메뉴 건너뛰기




Volumn 27, Issue 7, 2006, Pages 1693-1700

Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme

Author keywords

Inhibitory peptides; MurD; Phage display; Pseudomonas aeruginosa; UDP N acetylmuramyl l alanine:d glutamate ligase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; BACTERIAL DNA; GLUTAMIC ACID; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LIGASE; LIGASE INHIBITOR; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLMURAMYLALANYL DEXTRO GLUTAMATE LIGASE;

EID: 33744983912     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.01.017     Document Type: Article
Times cited : (25)

References (35)
  • 2
    • 0034283162 scopus 로고    scopus 로고
    • "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase
    • Bertrand J.A., Fanchon E., Martin L., Chantalat L., Auger G., Blanot D., et al. "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. J Mol Biol 301 (2000) 1257-1266
    • (2000) J Mol Biol , vol.301 , pp. 1257-1266
    • Bertrand, J.A.1    Fanchon, E.2    Martin, L.3    Chantalat, L.4    Auger, G.5    Blanot, D.6
  • 3
    • 0033592452 scopus 로고    scopus 로고
    • Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-l-alanine:d-glutamate ligase (MurD)
    • Bouhss A., Dementin S., Parquet C., Mengin-Lecreulx D., Bertrand J.A., Le Beller D., et al. Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-l-alanine:d-glutamate ligase (MurD). Biochemistry 38 (1999) 12240-12247
    • (1999) Biochemistry , vol.38 , pp. 12240-12247
    • Bouhss, A.1    Dementin, S.2    Parquet, C.3    Mengin-Lecreulx, D.4    Bertrand, J.A.5    Le Beller, D.6
  • 4
    • 0242412153 scopus 로고    scopus 로고
    • Separation methods applicable to the evaluation of enzyme-inhibitor and enzyme-substrate interactions
    • Burns K.L., and May S.W. Separation methods applicable to the evaluation of enzyme-inhibitor and enzyme-substrate interactions. J Chromatogr B Analyt Technol Biomed Life Sci 797 (2003) 175-190
    • (2003) J Chromatogr B Analyt Technol Biomed Life Sci , vol.797 , pp. 175-190
    • Burns, K.L.1    May, S.W.2
  • 5
    • 0037296380 scopus 로고    scopus 로고
    • Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA
    • Carettoni D., Gomez-Puertas P., Yim L., Mingorance J., Massidda O., Vicente M., et al. Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA. Proteins 50 (2003) 192-206
    • (2003) Proteins , vol.50 , pp. 192-206
    • Carettoni, D.1    Gomez-Puertas, P.2    Yim, L.3    Mingorance, J.4    Massidda, O.5    Vicente, M.6
  • 7
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet J.F., and Bardwell J.C. Oxidative protein folding in bacteria. Mol Microbiol 44 (2002) 1-8
    • (2002) Mol Microbiol , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 8
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim Biophys Acta 1462 (1999) 71-87
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 9
    • 0344256526 scopus 로고    scopus 로고
    • Starvation and temperature upshift cause an increase in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protein in yeast
    • Delgado M.L., Gil M.L., and Gozalbo D. Starvation and temperature upshift cause an increase in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protein in yeast. FEMS Yeast Res 4 (2003) 297-303
    • (2003) FEMS Yeast Res , vol.4 , pp. 297-303
    • Delgado, M.L.1    Gil, M.L.2    Gozalbo, D.3
  • 10
    • 0037339206 scopus 로고    scopus 로고
    • Identification of novel inhibitors of Pseudomonas aeruginosa MurC enzyme derived from phage-displayed peptide libraries
    • El Zoeiby A., Sanschagrin F., Darveau A., Brisson J.R., and Levesque R.C. Identification of novel inhibitors of Pseudomonas aeruginosa MurC enzyme derived from phage-displayed peptide libraries. J Antimicrob Chemother 51 (2003) 531-543
    • (2003) J Antimicrob Chemother , vol.51 , pp. 531-543
    • El Zoeiby, A.1    Sanschagrin, F.2    Darveau, A.3    Brisson, J.R.4    Levesque, R.C.5
  • 11
    • 0035943137 scopus 로고    scopus 로고
    • In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa
    • El Zoeiby A., Sanschagrin F., Havugimana P.C., Garnier A., and Levesque R.C. In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa. FEMS Microbiol Lett 201 (2001) 229-235
    • (2001) FEMS Microbiol Lett , vol.201 , pp. 229-235
    • El Zoeiby, A.1    Sanschagrin, F.2    Havugimana, P.C.3    Garnier, A.4    Levesque, R.C.5
  • 12
    • 0037223505 scopus 로고    scopus 로고
    • Structure and function of the Mur enzymes: development of novel inhibitors
    • El Zoeiby A., Sanschagrin F., and Levesque R.C. Structure and function of the Mur enzymes: development of novel inhibitors. Mol Microbiol 47 (2003) 1-12
    • (2003) Mol Microbiol , vol.47 , pp. 1-12
    • El Zoeiby, A.1    Sanschagrin, F.2    Levesque, R.C.3
  • 13
    • 0035210628 scopus 로고    scopus 로고
    • Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation
    • Fischer P.M., Krausz E., and Lane D.P. Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation. Bioconjug Chem 12 (2001) 825-841
    • (2001) Bioconjug Chem , vol.12 , pp. 825-841
    • Fischer, P.M.1    Krausz, E.2    Lane, D.P.3
  • 15
    • 0035471140 scopus 로고    scopus 로고
    • Protein design and phage display
    • Hoess R.H. Protein design and phage display. Chem Rev 101 (2001) 3205-3218
    • (2001) Chem Rev , vol.101 , pp. 3205-3218
    • Hoess, R.H.1
  • 16
    • 0036897745 scopus 로고    scopus 로고
    • Understanding bacterial biofilms in patients with cystic fibrosis: current and innovative approaches to potential therapies
    • Hoiby N. Understanding bacterial biofilms in patients with cystic fibrosis: current and innovative approaches to potential therapies. J Cyst Fibros 1 (2002) 249-254
    • (2002) J Cyst Fibros , vol.1 , pp. 249-254
    • Hoiby, N.1
  • 18
    • 0034092470 scopus 로고    scopus 로고
    • Detection of small-molecule enzyme inhibitors with peptides isolated from phage-displayed combinatorial peptide libraries
    • Hyde-DeRuyscher R., Paige L.A., Christensen D.J., Hyde-DeRuyscher N., Lim A., Fredericks Z.L., et al. Detection of small-molecule enzyme inhibitors with peptides isolated from phage-displayed combinatorial peptide libraries. Chem Biol 7 (2000) 17-25
    • (2000) Chem Biol , vol.7 , pp. 17-25
    • Hyde-DeRuyscher, R.1    Paige, L.A.2    Christensen, D.J.3    Hyde-DeRuyscher, N.4    Lim, A.5    Fredericks, Z.L.6
  • 19
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: causes, challenges and responses
    • Levy S.B., and Marshall B. Antibacterial resistance worldwide: causes, challenges and responses. Nat Med 10 (2004) S122-S129
    • (2004) Nat Med , vol.10
    • Levy, S.B.1    Marshall, B.2
  • 20
    • 0035038011 scopus 로고    scopus 로고
    • Drug targeting Mycobacterium tuberculosis cell wall synthesis: genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose
    • Ma Y., Stern R.J., Scherman M.S., Vissa V.D., Yan W., Jones V.C., et al. Drug targeting Mycobacterium tuberculosis cell wall synthesis: genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose. Antimicrob Agents Chemother 45 (2001) 1407-1416
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1407-1416
    • Ma, Y.1    Stern, R.J.2    Scherman, M.S.3    Vissa, V.D.4    Yan, W.5    Jones, V.C.6
  • 22
    • 0034193246 scopus 로고    scopus 로고
    • The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions
    • Modun B., Morrissey J., and Williams P. The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions. Trends Microbiol 8 (2000) 231-237
    • (2000) Trends Microbiol , vol.8 , pp. 231-237
    • Modun, B.1    Morrissey, J.2    Williams, P.3
  • 23
    • 0032497397 scopus 로고    scopus 로고
    • Combinatorial chemistry: from peptides and peptidomimetics to small organic and heterocyclic compounds
    • Nefzi A., Dooley C., Ostresh J.M., and Houghten R.A. Combinatorial chemistry: from peptides and peptidomimetics to small organic and heterocyclic compounds. Bioorg Med Chem Lett 8 (1998) 2273-2278
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 2273-2278
    • Nefzi, A.1    Dooley, C.2    Ostresh, J.M.3    Houghten, R.A.4
  • 24
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Pancholi V., and Chhatwal G.S. Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol 293 (2003) 391-401
    • (2003) Int J Med Microbiol , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 25
    • 3543143166 scopus 로고    scopus 로고
    • Identification of Pseudomonas aeruginosa FtsZ peptide inhibitors as a tool for development of novel antimicrobials
    • Paradis-Bleau C., Sanschagrin F., and Levesque R.C. Identification of Pseudomonas aeruginosa FtsZ peptide inhibitors as a tool for development of novel antimicrobials. J Antimicrob Chemother 54 (2004) 278-280
    • (2004) J Antimicrob Chemother , vol.54 , pp. 278-280
    • Paradis-Bleau, C.1    Sanschagrin, F.2    Levesque, R.C.3
  • 27
    • 22144494583 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa, Candida albicans, and device-related nosocomial infections: implications, trends, and potential approaches for control
    • Pierce G.E. Pseudomonas aeruginosa, Candida albicans, and device-related nosocomial infections: implications, trends, and potential approaches for control. J Ind Microbiol Biotechnol 32 (2005) 309-318
    • (2005) J Ind Microbiol Biotechnol , vol.32 , pp. 309-318
    • Pierce, G.E.1
  • 28
    • 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
  • 29
    • 0033576995 scopus 로고    scopus 로고
    • Preparative enzymatic synthesis and characterization of the cytoplasmic intermediates of murein biosynthesis
    • Reddy S.G., Waddell S.T., Kuo D.W., Wong K.K., and Pompliano D.L. Preparative enzymatic synthesis and characterization of the cytoplasmic intermediates of murein biosynthesis. J Am Chem Soc 121 (1999) 1175-1178
    • (1999) J Am Chem Soc , vol.121 , pp. 1175-1178
    • Reddy, S.G.1    Waddell, S.T.2    Kuo, D.W.3    Wong, K.K.4    Pompliano, D.L.5
  • 30
    • 0034018940 scopus 로고    scopus 로고
    • Structure-function analysis of alpha-helix H4 using PSE-4 as a model enzyme representative of class A beta-lactamases
    • Savoie A., Sanschagrin F., Palzkill T., Voyer N., and Levesque R.C. Structure-function analysis of alpha-helix H4 using PSE-4 as a model enzyme representative of class A beta-lactamases. Protein Eng 13 (2000) 267-274
    • (2000) Protein Eng , vol.13 , pp. 267-274
    • Savoie, A.1    Sanschagrin, F.2    Palzkill, T.3    Voyer, N.4    Levesque, R.C.5
  • 31
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Shai Y., and Oren Z. From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22 (2001) 1629-1641
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 32
    • 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
  • 33
    • 27944446768 scopus 로고    scopus 로고
    • Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD
    • Strancar K., Blanot D., and Gobec S. Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD. Bioorg Med Chem Lett 16 (2006) 343-348
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 343-348
    • Strancar, K.1    Blanot, D.2    Gobec, S.3
  • 34
    • 0032850461 scopus 로고    scopus 로고
    • Comparison of the d-glutamate-adding enzymes from selected Gram-positive and Gram-negative bacteria
    • Walsh A.W., Falk P.J., Thanassi J., Discotto L., Pucci M.J., and Ho H.T. Comparison of the d-glutamate-adding enzymes from selected Gram-positive and Gram-negative bacteria. J Bacteriol 181 (1999) 5395-5401
    • (1999) J Bacteriol , vol.181 , pp. 5395-5401
    • Walsh, A.W.1    Falk, P.J.2    Thanassi, J.3    Discotto, L.4    Pucci, M.J.5    Ho, H.T.6
  • 35
    • 0041664049 scopus 로고    scopus 로고
    • Bacterial shape
    • Young K.D. Bacterial shape. Mol Microbiol 49 (2003) 571-580
    • (2003) Mol Microbiol , vol.49 , pp. 571-580
    • Young, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.