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Volumn 54, Issue 13, 2011, Pages 4600-4610

Structure-based design of a new series of d-glutamic acid based inhibitors of bacterial UDP-N-acetylmuramoyl-l-alanine: D-glutamate ligase (MurD)

Author keywords

[No Author keywords available]

Indexed keywords

2 [3 [[1 CARBOXY N [4 [(4 OXO 2 THIOXOTHIAZOLIDIN 5 YLIDENE)METHYL]PHENYL]FORMAMIDO]METHYL]BENZAMIDO]PENTANEDIOIC ACID; 2 [3 [[2 CARBOXY N [4 [(4 OXO 2 THIOXOTHIAZOLIDIN 5 YLIDENE)METHYL]PHENYL]ACETAMIDO]METHYL]BENZAMIDO]PENTANEDIOIC ACID; 2 [3 [[3 CARBOXY N [4 [(4 OXO 2 THIOXOTHIAZOLIDIN 5 YLIDENE)METHYL]PHENYL]PROPANAMIDO]METHYL]BENZAMIDO]PENTANEDIOIC ACID; ANTIINFECTIVE AGENT; BENZYLIDENE DERIVATIVE; DIMETHYL 2 [3 [[2 ETHOXY 2 OXO N [4 [(4 OXO 2 THIOXOTHIAZOLIDIN 5 YLIDENE)METHYL]PHENYL]ACETAMIDO]METHYL]BENZAMIDO]PENTANEDIOIC ACID; DIMETHYL 2 [3 [[4 METHOXY 2 OXO N [4 [(4 OXO 2 THIOXOTHIAZOLIDIN 5 YLIDENE)METHYL]PHENYL]BUTANAMIDO]METHYL]BENZAMIDO]PENTANEDIOIC ACID; GLUTAMIC ACID DERIVATIVE; LIGASE; LIGASE INHIBITOR; PROTEIN MURD; THIAZOLIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79960189764     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm2002525     Document Type: Article
Times cited : (50)

References (44)
  • 1
    • 0037439518 scopus 로고    scopus 로고
    • Bacterial resistance: Origins, epidemiology, and impact
    • Livermore, D. M. Bacterial resistance: origins, epidemiology, and impact Clin. Infect. Dis. 2003, 36, 11-23
    • (2003) Clin. Infect. Dis. , vol.36 , pp. 11-23
    • Livermore, D.M.1
  • 3
    • 33644517894 scopus 로고    scopus 로고
    • Unmet medical needs in antibacterial therapy
    • Rice, L. B. Unmet medical needs in antibacterial therapy Biochem. Pharmacol. 2006, 71, 991-5
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 991-5
    • Rice, L.B.1
  • 4
    • 35948972121 scopus 로고    scopus 로고
    • Superbugs in the coming new decade; multidrug resistance and prospects for treatment of Staphylococcus aureus, Enterococcus spp. and Pseudomonas aeruginosa in 2010
    • DOI 10.1016/j.mib.2007.07.004, PII S136952740700094X, Antimicrobials/Genomics
    • Nordmann, P.; Naas, T.; Fortineau, N.; Poirel, L. Superbugs in the coming new decade; multidrug resistance and prospects for treatment of Staphylococcus aureus, Enterococcus spp. and Pseudomonas aeruginosa in 2010 Curr. Opin. Microbiol. 2007, 10, 436-440 (Pubitemid 350064580)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.5 , pp. 436-440
    • Nordmann, P.1    Naas, T.2    Fortineau, N.3    Poirel, L.4
  • 5
    • 39149110299 scopus 로고    scopus 로고
    • Peptidoglycan structure and architecture
    • DOI 10.1111/j.1574-6976.2007.00094.x
    • Vollmer, W.; Blanot, D.; de Pedro, M. A. Peptidoglycan structure and architecture FEMS Microbiol. Rev. 2008, 32, 149-167 (Pubitemid 351257814)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 149-167
    • Vollmer, W.1    Blanot, D.2    De Pedro, M.A.3
  • 6
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of the bacterial peptidoglycan monomer unit
    • DOI 10.1039/a804532a
    • van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit Nat. Prod. Rep. 2001, 18, 503-519 (Pubitemid 33016991)
    • (2001) Natural Product Reports , vol.18 , Issue.5 , pp. 503-519
    • Van Heijenoort, J.1
  • 8
    • 0037223505 scopus 로고    scopus 로고
    • Structure and function of the Mur enzymes: Development of novel inhibitors
    • DOI 10.1046/j.1365-2958.2003.03289.x
    • El Zoeiby, A.; Sanschagrin, F.; Levesque, R. C. Structure and function of the Mur enzymes: development of novel inhibitors Mol. Microbiol. 2003, 47, 1-12 (Pubitemid 36051319)
    • (2003) Molecular Microbiology , vol.47 , Issue.1 , pp. 1-12
    • El Zoeiby, A.1    Sanschagrin, F.2    Levesque, R.C.3
  • 10
    • 0036403545 scopus 로고    scopus 로고
    • MurC and MurD synthetases of peptidoglycan biosynthesis: Borohydride trapping of Acyl-phosphate intermediates
    • DOI 10.1016/S0076-6879(02)54015-5
    • Bouhss, A.; Dementin, S.; van Heijenoort, J.; Parquet, C.; Blanot, D. MurC and MurD synthetases of peptidoglycan biosynthesis: borohydride trapping of acyl-phosphate intermediates Methods Enzymol. 2002, 354, 189-196 (Pubitemid 35217263)
    • (2002) Methods in Enzymology , vol.354 , pp. 189-196
    • Bouhss, A.1    Dementin, S.2    Van Heijenoort, J.3    Parquet, C.4    Blanot, D.5
  • 11
    • 0030960337 scopus 로고    scopus 로고
    • Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase
    • DOI 10.1021/bi970266r
    • Emanuele, J. J.; Jin, H. Y.; Yanchunas, J.; Villafranca, J. J. Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate- N -acetylmuramate: l -alanine ligase Biochemistry 1997, 36, 7264-7271 (Pubitemid 27258143)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 7264-7271
    • Emanuele Jr., J.J.1    Jin, H.2    Yanchunas Jr., J.3    Villafranca, J.J.4
  • 12
    • 0030471790 scopus 로고    scopus 로고
    • Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide d -alanyl- d -alanine-adding enzyme: Use of a glutathione S -transferase fusion
    • Anderson, M. S.; Eveland, S. S.; Onishi, H. R.; Pompliano, D. L. Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide d -alanyl- d -alanine-adding enzyme: use of a glutathione S -transferase fusion Biochemistry 1996, 35, 16264-16269
    • (1996) Biochemistry , vol.35 , pp. 16264-16269
    • Anderson, M.S.1    Eveland, S.S.2    Onishi, H.R.3    Pompliano, D.L.4
  • 13
    • 0030927105 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli
    • DOI 10.1093/emboj/16.12.3416
    • Bertrand, J. A.; Auger, G.; Fanchon, E.; Martin, L.; Blanot, D.; van Heijenoort, J.; Dideberg, O. Crystal structure of UDP- N -acetylmuramoyl- l -alanine: d -glutamate ligase from Escherichia coli EMBO J. 1997, 16, 3416-3425 (Pubitemid 27250037)
    • (1997) EMBO Journal , vol.16 , Issue.12 , pp. 3416-3425
    • Bertrand, J.A.1    Auger, G.2    Fanchon, E.3    Martin, L.4    Blanot, D.5    Van Heijenoort, J.6    Dideberg, O.7
  • 15
    • 34249703449 scopus 로고    scopus 로고
    • Structural and Functional Characterization of Enantiomeric Glutamic Acid Derivatives as Potential Transition State Analogue Inhibitors of MurD Ligase
    • DOI 10.1016/j.jmb.2007.04.048, PII S0022283607005402
    • Kotnik, M.; Humljan, J.; Contreras-Martel, C.; Oblak, M.; Kristan, K.; Hervé, M.; Blanot, D.; Urleb, U.; Gobec, S.; Dessen, A.; Šolmajer, T. Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase J. Mol. Biol. 2007, 370, 107-115 (Pubitemid 46830698)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.1 , pp. 107-115
    • Kotnik, M.1    Humljan, J.2    Contreras-Martel, C.3    Oblak, M.4    Kristan, K.5    Herve, M.6    Blanot, D.7    Urleb, U.8    Gobec, S.9    Dessen, A.10    Solmajer, T.11
  • 16
    • 57349132464 scopus 로고    scopus 로고
    • Novel naphthalene- N -sulfonyl- d -glutamic acid derivatives as inhibitors of MurD, a key peptidoglycan biosynthesis enzyme
    • Humljan, J.; Kotnik, M.; Contreras-Martel, C.; Blanot, D.; Urleb, U.; Dessen, A.; Šolmajer, T.; Gobec, S. Novel naphthalene- N -sulfonyl- d -glutamic acid derivatives as inhibitors of MurD, a key peptidoglycan biosynthesis enzyme J. Med. Chem. 2008, 51, 7486-7494
    • (2008) J. Med. Chem. , vol.51 , pp. 7486-7494
    • Humljan, J.1    Kotnik, M.2    Contreras-Martel, C.3    Blanot, D.4    Urleb, U.5    Dessen, A.6    Šolmajer, T.7    Gobec, S.8
  • 17
    • 0029867778 scopus 로고    scopus 로고
    • Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis
    • DOI 10.1021/jo951780a
    • Tanner, M. E.; Vaganay, S.; van Heijenoort, J.; Blanot, D. Phosphinate Inhibitors of the d -glutamic acid-adding enzyme of peptidoglycan biosynthesis J. Org. Chem. 1996, 61, 1756-1760 (Pubitemid 26106393)
    • (1996) Journal of Organic Chemistry , vol.61 , Issue.5 , pp. 1756-1760
    • Tanner, M.E.1    Vaganay, S.2    Van Heijenoort, J.3    Blanot, D.4
  • 18
    • 27944446768 scopus 로고    scopus 로고
    • Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD
    • DOI 10.1016/j.bmcl.2005.09.086, PII S0960894X05012667
    • Štrancar, K.; Blanot, D.; Gobec, S. Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD Bioorg. Med. Chem. Lett. 2006, 16, 343-348 (Pubitemid 41680624)
    • (2006) Bioorganic and Medicinal Chemistry Letters , vol.16 , Issue.2 , pp. 343-348
    • Strancar, K.1    Blanot, D.2    Gobec, S.3
  • 19
    • 65349160436 scopus 로고    scopus 로고
    • Discovery of novel benzene 1,3-dicarboxylic acid inhibitors of bacterial MurD and MurE ligases by structure-based virtual screening approach
    • Perdih, A.; Kovač, A.; Wolber, G.; Blanot, D.; Gobec, S.; Šolmajer, T. Discovery of novel benzene 1,3-dicarboxylic acid inhibitors of bacterial MurD and MurE ligases by structure-based virtual screening approach Bioorg. Med. Chem. Lett. 2009, 19, 2668-2673
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2668-2673
    • Perdih, A.1    Kovač, A.2    Wolber, G.3    Blanot, D.4    Gobec, S.5    Šolmajer, T.6
  • 20
    • 61549097473 scopus 로고    scopus 로고
    • Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening
    • Turk, S.; Kovač, A.; Boniface, A.; Bostock, J. M.; Chopra, I.; Blanot, D.; Gobec, S. Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening Bioorg. Med. Chem. 2009, 17, 1884-1889
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1884-1889
    • Turk, S.1    Kovač, A.2    Boniface, A.3    Bostock, J.M.4    Chopra, I.5    Blanot, D.6    Gobec, S.7
  • 22
    • 33744983912 scopus 로고    scopus 로고
    • Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme
    • DOI 10.1016/j.peptides.2006.01.017, PII S0196978106000660
    • Paradis-Bleau, C.; Beaumont, M.; Boudreault, L.; Lloyd, A.; Sanschagrin, F.; Bugg, T. D.; Levesque, R. C. Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme Peptides 2006, 27, 1693-1700 (Pubitemid 43866279)
    • (2006) Peptides , vol.27 , Issue.7 , pp. 1693-1700
    • Paradis-Bleau, C.1    Beaumont, M.2    Boudreault, L.3    Lloyd, A.4    Sanschagrin, F.5    Bugg, T.D.H.6    Levesque, R.C.7
  • 23
    • 65449184560 scopus 로고    scopus 로고
    • New high-throughput fluorimetric assay for discovering inhibitors of UDP- N -acetylmuramyl- l -alanine: D -glutamate (MurD) ligase
    • Kristan, K.; Kotnik, M.; Oblak, M.; Urleb, U. New high-throughput fluorimetric assay for discovering inhibitors of UDP- N -acetylmuramyl- l -alanine: d -glutamate (MurD) ligase J. Biomol. Screening 2009, 14, 412-418
    • (2009) J. Biomol. Screening , vol.14 , pp. 412-418
    • Kristan, K.1    Kotnik, M.2    Oblak, M.3    Urleb, U.4
  • 24
    • 34548258863 scopus 로고    scopus 로고
    • Development of novel inhibitors targeting intracellular steps of peptidoglycan biosynthesis
    • DOI 10.2174/138161207781368828
    • Kotnik, M.; Štefanič Anderluh, P.; Preželj, A. Development of novel inhibitors targeting intracellular steps of peptidoglycan biosynthesis Curr. Pharm. Des. 2007, 13, 2283-2309 (Pubitemid 47317036)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.22 , pp. 2283-2309
    • Kotnik, M.1    Anderluh, P.S.2    Prezelj, A.3
  • 29
    • 79960171696 scopus 로고    scopus 로고
    • GOLD, version 4.1, is available from The Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge, CB2 1EZ, U.K.
    • GOLD, version 4.1, is available from The Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge, CB2 1EZ, U.K.; www.ccdc.cam.ac.uk.
  • 30
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B.; Holloway, G. A. New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 2010, 53, 2719-2740
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 31
    • 77958044565 scopus 로고    scopus 로고
    • Observations on screening-based research and some concerning trends in the literature
    • Baell, J. B. Observations on screening-based research and some concerning trends in the literature Future Med. Chem. 2010, 2, 1529-1546
    • (2010) Future Med. Chem. , vol.2 , pp. 1529-1546
    • Baell, J.B.1
  • 32
    • 78650674952 scopus 로고    scopus 로고
    • False positives in the early stages of drug discovery
    • Šink, R.; Gobec, S.; Pečar, S.; Zega, A. False positives in the early stages of drug discovery Curr. Med. Chem. 2010, 17, 4231-4255
    • (2010) Curr. Med. Chem. , vol.17 , pp. 4231-4255
    • Šink, R.1    Gobec, S.2    Pečar, S.3    Zega, A.4
  • 33
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 1997, 267, 727-748 (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 36
    • 0024596463 scopus 로고
    • Structural eludicidation of epalrestat (ONO-2235), a potent aldose reductase inhibitor, and isomerization of its double bonds
    • DOI 10.1016/S0040-4039(00)95290-0
    • Ishida, T.; In, Y.; Inoue, M.; Ueno, Y.; Tanaka, C.; Hamanaka, N. Structural elucidation of epalrestat(ono-2235), a potent aldose reductase inhibitor, and isomerization of its double-bonds Tetrahedron Lett. 1989, 30, 959-962 (Pubitemid 19068970)
    • (1989) Tetrahedron Letters , vol.30 , Issue.8 , pp. 959-962
    • Ishida, T.1    In, Y.2    Inoue, M.3    Ueno, Y.4    Tanaka, C.5    Hamanaka, N.6
  • 37
    • 70349419722 scopus 로고    scopus 로고
    • A convenient synthesis of 4-benzyl-2-(2-(4-oxo-2-thioxothiazolidin-5- ylidene)ethyl)-2 H -1,4-benzoxazin-3(4 H)-ones and 5-(2-(4-benzyl-3-oxo-3,4- dihydro-2 H -1,4-benzoxazin-2-yl)ethylidene)thiazolidine-2,4-diones
    • Zidar, N.; Kladnik, J.; Kikelj, D. A convenient synthesis of 4-benzyl-2-(2-(4-oxo-2-thioxothiazolidin-5-ylidene)ethyl)-2 H -1,4-benzoxazin-3(4 H)-ones and 5-(2-(4-benzyl-3-oxo-3,4-dihydro-2 H -1,4-benzoxazin-2-yl)ethylidene)thiazolidine-2,4-diones Acta Chim. Slov. 2009, 56, 635-642
    • (2009) Acta Chim. Slov. , vol.56 , pp. 635-642
    • Zidar, N.1    Kladnik, J.2    Kikelj, D.3
  • 38
    • 66449103022 scopus 로고    scopus 로고
    • Facile reductive amination of aldehydes with electron-deficient anilines by acyloxyborohydrides in TFA: Application to a diazaindoline scale-up
    • Boros, E. E.; Thompson, J. B.; Katamreddy, S. R.; Carpenter, A. J. Facile reductive amination of aldehydes with electron-deficient anilines by acyloxyborohydrides in TFA: application to a diazaindoline scale-up J. Org. Chem. 2009, 74, 3587-3590
    • (2009) J. Org. Chem. , vol.74 , pp. 3587-3590
    • Boros, E.E.1    Thompson, J.B.2    Katamreddy, S.R.3    Carpenter, A.J.4
  • 39
    • 67749103816 scopus 로고    scopus 로고
    • Self-assembly of dendritic crowns into chiral supramolecular spheres
    • Percec, V.; Imam, M. R.; Peterca, M.; Wilson, D. A.; Heiney, P. A. Self-assembly of dendritic crowns into chiral supramolecular spheres J. Am. Chem. Soc. 2009, 131, 1294-1304
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1294-1304
    • Percec, V.1    Imam, M.R.2    Peterca, M.3    Wilson, D.A.4    Heiney, P.A.5
  • 40
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • DOI 10.1016/0003-2697(79)90115-5
    • Lanzetta, P. A.; Alvarez, L. J.; Reinach, P. S.; Candia, O. A. Improved assay for nanomole amounts of inorganic-phosphate Anal. Biochem. 1979, 100, 95-97 (Pubitemid 10157636)
    • (1979) Analytical Biochemistry , vol.100 , Issue.1 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 43
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94
    • Halgren, T. A. Merck molecular force field. 1. Basis, form, scope, parameterization, and performance of MMFF94 J. Comput. Chem. 1996, 17, 490-519 (Pubitemid 126567067)
    • (1996) Journal of Computational Chemistry , vol.17 , Issue.5-6 , pp. 490-519
    • Halgren, T.A.1
  • 44
    • 79960171948 scopus 로고    scopus 로고
    • Pymol is available from Delano Scientific LLC, San Francisco, CA.
    • Pymol is available from Delano Scientific LLC, San Francisco, CA; http://pymol.sourceforge.net.


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