu, M. (2012). Discovery of selective menaquinone biosynthesis inhibitors against Mycobacterium tuberculosis. Journal of Medicinal Chemistry, 55(8), 3739–3755. https://doi.org/10.1021/jm201608g
   PubMed Web of Science ®Google Scholar
• Dhaliwal, B., Nichols, C. E., Ren, J., Lockyer, M., Charles, I., Hawkins, A. R., & Stammers, D. K. (2004). Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase. FEBS Letters, 574(1–3), 49–54. https://doi.org/10.1016/j.febslet.2004.08.005
   PubMed Web of Science ®Google Scholar
• Dias, M. V., Faím, L. M., Vasconcelos, I. B., de Oliveira, J. S., Basso, L. A., Santos, D. S., & de Azevedo, W. F. Jr (2007). Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 63(1), 1–6. https://doi.org/10.1107/S1744309106046823
   PubMedGoogle Scholar
• Elliott, A. M., Halwiindi, B., Hayes, R. J., Luo, N., Mwinga, A. G., Tembo, G., Machiels, L., Steenbergen, G., Pobee, J. O., Nunn, P., & McAdam, K. P. (1995). The impact of human immunodeficiency virus on mortality of patients treated for tuberculosis in a cohort study in Zambia. Transactions of the Royal Society of Tropical Medicine and Hygiene, 89(1), 78–82. https://doi.org/10.1016/0035-9203(95)90668-1
   PubMed Web of Science ®Google Scholar
• Faim, L. M., Kias, M. V. B., & Vasconcelos, I. G. (2008). Crystal structure of shikimate kinase from Mycobacterium tuberculosis in complex with AMP-PNP. Deposited 11/11/2008. Protein Data Bank. https://doi.org/10.2210/pdb3baf/pdb
   Google Scholar
• Fox, W., Ellard, G. A., & Mitchison, D. A. (1999). Studies on the treatment of tuberculosis undertaken by the British Medical Research Council tuberculosis units, 1946-1986, with relevant subsequent publications. The International Journal of Tuberculosis and Lung Disease: The Official Journal of the International Union against Tuberculosis and Lung Disease, 3(10), S231–S279. https://pubmed.ncbi.nlm.nih.gov/10529902/
   PubMed Web of Science ®Google Scholar
• Freitas de Freitas, T., Roth, C. D., Abbadi, B. L., Hopf, F. S. M., Perelló, M. A., de Matos Czeczot, A., de Souza, E. V., Borsoi, A. F., Machado, P., Bizarro, C. V., & Basso, L. A. (2022). Identification of potential inhibitors of Mycobacterium tuberculosis shikimate kinase: Molecular docking, in-silico toxicity and invitro experiments. Journal of Computer Aided Molecular Design, 37, 117–128. https://doi.org/10.1007/s/10822-022-00495-w
   PubMed Web of Science ®Google Scholar
• Gan, J., Gu, Y., Li, Y., Yan, H., & Ji, X. (2006). Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue. Biochemistry, 45(28), 8539–8545. https://doi.org/10.1021/bi0606290
   PubMed Web of Science ®Google Scholar
• Gonzalez-Bello, C. (2016). Inhibition of shikimate kinase and type II dehydroquinase for antibiotic discovery: Structure-based design and simulation studies. Current Topics in Medicinal Chemistry, 16, 960–977.
   PubMed Web of Science ®Google Scholar
• Gordon, S., Simithy, J., Goodwin, D. C., & Calderón, A. I. (2014). Selective Mycobacterium tuberculosis shikimate kinase inhibitors as potential antibacterials. Perspectives in Medicinal Chemistry, 7, 9–20. https://doi.org/10.4137/PMC.S13212
   Google Scholar
• Görisch, H. (1978). On the mechanism of the chorismate mutase reaction. Biochemistry, 17(18), 3700–3705. https://doi.org/10.1021/bi00611a004
   PubMed Web of Science ®Google Scholar
• Grzegorzewicz, A. E., Pham, H., Gundi, V. A., Scherman, M. S., North, E. J., Hess, T., Jones, V., Gruppo, V., Born, S. E., Korduláková, J., Chavadi, S. S., Morisseau, C., Lenaerts, A. J., Lee, R. E., McNeil, M. R., & Jackson, M. (2012). Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane. Nature Chemical Biology, 8(4), 334–341. https://doi.org/10.1038/nchembio.794
   PubMed Web of Science ®Google Scholar
• Gu, Y., Reshetnikova, L., Li, Y., Wu, Y., Yan, H., Singh, S., & Ji, X. (2002). Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis. Journal of Molecular Biology, 319(3), 779–789. https://doi.org/10.1016/S0022-2836(02)00339-X
   PubMed Web of Science ®Google Scholar
• Hartmann, M. D., Bourenkov, G. P., Oberschall, A., Strizhov, N., & Bartunik, H. D. (2006). Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis. Journal of Molecular Biology, 364(3), 411–423. https://doi.org/10.1016/j.jmb.2006.09.001
   PubMed Web of Science ®Google Scholar
• Herrmann, K. M. (1995). The shikimate pathway: Early steps in the biosynthesis of aromatic compounds. The Plant Cell, 7(7), 907–919. https://doi.org/10.1105/tpc.7.7.907
   PubMed Web of Science ®Google Scholar
• Höner Zu Bentrup, K., Miczak, A., Swenson, D. L., & Russell, D. G. (1999). Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. Journal of Bacteriology, 181(23), 7161–7167. https://doi.org/10.1128/JB.181.23.7161-7167.1999
   PubMed Web of Science ®Google Scholar
• Hsu, K. C., Cheng, W. C., Chen, Y. F., Wang, H. J., Li, L. T., Wang, W. C., & Yang, J. M. (2012). Core site-moiety maps reveal inhibitors and binding mechanisms of orthologous proteins by screening compound libraries. PLoS One, 7(2), e32142. https://doi.org/10.1371/journal.pone.0032142
   PubMed Web of Science ®Google Scholar
• Hugonnet, J. E., Tremblay, L. W., Boshoff, H. I., Barry, C. E., 3rd., & Blanchard, J. S. (2009). Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis. Science (New York, N.Y.), 323(5918), 1215–1218. https://doi.org/10.1126/science.1167498
   PubMed Web of Science ®Google Scholar
• Igarashi, M., Nakagawa, N., Doi, N., Hattori, S., Naganawa, H., & Hamada, M. A. S. A. (2003). Caprazamycin B, a novel anti-tuberculosis antibiotic, from Streptomyces sp. The Journal of Antibiotics, 56(6), 580–583. https://doi.org/10.7164/antibiotics.56.580
   PubMed Web of Science ®Google Scholar
• Iseman, M. D. (1993). Treatment of multidrug-resistant tuberculosis. The New England Journal of Medicine, 329(11), 784–791. https://doi.org/10.1056/nejm199309093291108
   PubMed Web of Science ®Google Scholar
• Jackson, M., Raynaud, C., Lanéelle, M. A., Guilhot, C., Laurent-Winter, C., Ensergueix, D., Gicquel, B., & Daffé, M. (1999). Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope. Molecular Microbiology, 31(5), 1573–1587. https://doi.org/10.1046/j.1365-2958.1999.01310.x
   PubMed Web of Science ®Google Scholar
• Jeyakanthan, J., Nithya, N., Shimada, A., Velmurugan, D., Ebihara, A., Shinkai, A., Kuramitsu, S., Shiro, Y., & Yokoyama, S. (2008). Crystal structure of Shikimate kinase (aq_2177) from Aquifex Aeolicus vf5. RIKEN Structural Genomics/Proteomics Initiative (RSGI), 2008-05-13. https://doi.org/10.2210/pdb2PT5/pdb
   Google Scholar
• Juliasih, N. N., Mertaniasih, N. M., Hadi, C., Soedarsono, Sari, R. M., & Alfian, I. N. (2020). Factors affecting tuberculosis patients’ quality of life in Surabaya, Indonesia. Journal of Multidisciplinary Healthcare, 13, 1475–1480. https://doi.org/10.2147/JMDH.S274386
   PubMed Web of Science ®Google Scholar
• Kaczmarek, A. (2014). Target validation of shikimate kinase inhibitors: A structural and kinetic perspective. Journal of Medicinal Chemistry, 57(17), 7056–7071.
   Google Scholar
• Kailasam, P., & Holliday, G. L. (2015). Structure-based target validation using shikimate kinase inhibitors. Bioorganic & Medicinal Chemistry, 23(17), 5306–5317.
   Google Scholar
• Kang, S., Kim, R. Y., Seo, M. J., Lee, S., Kim, Y. M., Seo, M., Seo, J. J., Ko, Y., Choi, I., Jang, J., Nam, J., Park, S., Kang, H., Kim, H. J., Kim, J., Ahn, S., Pethe, K., Nam, K., No, Z., & Kim, J. (2014). Lead optimization of a novel series of imidazo[1,2-a]pyridine amides leading to a clinical candidate (Q203) as a multi- and extensively-drug-resistant anti-tuberculosis agent. Journal of Medicinal Chemistry, 57(12), 5293–5305. https://doi.org/10.1021/jm5003606
   PubMed Web of Science ®Google Scholar
• Kast, P., Tewari, B. Y., Wiest, O., Hilvert, D., Houk, K. N., & Goldberg, R. N. (1997). Thermodynamics of the conversion of chorismate to prephenate: Experimental results and theoretical predictions. The Journal of Physical Chemistry B, 101(50), 10976–10982. https://doi.org/10.1021/jp972501l
   Web of Science ®Google Scholar
• Kaye, K., & Frieden, T. R. (1996). Tuberculosis control: The relevance of classic principles in an era of acquired immunodeficiency syndrome and multidrug resistance. Epidemiologic Reviews, 18(1), 52–63. https://doi.org/10.1093/oxfordjournals.epirev.a017916
   PubMed Web of Science ®Google Scholar
• Kitagawa, W., & Tamura, T. (2008). A quinoline antibiotic from Rhodococcus erythropolis JCM 6824. The Journal of Antibiotics, 61(11), 680–682. https://doi.org/10.1038/ja.2008.96
   PubMed Web of Science ®Google Scholar
• Kochi, A. (1991). The global tuberculosis situation and the new control strategy of the World Health Organization. Tubercle, 72(1), 1–6. https://doi.org/10.1016/0041-3879(91)90017-m
   PubMedGoogle Scholar
• Kolb, A., & Schirmer, T. (2012). Target validation of shikimate kinases. Current Opinion in Chemical Biology, 16(4), 481–491.
   Google Scholar
• Krell, T., Maclean, J., Boam, D. J., Cooper, A., Resmini, M., Brocklehurst, K., Kelly, S. M., Price, N. C., Lapthorn, A. J., & Coggins, J. R. (2001). Biochemical and X-ray crystallographic studies on shikimate kinase: The important structural role of the P-loop lysine. Protein Science, 10(6), 1137–1149. https://doi.org/10.1110/ps.52501
   PubMed Web of Science ®Google Scholar
• Krishnasamy, S. K., Namasivayam, V., Mathew, S., Eakambaram, R. S., Ibrahim, I. A., Natarajan, A., & Palaniappan, S. (2016). Design, synthesis, and characterization of some hybridized pyrazolone pharmacophore analogs against Mycobacterium tuberculosis. Archiv Der Pharmazie, 349(5), 383–397. https://doi.org/10.1002/ardp.201600019
   PubMed Web of Science ®Google Scholar
• Kumar, M., Verma, S., Sharma, S., Srinivasan, A., Singh, T. P., & Kaur, P. (2010). Structure-based in silico design of a high-affinity dipeptide inhibitor for novel protein drug target shikimate kinase of Mycobacterium tuberculosis. Chemical Biology & Drug Design, 76(3), 277–284. https://doi.org/10.1111/j.1747-0285.2010.01005.x
   PubMed Web of Science ®Google Scholar
• Kurosu, M., & Crick, D. C. (2009). MenA is a promising drug target for developing novel lead molecules to combat Mycobacterium tuberculosis. Medicinal Chemistry, 5(2), 197–207. https://doi.org/10.2174/157340609787582882
   PubMed Web of Science ®Google Scholar
• Lechartier, B., Hartkoorn, R. C., & Cole, S. T. (2012). In vitro combination studies of benzothiazinone lead compound BTZ043 against Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy, 56(11), 5790–5793. https://doi.org/10.1128/AAC.01476-12
   PubMed Web of Science ®Google Scholar
• Lenaerts, A. J., Gruppo, V., Marietta, K. S., Johnson, C. M., Driscoll, D. K., Tompkins, N. M., Rose, J. D., Reynolds, R. C., & Orme, I. M. (2005). Preclinical testing of the nitroimidazopyran PA-824 for activity against Mycobacterium tuberculosis in a series of in vitro and in vivo models. Antimicrobial Agents and Chemotherapy, 49(6), 2294–2301. https://doi.org/10.1128/AAC.49.6.2294-2301.2005
   PubMed Web of Science ®Google Scholar
• Longo, D. L., Fauci, A. S., Hauser, S. L., & Jameson, J. L. (2012). Harrison’s principles of internal medicine (18th ed.). McGraw Hill. 165: Tuberculosis. https://books.google.co.in/books?id=RSLZvLBjjF4C&pg=PT141&lpg=PT141&dq=L.+Fauci.+Harrison%27s+Principles+of+Internal+Medicine+(18th+ed.).+New+York:+McGraw+Hill.+pp.+Chapter+165:+Tuberculosis+(2012).&source=bl&ots=ONg0FyjHKx&sig=ACfU3U3C5caH01HMcvRmmsE8Mmd5dypepQ&hl=en&sa=X&ved=2ahUKEwiz3a7B6OX2AhVezzgGHcFcA6cQ6AF6BAgZEAM.
   Google Scholar
• Makarov, V., Lechartier, B., Zhang, M., Neres, J., Sar, A. M., Raadsen, S. A., Hartkoorn, R. C., Ryabova, O. B., Vocat, A., Decosterd, L. A., Widmer, N., Buclin, T., Bitter, W., Andries, K., Pojer, F., Dyson, P. J., & Cole, S. T. (2014). Towards a new combination therapy for tuberculosis with next generation benzothiazinones. EMBO Molecular Medicine, 6(3), 372–383. https://doi.org/10.1002/emmm.201303575
   PubMed Web of Science ®Google Scholar
• Makarov, V., Manina, G., Mikusova, K., Möllmann, U., Ryabova, O., Saint-Joanis, B., Dhar, N., Pasca, M. R., Buroni, S., Lucarelli, A. P., Milano, A., De Rossi, E., Belanova, M., Bobovska, A., Dianiskova, P., Kordulakova, J., Sala, C., Fullam, E., Schneider, P., … Cole, S. T. (2009). Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science (New York, N.Y.), 324(5928), 801–804. https://doi.org/10.1126/science.1171583
   PubMed Web of Science ®Google Scholar
• Makarov, V., Neres, J., Hartkoorn, R. C., Ryabova, O. B., Kazakova, E., Šarkan, M., Huszár, S., Piton, J., Kolly, G. S., Vocat, A., Conroy, T. M., Mikušová, K., & Cole, S. T. (2015). The 8-pyrrole-benzothiazinones are noncovalent inhibitors of DprE1 from Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy, 59(8), 4446–4452. https://doi.org/10.1128/AAC.00778-15
   PubMed Web of Science ®Google Scholar
• McShane, H. (2005). Co-infection with HIV and TB: Double trouble. International Journal of STD & AIDS, 16(2), 95–101. https://doi.org/10.1258/0956462053057576
   PubMed Web of Science ®Google Scholar
• Mehra, R., Rajput, V. S., Gupta, M., Chib, R., Kumar, A., Wazir, P., Khan, I. A., & Nargotra, A. (2016). Benzothiazole derivative as a novel mycobacterium tuberculosis shikimate kinase inhibitor: Identification and elucidation of its allosteric mode of inhibition. Journal of Chemical Information and Modeling, 56(5), 930–940. https://doi.org/10.1021/acs.jcim.6b00056
   PubMed Web of Science ®Google Scholar
• Michel, G., Roszak, A. W., Sauvé, V., Maclean, J., Matte, A., Coggins, J. R., Cygler, M., & Lapthorn, A. J. (2003). Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. Journal of Biological Chemistry, 278(21), 19463–19472. https://doi.org/10.1074/jbc.M300794200
   PubMed Web of Science ®Google Scholar
• Mikusova, K., Makarov, V., & Neres, J. (2013). DprE1–from the discovery to the promising tuberculosis drug target. Current Pharmaceutical Design, 20(27), 4379–4403. https://doi.org/10.2174/138161282027140630122724
   Web of Science ®Google Scholar
• Millar, G., Lewendon, A., Hunter, M. G., & Coggins, J. R. (1986). The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product. Biochemical Journal, 237(2), 427–437. https://doi.org/10.1042/bj2370427
   PubMed Web of Science ®Google Scholar
• Minasov, G., Light, S. H., Halavaty, A., Shuvalova, L., Papazisi, L., & Anderson, W. F., Center for Structural Genomics of Infectious Diseases (CSGID). (2012). 1.7 Angstrom Resolution Crystal Structure of Shikimate Kinase from Bacteroides thetaiotaomicron. https://doi.org/10.2210/pdb3VAA/pdb
   Google Scholar
• Monga, V., Goyal, K., Steindel, M., Malhotra, M., Rajani, D. P., & Rajani, S. D. (2014). Synthesis and evaluation of new chalcones, derived pyrazoline and cyclohexenone derivatives as potent antimicrobial, anti-tubercular and antileishmanial agents. Medicinal Chemistry Research, 23(4), 2019–2032. https://doi.org/10.1007/s00044-013-0803-1
   Web of Science ®Google Scholar
• Mowbray, S. L., Kathiravan, M. K., Pandey, A. A., & Odell, L. R. (2014). Inhibition of glutamine synthetase: A potential drug target in Mycobacterium tuberculosis. Molecules (Basel, Switzerland), 19(9), 13161–13176. https://doi.org/10.3390/molecules190913161
   PubMed Web of Science ®Google Scholar
• National Tuberculosis Control Programme. (2007). Tuberculosis control in Bangladesh: Annual report 2007. National Tuberculosis Control Programme, Directorate General of Health Services, Ministry of Health and Family Welfare, Government of Bangladesh, 37. http://www.globalhealthdelivery.org/files/ghd/files/ghd-010_bracs_tb_program_lapkovc.pdf
   Google Scholar
• New Drug Therapy Approvals. (2019). US Food and Drug Administration. https://www.fda.gov/drugs/new-drugs-fda-cders-new-molecular-entities-and-new-therapeutic-biological-products/new-drug-therapy-approvals-2019
   Google Scholar
• Nunes, J., Duque, M. A., de Freitas, T. F., Galina, L., Timmers, L., Bizarro, C. V., Machado, P., Basso, L. A., & Ducati, R. G. (2020). Mycobacterium tuberculosis shikimate pathway enzymes as targets for the rational design of anti-tuberculosis drugs. Molecules (Basel, Switzerland), 25(6), 1259. https://doi.org/10.3390/molecules25061259
   PubMed Web of Science ®Google Scholar
• O’Donnell, M. R., Reddy, D., & Saukkonen, J. J. (2014). Antimycobacterial agents. In D. Kasper, A. Fauci, S. Hauser, D. Longo, J. Jameson, & J. Loscalzo (Eds.), Harrison’s principles of internal medicine, 19e. McGraw Hill. https://accessmedicine.mhmedical.com/content.aspx?bookid=1130&sectionid=79737263
   Google Scholar
• O’Malley, T., Alling, T., Early, J. V., Wescott, H. A., Kumar, A., Moraski, G. C., Miller, M. J., Masquelin, T., Hipskind, P. A., & Parish, T. (2018). Imidazopyridine compounds inhibit mycobacterial growth by depleting ATP levels. Antimicrobial Agents and Chemotherapy, 62(6), e02439–17. https://doi.org/10.1128/AAC.02439-17
   PubMed Web of Science ®Google Scholar
• O’Neill, D. A. (2008). Shikimate kinase target validation: Applications to drug Pedro discovery. Current Topics in Medicinal Chemistry, 8(10), 925–937.
   Google Scholar
• Ojeda-May, P. (2021). Exploring the mechanism of shikimate kinase through quantum mechanical and molecular mechanical (QM/MM) methods. Biophysica, 1(3), 334–343. https://doi.org/10.3390/biophysica1030025
   Google Scholar
• Oursler, K. K., Moore, R. D., Bishai, W. R., Harrington, S. M., Pope, D. S., & Chaisson, R. E. (2002). Survival of patients with pulmonary tuberculosis: Clinical and molecular epidemiologic factors. Clinical Infectious Diseases : An Official Publication of the Infectious Diseases Society of America, 34(6), 752–759. https://doi.org/10.1086/338784
   PubMed Web of Science ®Google Scholar
• Pandey, S., Dhamija, E., Kumar, S., Yadav, P., Narender, T., Dasgupta, A., Ramachandran, R., & Srivastav, K. (2020). Identification of active molecules against Mycobacterial Shikimate Kinase from Chemical library and their affinity with different domains. Briefings in Bioinformatics, https://doi.org/10.22541/au.160491622.24853329/v1
   Google Scholar
• Parwati, I., van Crevel, R., & van Soolingen, D. (2010). Possible underlying mechanisms for successful emergence of the Mycobacterium tuberculosis Beijing genotype strains. The Lancet Infectious Diseases, 10(2), 103–111. https://doi.org/10.1016/S1473-3099(09)70330-5
   PubMed Web of Science ®Google Scholar
• Pereira, J. H., de Oliveira, J. S., Canduri, F., Dias, M. V., Palma, M. S., Basso, L. A., Santos, D. S., & de Azevedo, W. F. Jr (2004). Structure of shikimate kinase from Mycobacterium tuberculosis reveals the binding of shikimic acid. Acta Crystallographica Section D Biological Crystallography, 60(12), 2310–2319. https://doi.org/10.1107/S090744490402517X
   PubMedGoogle Scholar
• Pernas, M., Blanco, B., Lence, E., Thompson, P., Alastair, H. R., & Bello, C. G. (2019). Synthesis of rigidified shikimic acid derivatives by ring-closing metathesis to imprint inhibitor efficacy against shikimate kinase enzyme. Organic Chemistry Frontiers, 6(14), 2514–2528. https://pubs.rsc.org/en/content/articlelanding/2019/qo/c9qo00562e. https://doi.org/10.1039/C9QO00562E
   Web of Science ®Google Scholar
• Pissinate, K., Villela, A. D., Rodrigues-Junior, V., Giacobbo, B. C., Grams, E. S., Abbadi, B. L., Trindade, R. V., Roesler Nery, L., Bonan, C. D., Back, D. F., Campos, M. M., Basso, L. A., Santos, D. S., & Machado, P. (2016). 2-(Quinolin-4-yloxy)acetamides are active against drug-susceptible and drug-resistant Mycobacterium tuberculosis strains. ACS Medicinal Chemistry Letters, 7(3), 235–239. https://doi.org/10.1021/acsmedchemlett.5b00324
   PubMed Web of Science ®Google Scholar
• Poce, G., Consalvi, S., Venditti, G., Alfonso, S., Desideri, N., Fernandez-Menendez, R., Bates, R. H., Ballell, L., Barros Aguirre, D., Rullas, J., De Logu, A., Gardner, M., Ioerger, T. R., Rubin, E. J., & Biava, M. (2019). Novel pyrazole-containing compounds active against Mycobacterium tuberculosis. ACS Medicinal Chemistry Letters, 10(10), 1423–1429. https://doi.org/10.1021/acsmedchemlett.9b00204
   PubMed Web of Science ®Google Scholar
• Rajput, V. S., Mehra, R., Kumar, S., Nargotra, A., Singh, P. P., & Khan, I. A. (2016). Screening of anti-tubercular compound library identifies novel shikimate kinase inhibitors of Mycobacterium tuberculosis. Applied Microbiology and Biotechnology, 100(12), 5415–5426. https://doi.org/10.1007/s00253-015-7268-8
   PubMed Web of Science ®Google Scholar
• Ramakant, B. (2009). 36 million people with TB cured. World Health Organization. http://www.weeklyblitz.net/363
   Google Scholar
• Reddy, M. R., Krishnasamy, S. K., & Kathiravan, M. K. (2020). Identification of novel scaffold using ligand and structure-based approach targeting shikimate kinase. Bioorganic Chemistry, 102, 104083. https://doi.org/10.1016/j.bioorg.2020.104083
   PubMed Web of Science ®Google Scholar
• Remuinan, M. J., Perez-Herran, E., Rullas, J., Alemparte, C., Martınez-Hoyos, M., Dow, D. J., Afari, J., Mehta, N., Esquivias, J., Jiménez, E., Ortega-Muro, F., Fraile-Gabaldón, M. T., Spivey, V. L., Loman, N. J., Pallen, M. J., Constantinidou, C., Minick, D. J., Cacho, M., Rebollo-Lopez, M. J., … Cammack, N. (2013). Tetrahydropyrazolo [1,5-a] pyrimidine-3-carboxamide and N-benzyl-60, 70-dihydrospiro [piperidine-4, 40-thieno [3,2-c] pyran] analogues with bactericidal efficacy against Mycobacterium tuberculosis targeting MmpL3. PLoS One, 8(4), e60933. https://doi.org/10.1371/journal.pone.0060933
   PubMed Web of Science ®Google Scholar
• Rios-Soto, L., Téllez-Valencia, A., Sierra-Campos, E., Valdez-Solana, M., Cisneros-Martínez, J., Gómez Palacio-Gastélum, M., Castillo-Villanueva, A., & Avitia-Domínguez, C. (2021). Finding the first potential inhibitors of shikimate kinase from methicillin resistant Staphylococcus aureus through computer-assisted drug design. Molecules (Basel, Switzerland), 26(21), 6736. https://doi.org/10.3390/molecules26216736
   PubMed Web of Science ®Google Scholar
• Rios-Soto, L., Téllez-Valencia, A., Sierra-Campos, E., Valdez-Solana, M., Cisneros-Martínez, J., Gómez Palacio-Gastélum, M., Castillo-Villanueva, A., & Avitia-Domínguez, C. (2021). Finding the first potential inhibitors of shikimate kinase from methicillin resistant Staphylococcus aureus through computer-assisted drug design. Molecules, 26(21), 6736. https://doi.org/10.3390/molecules26216736
   PubMed Web of Science ®Google Scholar
• Roberts, C. W., Roberts, F., Lyons, R. E., Kirisits, M. J., Mui, E. J., Finnerty, J., Johnson, J. J., Ferguson, D. J., Coggins, J. R., Krell, T., Coombs, G. H., Milhous, W. K., Kyle, D. E., Tzipori, S., Barnwell, J., Dame, J. B., Carlton, J., & McLeod, R. (2002). The shikimate pathway and its branches in apicomplexan parasites. The Journal of Infectious Diseases, 185(s1), S25–S36. https://doi.org/10.1086/338004
   PubMedGoogle Scholar
• Sahu, P. K., Mohapatra, P. K., Rajani, D. P., & Raval, M. K. (2020). Structure-based discovery of narirutin as a shikimate kinase inhibitor with anti-tubercular potency. Current Computer-Aided Drug Design, 16(5), 523–529. https://doi.org/10.2174/1573409915666191025112150
   PubMed Web of Science ®Google Scholar
• Sarathy, J. P., Ragunathan, P., Shin, J., Cooper, C. B., Upton, A. M., Grüber, G., & Dick, T. (2019). TBAJ-876 retains bedaquiline’s activity against subunits c and ε of Mycobacterium tuberculosis F-ATP synthase. Antimicrobial Agents and Chemotherapy, 63(10), e01191. https://doi.org/10.1128/AAC.01191-19
   PubMed Web of Science ®Google Scholar
• Shirude, P. S., Shandil, R. K., Manjunatha, M. R., Sadler, C., Panda, M., Panduga, V., Reddy, J., Saralaya, R., Nanduri, R., Ambady, A., Ravishankar, S., Sambandamurthy, V. K., Humnabadkar, V., Jena, L. K., Suresh, R. S., Srivastava, A., Prabhakar, K. R., Whiteaker, J., McLaughlin, R. E., … Chatterji, M. (2014). Lead optimization of 1,4-azaindoles as antimycobacterial agents. Journal of Medicinal Chemistry, 57(13), 5728–5737. https://doi.org/10.1021/jm500571f
   PubMed Web of Science ®Google Scholar
• Simithy, J., Fuanta, N. R., Alturki, M., Hobrath, J. V., Wahba, A. E., Pina, I., Rath, J., Hamann, M. T., DeRuiter, J., Goodwin, D. C., & Calderón, A. I. (2018). Slow-binding inhibition of mycobacterium tuberculosis shikimate kinase by manzamine alkaloids. Biochemistry, 57(32), 4923–4933. https://doi.org/10.1021/acs.biochem.8b00231
   PubMed Web of Science ®Google Scholar
• Simithy, J., Reeve, N., Hobrath, J. V., Reynolds, R. C., & Calderón, A. I. (2014). Identification of shikimate kinase inhibitors among anti-Mycobacterium tuberculosis compounds by LC-MS. Tuberculosis, 94(2), 152–158. https://doi.org/10.1016/j.tube.2013.12.004
   PubMed Web of Science ®Google Scholar
• Stec, J., Onajole, O. K., Lun, S., Guo, H., Merenbloom, B., Vistoli, G., Bishai, W. R., & Kozikowski, A. P. (2016). Indole-2-carboxamide-based MmpL3 inhibitors show exceptional anti-tubercular activity in an animal model of tuberculosis infection. Journal of Medicinal Chemistry, 59(13), 6232–6247. https://doi.org/10.1021/acs.jmedchem.6b00415
   PubMed Web of Science ®Google Scholar
• Stoffels, K., Allix-Béguec, C., Groenen, G., Wanlin, M., Berkvens, D., Mathys, V., Supply, P., & Fauville-Dufaux, M. (2013). From multidrug- to extensively drug-resistant tuberculosis: Upward trends as seen from a 15-year nationwide study. PLoS One, 8(5), e63128. https://doi.org/10.1371/journal.pone.0063128
   PubMed Web of Science ®Google Scholar
• Stover, C. K., Warrener, P., VanDevanter, D. R., Sherman, D. R., Arain, T. M., Langhorne, M. H., Anderson, S. W., Towell, J. A., Yuan, Y., McMurray, D. N., Kreiswirth, B. N., Barry, C. E., & Baker, W. R. (2000). A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis. Nature, 405(6789), 962–966. https://doi.org/10.1038/35016103. https://doi.org/10.1038/35016103
   PubMed Web of Science ®Google Scholar
• Su, C. C., Klenotic, P. A., Bolla, J. R., Purdy, G. E., Robinson, C. V., & Yu, E. W. (2019). MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine. Proceedings of the National Academy of Sciences, 116(23), 11241–11246. https://doi.org/10.1073/pnas.1901346116
   PubMed Web of Science ®Google Scholar
• Takahashi, Y., Igarashi, M., Miyake, T., Soutome, H., Ishikawa, K., Komatsuki, Y., Koyama, Y., Nakagawa, N., Hattori, S., Inoue, K., Doi, N., & Akamatsu, Y. (2013). Novel semisynthetic antibiotics from caprazamycins A-G: Caprazene derivatives and their antibacterial activity. The Journal of Antibiotics, 66(3), 171–178. https://doi.org/10.1038/ja.2013.9
   PubMed Web of Science ®Google Scholar
• TB Alliance. (2019, June 6). Pretomanid and BPaL regimen for treatment of highly resistant tuberculosis [Paper presentation]. Oral Presentation at: Antimicrobial Drugs Advisory Committee, Silver Spring, MD. https://www.fda.gov/media/128001/download
   Google Scholar
• TB Alliance. (2022). https://www.Tballiance.org/portfolio
   Google Scholar
• TB Database. (2021). http://Tbdb.bu.edu/cgi-bin/GeneDetails.html?id=SRv2539c
   Google Scholar
• Tenero, D., Derimanov, G., Carlton, A., Tonkyn, J., Davies, M., Cozens, S., Gresham, S., Gaudion, A., Puri, A., Muliaditan, M., Rullas-Trincado, J., Mendoza-Losana, A., Skingsley, A., & Barros-Aguirre, D. (2019). First-time-in-human study and prediction of early bactericidal activity for GSK3036656, a potent leucyl-tRNA synthetase inhibitor for tuberculosis treatment. Antimicrobial Agents and Chemotherapy, 63(8), e00240. https://doi.org/10.1128/AAC.00240-19
   PubMed Web of Science ®Google Scholar
• Thakur, G., Thakur, S., & Thakur, H. (2021). Status and challenges for tuberculosis control in India - Stakeholders’ perspective. Indian Journal of Tuberculosis, 68(3), 334–339. https://doi.org/10.1016/j.ijtb.2020.10.001
   PubMedGoogle Scholar
• Thomsen, R., & Christensen, M. H. (2006). MolDock: A new technique for high-accuracy molecular docking. Journal of Medicinal Chemistry, 49(11), 3315–3321. https://doi.org/10.1021/jm051197e
   PubMed Web of Science ®Google Scholar
• Tran, A. T., Watson, E. E., Pujari, V., Conroy, T., Dowman, L. J., Giltrap, A. M., Pang, A., Wong, W. R., Linington, R. G., Mahapatra, S., Saunders, J., Charman, S. A., West, N. P., Bugg, T. D., Tod, J., Dowson, C. G., Roper, D. I., Crick, D. C., Britton, W. J., & Payne, R. J. (2017). Sansanmycin natural product analogues as potent and selective anti-mycobacterials that inhibit lipid I biosynthesis. Nature Communications, 8(1), 14414. https://doi.org/10.1038/ncomms14414
   PubMedGoogle Scholar
• UniProt Database. (2021). https://www.uniprot.org/uniprot/P9WPY3#function
   Google Scholar
• US Food and Drug Administration. (2022). Drug approvals and databases. https://www.fda.gov/drugs/development-approval-process-drugs/drug-approvals-and-databases
   Google Scholar
• von Groote-Bidlingmaier, F., Patientia, R., Sanchez, E., Balanag, V., Ticona, E., Segura, P., Cadena, E., Yu, C., Cirule, A., Lizarbe, V., Davidaviciene, E., Domente, L., Variava, E., Caoili, J., Danilovits, M., Bielskiene, V., Staples, S., Hittel, N., Petersen, C., … Gupta, R. (2019). Efficacy and safety of delamanid in combination with an optimised background regimen for treatment of multidrug-resistant tuberculosis: A multicentre, randomised, double-blind, placebo-controlled, parallel group phase 3 trial. The Lancet Respiratory Medicine, 7(3), 249–259. https://doi.org/10.1016/S2213-2600(18)30426-0
   PubMed Web of Science ®Google Scholar
• Wallis, R. S., Dawson, R., Friedrich, S. O., Venter, A., Paige, D., Zhu, T., Silvia, A., Gobey, J., Ellery, C., Zhang, Y., Eisenach, K., Miller, P., & Diacon, A. H. (2014). Mycobactericidal activity of sutezolid (PNU-100480) in sputum (EBA) and blood (WBA) of patients with pulmonary tuberculosis. PLoS One, 9(4), e94462. https://doi.org/10.1371/journal.pone.0094462
   PubMed Web of Science ®Google Scholar
• Weinstein, L. H., Porter, C. A., & Laurencot, H. J. (1962). Role of the shikimic acid pathway in the formation of tryptophan in higher plants: Evidence for an alternative pathway in the bean. Evidence for an Alternative Pathway in the Bean, 194, 205–206. https://ui.adsabs.harvard.edu/link_gateway/1962Natur.194.205W/ https://doi.org/10.1038/194205a0
   Google Scholar
• World Health Organization. (2009). Global tuberculosis control 2009: Epidemiology, strategy, financing: WHO report 2009. World Health Organization 303. https://apps.who.int/iris/bitstream/handle/10665/44241/9789241598866_eng.pdf
   Google Scholar
• Wu, M. C., Styles, M. Q., Law, B. J., Struck, A. W., Nunns, L., & Micklefield, J. (2015). Engineered biosynthesis of enduracidin lipoglycopeptide antibiotics using the ramoplanin mannosyltransferase Ram29. Microbiology (Reading, England), 161(7), 1338–1347. https://doi.org/10.1099/mic.0.000095
   Google Scholar
• Xu, J., Wang, B., Fu, L., Zhu, H., Guo, S., Huang, H., Yin, D., Zhang, Y., & Lu, Y. (2019). In Vitro and In Vivo Activities of the Riminophenazine TBI-166 against Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy, 63(5), e02155-18. https://doi.org/10.1128/AAC.02155-18
   PubMed Web of Science ®Google Scholar
• Yano, T., Kassovska-Bratinova, S., Teh, J. S., Winkler, J., Sullivan, K., Isaacs, A., Schechter, N. M., & Rubin, H. (2011). Reduction of clofazimine by mycobacterial type 2 NADH: Quinone oxidoreductase: A pathway for the generation of bactericidal levels of reactive oxygen species. The Journal of Biological Chemistry, 286(12), 10276–10287. https://doi.org/10.1074/jbc.M110.200501
   PubMed Web of Science ®Google Scholar
• Young Lag, C. (2018). Delpazolid (LCB01-0371), Oxazolidinone antibiotic for MDR-TB LegoChem Biosciences. In 2018 WGND Annual Meeting. https://www.newTbdrugs.org/sites/default/files/meetings/files/07_WGND%20presentation-Lego-Chem%20Bio.pdf
   Google Scholar
• Zong, Z., Jing, W., Shi, J., Wen, S., Zhang, T., Huo, F., Shang, Y., Liang, Q., Huang, H., & Pang, Y. (2018). Comparison of in vitro activity and MIC distributions between the novel oxazolidinone delpazolid and linezolid against multidrug-resistant and extensively drug-resistant Mycobacterium tuberculosis in China. Antimicrobial Agents and Chemotherapy, 62(8), e00165-18. https://doi.org/10.1128/AAC.00165-18
   PubMed Web of Science ®Google Scholar