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Volumn 52, Issue 21, 2009, Pages 6539-6542

Coordination chemistry based approach to lipophilic inhibitors of 1-deoxy-D-xylulose-5-phosphate reductoisomerase

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXY DEXTRO XYLULOSE 5 PHOSPHATE REDUCTOISOMERASE; AMPICILLIN; FOSMIDOMYCIN; ISOMERASE; KANAMYCIN; UNCLASSIFIED DRUG;

EID: 71049170515     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9012592     Document Type: Article
Times cited : (58)

References (33)
  • 1
    • 7244250314 scopus 로고    scopus 로고
    • Antibiotics: A shot in the arm
    • Leeb, M. Antibiotics: a shot in the arm. Nature 2004, 431, 892-893.
    • (2004) Nature , vol.431 , pp. 892-893
    • Leeb, M.1
  • 2
    • 7244245763 scopus 로고    scopus 로고
    • Antibiotics at the crossroads
    • Nathan, C. Antibiotics at the crossroads. Nature 2004, 431, 899-902.
    • (2004) Nature , vol.431 , pp. 899-902
    • Nathan, C.1
  • 3
    • 3042782938 scopus 로고    scopus 로고
    • The MEP pathway: A new target for the development of herbicides, antibiotics and antimalarial drugs
    • (a) Rodriguez-Concepcion, M. The MEP pathway: a new target for the development of herbicides, antibiotics and antimalarial drugs. Curr. Pharm. Des. 2004, 10, 2391-2400.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2391-2400
    • Rodriguez-Concepcion, M.1
  • 4
    • 0041589189 scopus 로고    scopus 로고
    • The methylerythritol phosphate pathway and its significance as a novel drug target
    • (b) Testa, C. A.; Brown, M. J. The methylerythritol phosphate pathway and its significance as a novel drug target. Curr. Pharm. Biotechnol. 2003, 4, 248-259.
    • (2003) Curr. Pharm. Biotechnol. , vol.4 , pp. 248-259
    • Testa, C.A.1    Brown, M.J.2
  • 5
    • 0019256502 scopus 로고
    • In vitro and in vivo antibacterial activities of FR-31564, a new phosphonic acid antibiotic
    • Mine, Y.; Kamimura, T.; Nonoyama, S.; Nishida, M.; Goto, S.; Kuwahara, S. In vitro and in vivo antibacterial activities of FR-31564, a new phosphonic acid antibiotic. J. Antibiot. (Tokyo) 1980, 33, 36-43.
    • (1980) J. Antibiot. (Tokyo) , vol.33 , pp. 36-43
    • Mine, Y.1    Kamimura, T.2    Nonoyama, S.3    Nishida, M.4    Goto, S.5    Kuwahara, S.6
  • 6
    • 0032558613 scopus 로고    scopus 로고
    • Fosmidomycin, a specific inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in the nonmevalonate pathway for terpenoid biosynthesis
    • Kuzuyama, T.; Shimizu, T.; Takahashi, S.; Seto, H. Fosmidomycin, a specific inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in the nonmevalonate pathway for terpenoid biosynthesis. Tetrahedron Lett. 1998, 39, 7913-7916.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 7913-7916
    • Kuzuyama, T.1    Shimizu, T.2    Takahashi, S.3    Seto, H.4
  • 9
    • 28844484972 scopus 로고    scopus 로고
    • 1-Deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) from Mycobacterium tuberculosis: Towards understanding mycobacterial resistance to fosmidomycin
    • (a) Dhiman, R. K.; Schaeffer, M. L.; Bailey, A. M.; Testa, C. A.; Scherman, H.; Crick, D. C. 1-Deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) from Mycobacterium tuberculosis: towards understanding mycobacterial resistance to fosmidomycin. J. Bacteriol. 2005, 187, 8395-8402.
    • (2005) J. Bacteriol. , vol.187 , pp. 8395-8402
    • Dhiman, R.K.1    Schaeffer, M.L.2    Bailey, A.M.3    Testa, C.A.4    Scherman, H.5    Crick, D.C.6
  • 10
    • 44849135047 scopus 로고    scopus 로고
    • Dxr is essential in Mycobacterium tuberculosis and fosmidomycin resistance is due to a lack of uptake
    • DOI 10.1186/1471-2180-8-78
    • (b) Brown, A. C.; Parish, T. DXR is essential in Mycobacterium tuberculosis and fosmidomycin resistance is due to a lack of uptake. BMC Microbiol. 2008, 8, 78-86. (Pubitemid 351793258)
    • (2008) BMC Microbiology , vol.8 , pp. 78
    • Brown, A.C.1    Parish, T.2
  • 11
    • 48249107154 scopus 로고    scopus 로고
    • Evaluation of in vitro antibacterial activity of fosmidomycin and its derivatives
    • For development based on fosmidomycin, see the following: (a)
    • For development based on fosmidomycin, see the following: (a) Shtannikov, A. V.; Sergeeva, E. E.; Biketov, S. F.; Ostrovskii, D. N. Evaluation of in vitro antibacterial activity of fosmidomycin and its derivatives. Antibiot. Khimioter. 2007, 52, 3-9.
    • (2007) Antibiot. Khimioter. , vol.52 , pp. 3-9
    • Shtannikov, A.V.1    Sergeeva, E.E.2    Biketov, S.F.3    Ostrovskii, D.N.4
  • 12
    • 14244257854 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis as a target for antibacterial and antiparasitic drugs: Phosphonohydroxamic acids as inhibitors of deoxyxylulose phosphate reducto-isomerase
    • DOI 10.1042/BJ20041378
    • (b) Kuntz, L.; Tritsch, D.; Grosdemange-Billiard, C.; Hemmerlin, A.; Willem, A.; Bach, T. J.; Rohmer, M. Isoprenoid biosynthesis as a target for antibacterial and antiparasitic drugs: phosphonohydroxamic acids as inhibitors of deoxyxylulose phosphate reducto-isomerase. Biochem. J. 2005, 386, 127-135. (Pubitemid 40289232)
    • (2005) Biochemical Journal , vol.386 , Issue.1 , pp. 127-135
    • Kuntz, L.1    Tritsch, D.2    Grosdemange-Billiard, C.3    Hemmerlin, A.4    Willem, A.5    Bach, T.J.6    Rohmer, M.7
  • 13
    • 26944489968 scopus 로고    scopus 로고
    • A fragment-based approach to understanding inhibition of 1-deoxy-D-xylulose-5-phosphate reductoisomerase
    • (c) Merckle, L.; de Andres-Gomez, A.; Dick, B.; Cox, R. J.; Godfrey, C. R. A fragment-based approach to understanding inhibition of 1-deoxy-D-xylulose- 5-phosphate reductoisomerase. ChemBioChem 2005, 6, 1866-1874.
    • (2005) ChemBioChem , vol.6 , pp. 1866-1874
    • Merckle, L.1    De Andres-Gomez, A.2    Dick, B.3    Cox, R.J.4    Godfrey, C.R.5
  • 14
    • 43549115217 scopus 로고    scopus 로고
    • Synthesis and analysis of a fluorinated product analogue as an inhibitor for 1-deoxy-D-xylulose 5-phosphate reductoisomerase
    • (d) Munos, J. W.; Pu, X.; Liu, H. W. Synthesis and analysis of a fluorinated product analogue as an inhibitor for 1-deoxy-D-xylulose 5-phosphate reductoisomerase. Bioorg. Med. Chem. Lett. 2008, 18, 3090-3094.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3090-3094
    • Munos, J.W.1    Pu, X.2    Liu, H.W.3
  • 15
    • 34748895608 scopus 로고    scopus 로고
    • Novel deoxyxylulosephosphate-reductoisomerase inhibitors: Fosmidomycin derivatives with spacious acyl residues
    • (e) Ortmann, R.; Wiesner, J.; Silber, K.; Klebe, G.; Jomaa, H.; Schlitzer, M. Novel deoxyxylulosephosphate-reductoisomerase inhibitors: fosmidomycin derivatives with spacious acyl residues. Arch. Pharm. (Weinheim, Ger.) 2007, 340, 483-490.
    • (2007) Arch. Pharm. (Weinheim, Ger.) , vol.340 , pp. 483-490
    • Ortmann, R.1    Wiesner, J.2    Silber, K.3    Klebe, G.4    Jomaa, H.5    Schlitzer, M.6
  • 16
    • 18744377281 scopus 로고    scopus 로고
    • AFMoC enhances predictivity of 3D QSAR: A case study with DOXP-reductoisomerase
    • (f) Silber, K.; Heidler, P.; Kurz, T.; Klebe, G. AFMoC enhances predictivity of 3D QSAR: a case study with DOXP-reductoisomerase. J. Med. Chem. 2005, 48, 3547-3563.
    • (2005) J. Med. Chem. , vol.48 , pp. 3547-3563
    • Silber, K.1    Heidler, P.2    Kurz, T.3    Klebe, G.4
  • 17
    • 32844461335 scopus 로고    scopus 로고
    • Evaluation of fosmidomycin analogs as inhibitors of the Synechocystis sp. PCC6803 1-deoxy-D-xylulose 5-phosphate reductoisomerase
    • (g) Woo, Y. H.; Fernandes, R. P.; Proteau, P. J. Evaluation of fosmidomycin analogs as inhibitors of the Synechocystis sp. PCC6803 1-deoxy-D-xylulose 5-phosphate reductoisomerase. Bioorg. Med. Chem. 2006, 14, 2375-2385.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 2375-2385
    • Woo, Y.H.1    Fernandes, R.P.2    Proteau, P.J.3
  • 18
    • 33745178164 scopus 로고    scopus 로고
    • Synthesis and antimalarial activity of chain substituted pivaloyloxymethyl ester analogues of fosmidomycin and FR900098
    • (h) Kurz, T.; Schlüter, K.; Kaula, U.; Bergmann, B.; Walter, R. D.; Geffken, D. Synthesis and antimalarial activity of chain substituted pivaloyloxymethyl ester analogues of fosmidomycin and FR900098. Bioorg. Med. Chem. 2006, 14, 5121-5135.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 5121-5135
    • Kurz, T.1    Schlüter, K.2    Kaula, U.3    Bergmann, B.4    Walter, R.D.5    Geffken, D.6
  • 22
    • 4444236556 scopus 로고    scopus 로고
    • Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5- phosphate reductoisomerase complexes
    • For non-fosmidomycin-like inhibitors, see the following: (l)
    • For non-fosmidomycin-like inhibitors, see the following: (l) Yajima, S.; Hara, K.; Sanders, J. M.; Yin, F.; Ohsawa, K.; Wiesner, J.; Jomaa, H.; Oldfield, E. Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5- phosphate reductoisomerase complexes. J. Am. Chem. Soc. 2004, 126, 10824-10825.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10824-10825
    • Yajima, S.1    Hara, K.2    Sanders, J.M.3    Yin, F.4    Ohsawa, K.5    Wiesner, J.6    Jomaa, H.7    Oldfield, E.8
  • 23
    • 0042064058 scopus 로고    scopus 로고
    • High-throughput screen for inhibitors of 1-deoxy-D-xylulose 5-phosphate reductoisomerase by surrogate ligand competition
    • For high-throughput screening, see the following: (m)
    • For high-throughput screening, see the following: (m) Gottlin, E. B.; Benson, R. E.; Conary, S.; Antonio, B.; Duke, K.; Payne, E. S.; Ashraf, S. S.; Christensen, D. J. High-throughput screen for inhibitors of 1-deoxy-D-xylulose 5-phosphate reductoisomerase by surrogate ligand competition. J. Biomol. Screening 2003, 8, 332-339.
    • (2003) J. Biomol. Screening , vol.8 , pp. 332-339
    • Gottlin, E.B.1    Benson, R.E.2    Conary, S.3    Antonio, B.4    Duke, K.5    Payne, E.S.6    Ashraf, S.S.7    Christensen, D.J.8
  • 25
    • 9644301008 scopus 로고    scopus 로고
    • The crystal structure of E. coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation
    • MacSweeney, A.; Lange, R.; Fernandes, R. P.; Schulz, H.; Dale, G. E.; Douangamath, A.; Proteau, P. J.; Oefner, C. The crystal structure of E. coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation. J. Mol. Biol. 2005, 345, 115-127.
    • (2005) J. Mol. Biol. , vol.345 , pp. 115-127
    • MacSweeney, A.1    Lange, R.2    Fernandes, R.P.3    Schulz, H.4    Dale, G.E.5    Douangamath, A.6    Proteau, P.J.7    Oefner, C.8
  • 26
    • 49949138005 scopus 로고
    • Solution stability constants of some metal complexes of derivatives of catechol
    • Athavale, V. T.; Prabhu, L. H.; Vartak, D. G. Solution stability constants of some metal complexes of derivatives of catechol. J. Inorg. Nucl. Chem. 1966, 28, 1237-1249.
    • (1966) J. Inorg. Nucl. Chem. , vol.28 , pp. 1237-1249
    • Athavale, V.T.1    Prabhu, L.H.2    Vartak, D.G.3
  • 27
    • 0011283177 scopus 로고
    • Theomodynamic metal-ligand stability constants of alkali eath metals with N-p-chlorophenylbenzohydroxamic acid
    • Agrawal, Y. K.; Roshania, R. D. Theomodynamic metal-ligand stability constants of alkali eath metals with N-p-chlorophenylbenzohydroxamic acid. Z. Phys. Chem. (Leipzig) 1982, 263, 822-826.
    • (1982) Z. Phys. Chem. (Leipzig) , vol.263 , pp. 822-826
    • Agrawal, Y.K.1    Roshania, R.D.2
  • 28
    • 71049114346 scopus 로고    scopus 로고
    • www.schrodinger.com.
  • 29
    • 4444341426 scopus 로고    scopus 로고
    • The evolution of the matrix metalloproteinase inhibitor drug discovery program at abbott laboratories
    • For hydroxamate based matrix metalloproteinase inhibitors, see the following: (a)
    • For hydroxamate based matrix metalloproteinase inhibitors, see the following: (a) Wada, C. K. The evolution of the matrix metalloproteinase inhibitor drug discovery program at abbott laboratories. Curr. Top. Med. Chem. 2004, 4, 1255-1267.
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 1255-1267
    • Wada, C.K.1
  • 30
    • 4644314055 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin A after intraperitoneal administration to mice
    • For hydroxamate based histone deacetylase inhibitors, see the following: (b)
    • For hydroxamate based histone deacetylase inhibitors, see the following: (b) Sanderson, L.; Taylor, G. W.; Aboagye, E. O.; Alao, J. P.; Latigo, J. R.; Coombes, R. C.; Vigushin, D. M. Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin A after intraperitoneal administration to mice. Drug Metab. Dispos. 2004, 32, 1132-1138.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1132-1138
    • Sanderson, L.1    Taylor, G.W.2    Aboagye, E.O.3    Alao, J.P.4    Latigo, J.R.5    Coombes, R.C.6    Vigushin, D.M.7
  • 31
    • 34047168930 scopus 로고    scopus 로고
    • The design of inhibitors for medicinally relevant metalloproteins
    • (a) Jacobsen, F. E.; Lewis, J. A.; Cohen, S. M. The design of inhibitors for medicinally relevant metalloproteins. ChemMedChem 2007, 2, 152-171.
    • (2007) ChemMedChem , vol.2 , pp. 152-171
    • Jacobsen, F.E.1    Lewis, J.A.2    Cohen, S.M.3
  • 32
    • 33644944087 scopus 로고    scopus 로고
    • A new role for old ligands: Discerning chelators for zinc metalloproteinases
    • (b) Jacobsen, F. E.; Lewis, J. A.; Cohen, S. M. A new role for old ligands: discerning chelators for zinc metalloproteinases. J. Am. Chem. Soc. 2006, 128, 3156-3157.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3156-3157
    • Jacobsen, F.E.1    Lewis, J.A.2    Cohen, S.M.3
  • 33
    • 71049189705 scopus 로고    scopus 로고
    • See Supporting Information for detailed synthesis and references
    • See Supporting Information for detailed synthesis and references.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.