메뉴 건너뛰기




Volumn 90, Issue 1, 2010, Pages 16-24

ATP-dependent MurE ligase in Mycobacterium tuberculosis: Biochemical and structural characterisation

Author keywords

ATP dependent ligase; Cell wall peptidoglycan biosynthesis; Enzyme kinetics; Protein structure; Tuberculosis

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; DIAMINOPIMELIC ACID; PEPTIDOGLYCAN; UDP MURNAC TRIPEPTIDE LIGASE; UNCLASSIFIED DRUG;

EID: 75149131973     PISSN: 14729792     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tube.2009.10.007     Document Type: Article
Times cited : (45)

References (59)
  • 1
    • 33847725133 scopus 로고    scopus 로고
    • Trials and tribulations
    • Mandavilli A. Trials and tribulations. Nat Med 13 (2007) 272-273
    • (2007) Nat Med , vol.13 , pp. 272-273
    • Mandavilli, A.1
  • 2
    • 33847714722 scopus 로고    scopus 로고
    • Virtually incurable TB warns of impending disaster
    • Mandavilli A. Virtually incurable TB warns of impending disaster. Nat Med 13 (2007) 271
    • (2007) Nat Med , vol.13 , pp. 271
    • Mandavilli, A.1
  • 3
    • 40949100778 scopus 로고    scopus 로고
    • Tuberculosis drug resistance comes full circle
    • Reichman L.B. Tuberculosis drug resistance comes full circle. Lancet 371 (2008) 1052-1053
    • (2008) Lancet , vol.371 , pp. 1052-1053
    • Reichman, L.B.1
  • 4
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • Brennan P.J. Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinb) 83 (2003) 91-97
    • (2003) Tuberculosis (Edinb) , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 5
    • 0141677776 scopus 로고    scopus 로고
    • Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy
    • Gao L.Y., Laval F., Lawson E.H., Groger R.K., Woodruff A., Morisaki J.H., et al. Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol Microbiol 49 (2003) 1547-1563
    • (2003) Mol Microbiol , vol.49 , pp. 1547-1563
    • Gao, L.Y.1    Laval, F.2    Lawson, E.H.3    Groger, R.K.4    Woodruff, A.5    Morisaki, J.H.6
  • 6
    • 34247572374 scopus 로고    scopus 로고
    • Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice
    • Bhatt A., Fujiwara N., Bhatt K., Gurcha S.S., Kremer L., Chen B., et al. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc Natl Acad Sci U S A 104 (2007) 5157-5162
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5157-5162
    • Bhatt, A.1    Fujiwara, N.2    Bhatt, K.3    Gurcha, S.S.4    Kremer, L.5    Chen, B.6
  • 9
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of the bacterial peptidoglycan monomer unit
    • van Heijenoort J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat Prod Rep 18 (2001) 503-519
    • (2001) Nat Prod Rep , vol.18 , pp. 503-519
    • van Heijenoort, J.1
  • 10
    • 0032741590 scopus 로고    scopus 로고
    • Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis
    • De Smet K.A., Kempsell K.E., Gallagher A., Duncan K., and Young D.B. Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis. Microbiology (Reading, England) 145 Pt 11 (1999) 3177-3184
    • (1999) Microbiology (Reading, England) , vol.145 , Issue.PART 11 , pp. 3177-3184
    • De Smet, K.A.1    Kempsell, K.E.2    Gallagher, A.3    Duncan, K.4    Young, D.B.5
  • 11
    • 0034351486 scopus 로고    scopus 로고
    • Comparison of the UDP-N-acetylmuramate:l-alanine ligase enzymes from Mycobacterium tuberculosis and
    • Mahapatra S., Crick D.C., and Brennan P.J. Comparison of the UDP-N-acetylmuramate:l-alanine ligase enzymes from Mycobacterium tuberculosis and. Mycobacterium leprae. J Bacteriol 182 (2000) 6827-6830
    • (2000) Mycobacterium leprae. J Bacteriol , vol.182 , pp. 6827-6830
    • Mahapatra, S.1    Crick, D.C.2    Brennan, P.J.3
  • 12
    • 15244352162 scopus 로고    scopus 로고
    • Glycolylation of the nucleotide precursors of peptidoglycan biosynthesis of Mycobacterium spp. is altered by drug treatment
    • Mahapatra S., Scherman H., Brennan P.J., and Crick D.C.N. Glycolylation of the nucleotide precursors of peptidoglycan biosynthesis of Mycobacterium spp. is altered by drug treatment. J Bacteriol 187 (2005) 2341-2347
    • (2005) J Bacteriol , vol.187 , pp. 2341-2347
    • Mahapatra, S.1    Scherman, H.2    Brennan, P.J.3    Crick, D.C.N.4
  • 13
    • 0016209670 scopus 로고
    • Occurrence of d-alanyl-(d)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria
    • Wietzerbin J., Das B.C., Petit J.F., Lederer E., Leyh-Bouille M., and Ghuysen J.M. Occurrence of d-alanyl-(d)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria. Biochemistry 13 (1974) 3471-3476
    • (1974) Biochemistry , vol.13 , pp. 3471-3476
    • Wietzerbin, J.1    Das, B.C.2    Petit, J.F.3    Lederer, E.4    Leyh-Bouille, M.5    Ghuysen, J.M.6
  • 14
    • 0014902764 scopus 로고
    • Studies on peptides, glycopeptides and antigenic polysaccharide-glycopeptide complexes isolated from an L-11 enzyme lysate of the cell walls of Mycobacterium tuberculosis strain H37Rv
    • Kotani S., Yanagida I., Kato K., and Matsuda T. Studies on peptides, glycopeptides and antigenic polysaccharide-glycopeptide complexes isolated from an L-11 enzyme lysate of the cell walls of Mycobacterium tuberculosis strain H37Rv. Biken journal 13 (1970) 249-275
    • (1970) Biken journal , vol.13 , pp. 249-275
    • Kotani, S.1    Yanagida, I.2    Kato, K.3    Matsuda, T.4
  • 15
    • 16844383874 scopus 로고    scopus 로고
    • Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate
    • Mahapatra S., Yagi T., Belisle J.T., Espinosa B.J., Hill P.J., McNeil M.R., et al. Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate. J Bacteriol 187 (2005) 2747-2757
    • (2005) J Bacteriol , vol.187 , pp. 2747-2757
    • Mahapatra, S.1    Yagi, T.2    Belisle, J.T.3    Espinosa, B.J.4    Hill, P.J.5    McNeil, M.R.6
  • 16
    • 0029739897 scopus 로고    scopus 로고
    • Study of the reaction mechanism of the d-glutamic acid-adding enzyme from Escherichia coli
    • Vaganay S., Tanner M.E., van Heijenoort J., and Blanot D. Study of the reaction mechanism of the d-glutamic acid-adding enzyme from Escherichia coli. Microb Drug Resist 2 (1996) 51-54
    • (1996) Microb Drug Resist , vol.2 , pp. 51-54
    • Vaganay, S.1    Tanner, M.E.2    van Heijenoort, J.3    Blanot, D.4
  • 17
    • 33748324503 scopus 로고    scopus 로고
    • Structure, function and dynamics in the Mur family of bacterial cell wall ligases
    • Smith C.A. Structure, function and dynamics in the Mur family of bacterial cell wall ligases. J Mol Biol 362 (2006) 640-655
    • (2006) J Mol Biol , vol.362 , pp. 640-655
    • Smith, C.A.1
  • 18
    • 0035815667 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylmuramoyl-l-alanyl-d-glutamate: meso-diaminopimelate ligase from Escherichia coli
    • Gordon E., Flouret B., Chantalat L., van Heijenoort J., Mengin-Lecreulx D., and Dideberg O. Crystal structure of UDP-N-acetylmuramoyl-l-alanyl-d-glutamate: meso-diaminopimelate ligase from Escherichia coli. J Biol Chem 276 (2001) 10999-11006
    • (2001) J Biol Chem , vol.276 , pp. 10999-11006
    • Gordon, E.1    Flouret, B.2    Chantalat, L.3    van Heijenoort, J.4    Mengin-Lecreulx, D.5    Dideberg, O.6
  • 19
    • 0032823023 scopus 로고    scopus 로고
    • Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:l-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth
    • Mengin-Lecreulx D., Falla T., Blanot D., van Heijenoort J., Adams D.J., and Chopra I. Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:l-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth. J Bacteriol 181 (1999) 5909-5914
    • (1999) J Bacteriol , vol.181 , pp. 5909-5914
    • Mengin-Lecreulx, D.1    Falla, T.2    Blanot, D.3    van Heijenoort, J.4    Adams, D.J.5    Chopra, I.6
  • 20
    • 0033927088 scopus 로고    scopus 로고
    • A method for demonstrating gene essentiality in Staphylococcus aureus
    • Jana M., Luong T.T., Komatsuzawa H., Shigeta M., and Lee C.Y. A method for demonstrating gene essentiality in Staphylococcus aureus. Plasmid 44 (2000) 100-104
    • (2000) Plasmid , vol.44 , pp. 100-104
    • Jana, M.1    Luong, T.T.2    Komatsuzawa, H.3    Shigeta, M.4    Lee, C.Y.5
  • 21
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti C.M., Boyd D.H., and Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48 (2003) 77-84
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 22
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 23
    • 0014830906 scopus 로고
    • Cell wall polymers of Bacillus sphaericus 9602. II. Synthesis of the first enzyme unique to cortex synthesis during sporulation
    • Tipper D.J., and Pratt I. Cell wall polymers of Bacillus sphaericus 9602. II. Synthesis of the first enzyme unique to cortex synthesis during sporulation. J Bacteriol 103 (1970) 305-317
    • (1970) J Bacteriol , vol.103 , pp. 305-317
    • Tipper, D.J.1    Pratt, I.2
  • 24
    • 41949083782 scopus 로고    scopus 로고
    • Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species
    • Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., et al. Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species. J Bacteriol 190 (2008) 2892-2902
    • (2008) J Bacteriol , vol.190 , pp. 2892-2902
    • Hu, X.1    Fan, W.2    Han, B.3    Liu, H.4    Zheng, D.5    Li, Q.6
  • 25
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Jnt CCP4+ ESF-EAMCB Newslett Protein Crystallogr 26 (1992)
    • (1992) Jnt CCP4+ ESF-EAMCB Newslett Protein Crystallogr , vol.26
    • Leslie, A.G.W.1
  • 26
  • 27
    • 33947523060 scopus 로고    scopus 로고
    • Automated search-model discovery and preparation for structure solution by molecular replacement
    • Keegan R.M., and Winn M.D. Automated search-model discovery and preparation for structure solution by molecular replacement. Acta Crystallogr D Biol Crystallogr 63 (2007) 447-457
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 447-457
    • Keegan, R.M.1    Winn, M.D.2
  • 28
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30 (1997) 1022-1025
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 (2004) 2126-2132
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn M.D., Murshudov G.N., and Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 374 (2003) 300-321
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 32
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 372 (2007) 774-797
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 33
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60 (2004) 2256-2268
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 0034423412 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution
    • Yan Y., Munshi S., Leiting B., Anderson M.S., Chrzas J., and Chen Z. Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution. J Mol Biol 304 (2000) 435-445
    • (2000) J Mol Biol , vol.304 , pp. 435-445
    • Yan, Y.1    Munshi, S.2    Leiting, B.3    Anderson, M.S.4    Chrzas, J.5    Chen, Z.6
  • 35
    • 0033546272 scopus 로고    scopus 로고
    • Determination of the MurD mechanism through crystallographic analysis of enzyme complexes
    • Bertrand J.A., Auger G., Martin L., Fanchon E., Blanot D., Le Beller D., et al. Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. J Mol Biol 289 (1999) 579-590
    • (1999) J Mol Biol , vol.289 , pp. 579-590
    • Bertrand, J.A.1    Auger, G.2    Martin, L.3    Fanchon, E.4    Blanot, D.5    Le Beller, D.6
  • 36
    • 12844275936 scopus 로고    scopus 로고
    • Identification of the namH gene, encoding the hydroxylase responsible for the N-glycolylation of the mycobacterial peptidoglycan
    • Raymond J.B., Mahapatra S., Crick D.C., and Pavelka Jr. M.S. Identification of the namH gene, encoding the hydroxylase responsible for the N-glycolylation of the mycobacterial peptidoglycan. J Biol Chem 280 (2005) 326-333
    • (2005) J Biol Chem , vol.280 , pp. 326-333
    • Raymond, J.B.1    Mahapatra, S.2    Crick, D.C.3    Pavelka Jr., M.S.4
  • 37
    • 0035715193 scopus 로고    scopus 로고
    • The cell wall and cell division gene cluster in the Mra operon of Pseudomonas aeruginosa: cloning, production, and purification of active enzymes
    • Azzolina B.A., Yuan X., Anderson M.S., and El-Sherbeini M. The cell wall and cell division gene cluster in the Mra operon of Pseudomonas aeruginosa: cloning, production, and purification of active enzymes. Protein Exp Purif 21 (2001) 393-400
    • (2001) Protein Exp Purif , vol.21 , pp. 393-400
    • Azzolina, B.A.1    Yuan, X.2    Anderson, M.S.3    El-Sherbeini, M.4
  • 38
    • 0025688726 scopus 로고
    • Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-l-alanyl-d-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli
    • Michaud C., Mengin-Lecreulx D., van Heijenoort J., and Blanot D. Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-l-alanyl-d-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli. Eur J Biochem 194 (1990) 853-861
    • (1990) Eur J Biochem , vol.194 , pp. 853-861
    • Michaud, C.1    Mengin-Lecreulx, D.2    van Heijenoort, J.3    Blanot, D.4
  • 39
    • 3242889291 scopus 로고    scopus 로고
    • Cloning, expression and characterization of the Streptococcus pyogenes murE gene encoding a UDP-MurNAc-l-alanyl-d-glutamate: l-lysine ligase
    • Thomas A.T., Renee M.C., and David L.P. Cloning, expression and characterization of the Streptococcus pyogenes murE gene encoding a UDP-MurNAc-l-alanyl-d-glutamate: l-lysine ligase. Enzyme and Microbial Technology 35 (2004) 300-308
    • (2004) Enzyme and Microbial Technology , vol.35 , pp. 300-308
    • Thomas, A.T.1    Renee, M.C.2    David, L.P.3
  • 40
    • 0019578458 scopus 로고
    • Reverse-phase high-pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan
    • Flouret B., Mengin-Lecreulx D., and van Heijenoort J. Reverse-phase high-pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan. Anal Biochem 114 (1981) 59-63
    • (1981) Anal Biochem , vol.114 , pp. 59-63
    • Flouret, B.1    Mengin-Lecreulx, D.2    van Heijenoort, J.3
  • 41
    • 77956844354 scopus 로고
    • Labischinski H., and Maidhof H. (Eds), Elsevier Science, Amsterdam
    • In: Labischinski H., and Maidhof H. (Eds). Bacterial cell wall vol. 27 (1994), Elsevier Science, Amsterdam 23-38
    • (1994) Bacterial cell wall , vol.27 , pp. 23-38
  • 42
    • 0015919757 scopus 로고
    • Enzymatic synthesis of the peptide in bacterial uridine nucleotides. VII. Comparative biochemistry
    • Ito E., and Strominger J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. VII. Comparative biochemistry. J Biol Chem 248 (1973) 3131-3136
    • (1973) J Biol Chem , vol.248 , pp. 3131-3136
    • Ito, E.1    Strominger, J.L.2
  • 43
    • 0036471217 scopus 로고    scopus 로고
    • Overexpression, purification and biochemical characterization of a class A high-molecular-mass penicillin-binding protein (PBP), PBP1* and its soluble derivative from Mycobacterium tuberculosis
    • Bhakta S., and Basu J. Overexpression, purification and biochemical characterization of a class A high-molecular-mass penicillin-binding protein (PBP), PBP1* and its soluble derivative from Mycobacterium tuberculosis. Biochem J 361 (2002) 635-639
    • (2002) Biochem J , vol.361 , pp. 635-639
    • Bhakta, S.1    Basu, J.2
  • 44
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by l, d-transpeptidation
    • Lavollay M., Arthur M., Fourgeaud M., Dubost L., Marie A., Veziris N., et al. The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by l, d-transpeptidation. J Bacteriol 190 (2008) 4360-4366
    • (2008) J Bacteriol , vol.190 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5    Veziris, N.6
  • 45
    • 0028361885 scopus 로고
    • Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli
    • Mengin-Lecreulx D., Blanot D., and van Heijenoort J. Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli. J Bacteriol 176 (1994) 4321-4327
    • (1994) J Bacteriol , vol.176 , pp. 4321-4327
    • Mengin-Lecreulx, D.1    Blanot, D.2    van Heijenoort, J.3
  • 46
    • 33744937347 scopus 로고    scopus 로고
    • The MurE synthetase from Thermotoga maritima is endowed with an unusual d-lysine adding activity
    • Boniface A., Bouhss A., Mengin-Lecreulx D., and Blanot D. The MurE synthetase from Thermotoga maritima is endowed with an unusual d-lysine adding activity. J Biol Chem 281 (2006) 15680-15686
    • (2006) J Biol Chem , vol.281 , pp. 15680-15686
    • Boniface, A.1    Bouhss, A.2    Mengin-Lecreulx, D.3    Blanot, D.4
  • 47
    • 0000283410 scopus 로고
    • Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of d-glutamic acid-adding enzyme
    • Nathenson S.G., Strominger J.L., and Ito E. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of d-glutamic acid-adding enzyme. J Biol Chem 239 (1964) 1773-1776
    • (1964) J Biol Chem , vol.239 , pp. 1773-1776
    • Nathenson, S.G.1    Strominger, J.L.2    Ito, E.3
  • 48
    • 0001625196 scopus 로고
    • Enzymatic synthesis of the peptide in bacterial uridine nucleotides. III. Purification and properties of l-lysin-adding enzyme
    • Ito E., and Strominger J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. III. Purification and properties of l-lysin-adding enzyme. J Biol Chem 239 (1964) 210-214
    • (1964) J Biol Chem , vol.239 , pp. 210-214
    • Ito, E.1    Strominger, J.L.2
  • 49
    • 27644588079 scopus 로고    scopus 로고
    • Potential drug targets in Mycobacterium tuberculosis through metabolic pathway analysis
    • Anishetty S., Pulimi M., and Pennathur G. Potential drug targets in Mycobacterium tuberculosis through metabolic pathway analysis. Comput Biol Chem 29 (2005) 368-378
    • (2005) Comput Biol Chem , vol.29 , pp. 368-378
    • Anishetty, S.1    Pulimi, M.2    Pennathur, G.3
  • 50
    • 0242323605 scopus 로고    scopus 로고
    • Novel inhibitors of bacterial cell wall synthesis
    • Silver L.L. Novel inhibitors of bacterial cell wall synthesis. Curr Opin Microbiol 6 (2003) 431-438
    • (2003) Curr Opin Microbiol , vol.6 , pp. 431-438
    • Silver, L.L.1
  • 51
    • 47649112998 scopus 로고    scopus 로고
    • Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis
    • Bratkovic T., Lunder M., Urleb U., and Strukelj B. Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis. J Basic Microbiol 48 (2008) 202-206
    • (2008) J Basic Microbiol , vol.48 , pp. 202-206
    • Bratkovic, T.1    Lunder, M.2    Urleb, U.3    Strukelj, B.4
  • 53
    • 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., Kovac A., Wolber G., Blanot D., Gobec S., and Solmajer 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 19 (2009) 2668-2673
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 2668-2673
    • Perdih, A.1    Kovac, A.2    Wolber, G.3    Blanot, D.4    Gobec, S.5    Solmajer, T.6
  • 54
    • 34249719140 scopus 로고    scopus 로고
    • Phosphinate inhibitors of UDP-N-acetylmuramoyl-l-alanyl-d-glutamate: l-lysine ligase (MurE)
    • Strancar K., Boniface A., Blanot D., and Gobec S. Phosphinate inhibitors of UDP-N-acetylmuramoyl-l-alanyl-d-glutamate: l-lysine ligase (MurE). Arch Pharm (Weinheim) 340 (2007) 127-134
    • (2007) Arch Pharm (Weinheim) , vol.340 , pp. 127-134
    • Strancar, K.1    Boniface, A.2    Blanot, D.3    Gobec, S.4
  • 55
    • 0029867778 scopus 로고    scopus 로고
    • Phosphinate inhibitors of the d-glutamic acid-adding enzyme of peptidoglycan biosynthesis
    • Tanner M.E., Vaganay S., van Heijenoort J., and Blanot D. Phosphinate inhibitors of the d-glutamic acid-adding enzyme of peptidoglycan biosynthesis. J Org Chem 61 (1996) 1756-1760
    • (1996) J Org Chem , vol.61 , pp. 1756-1760
    • Tanner, M.E.1    Vaganay, S.2    van Heijenoort, J.3    Blanot, D.4
  • 56
    • 57749085472 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of new glutamic acid-based inhibitors of MurD ligase
    • Tomasic T., Zidar N., Rupnik V., Kovac A., Blanot D., Gobec S., et al. Synthesis and biological evaluation of new glutamic acid-based inhibitors of MurD ligase. Bioorg Med Chem Lett 19 (2009) 153-157
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 153-157
    • Tomasic, T.1    Zidar, N.2    Rupnik, V.3    Kovac, A.4    Blanot, D.5    Gobec, S.6
  • 57
    • 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., Kovac A., Boniface A., Bostock J.M., Chopra I., Blanot D., et al. Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening. Bioorg Med Chem 17 (2009) 1884-1889
    • (2009) Bioorg Med Chem , vol.17 , pp. 1884-1889
    • Turk, S.1    Kovac, A.2    Boniface, A.3    Bostock, J.M.4    Chopra, I.5    Blanot, D.6
  • 58
    • 0016194384 scopus 로고
    • The mechanism of action of fosfomycin (phosphonomycin)
    • Kahan F.M., Kahan J.S., Cassidy P.J., and Kropp H. The mechanism of action of fosfomycin (phosphonomycin). Ann N Y Acad Sci 235 (1974) 364-386
    • (1974) Ann N Y Acad Sci , vol.235 , pp. 364-386
    • Kahan, F.M.1    Kahan, J.S.2    Cassidy, P.J.3    Kropp, H.4
  • 59
    • 0036791627 scopus 로고    scopus 로고
    • New (and not so new) antibacterial targets - from where and when will the novel drugs come?
    • Projan S.J. New (and not so new) antibacterial targets - from where and when will the novel drugs come?. Curr Opin Pharmacol 2 (2002) 513-522
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 513-522
    • Projan, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.