메뉴 건너뛰기




Volumn 50, Issue 1, 2006, Pages 230-236

Utility of muropeptide ligase for identification of inhibitors of the cell wall biosynthesis enzyme MurF

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINOPYRIDINE DERIVATIVE; BACTERIAL ENZYME; DIAMINOPIMELIC ACID; ENZYME INHIBITOR; GLUTAMIC ACID; LIGASE; MURF INHIBITOR; MUROPEPTIDE LIGASE; PROTEIN MURF; THIAZOLYLAMINOPYRIDINE; TRIPEPTIDE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE;

EID: 29944442521     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.50.1.230-236.2006     Document Type: Article
Times cited : (31)

References (25)
  • 1
    • 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., S. S. Eveland, H. R. Onishi, and D. L. Pompliano. 1996. Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: use of a glutathione S-transferase fusion. Biochemistry 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
  • 4
    • 0027512265 scopus 로고
    • Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase
    • Benson, T. E., J. L. Marquardt, A. C. Marquardt, F. A. Etzkorn, and C. T. Walsh. 1993. Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase. Biochemistry 32:2024-2030.
    • (1993) Biochemistry , vol.32 , pp. 2024-2030
    • Benson, T.E.1    Marquardt, J.L.2    Marquardt, A.C.3    Etzkorn, F.A.4    Walsh, C.T.5
  • 5
    • 0028084561 scopus 로고
    • Synthesis of α and β anomers of UDP-N-acetylmuramic acid
    • Blanot, D., G. Auger, D. Liger, and J. van Heijenoort. 1994. Synthesis of α and β anomers of UDP-N-acetylmuramic acid. Carbohydr. Res. 252:107-115.
    • (1994) Carbohydr. Res. , vol.252 , pp. 107-115
    • Blanot, D.1    Auger, G.2    Liger, D.3    Van Heijenoort, J.4
  • 7
    • 0025210655 scopus 로고
    • Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli
    • Duncan, K., J. Van Heijenoort, and C. T. Walsh. 1990. Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli. Biochemistry 29:2379-2386.
    • (1990) Biochemistry , vol.29 , pp. 2379-2386
    • Duncan, K.1    Van Heijenoort, J.2    Walsh, C.T.3
  • 8
    • 0035943137 scopus 로고    scopus 로고
    • In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa
    • El Zoeiby, A., F. Sanschagrin, P. C. Havugimana, A. Garnier, and R. C. Levesque. 2001. In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 201:229-235.
    • (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
  • 9
    • 0037223505 scopus 로고    scopus 로고
    • Structure and function of the Mur enzymes: Development of novel inhibitors
    • El Zoeiby, A., F. Sanschagrin, and R. C. Levesque. 2003. Structure and function of the Mur enzymes: development of novel inhibitors. Mol. Microbiol. 47:1-12.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1-12
    • El Zoeiby, A.1    Sanschagrin, F.2    Levesque, R.C.3
  • 11
    • 0026090486 scopus 로고
    • One-step purification procedure for UDP-N-acetylmuramyl-peptide murein precursors from Bacillus cereus
    • Kohlrausch, U., and J. V. Hoeltje. 1991. One-step purification procedure for UDP-N-acetylmuramyl-peptide murein precursors from Bacillus cereus. FEMS Microbiol. Lett. 78:253-257.
    • (1991) FEMS Microbiol. Lett. , vol.78 , pp. 253-257
    • Kohlrausch, U.1    Hoeltje, J.V.2
  • 12
    • 0015539001 scopus 로고
    • Temperature-sensitive mutant of Escherichia coli K-12 with an impaired D-alanine:D-alanine ligase
    • Lugtenberg, E. J., and A. van Schijndel-van Dam. 1972. Temperature-sensitive mutant of Escherichia coli K-12 with an impaired D-alanine:D-alanine ligase. J. Bacteriol. 113:96-104.
    • (1972) J. Bacteriol. , vol.113 , pp. 96-104
    • Lugtenberg, E.J.1    Van Schijndel-Van Dam, A.2
  • 13
    • 0029787789 scopus 로고    scopus 로고
    • Identification of the mpl gene encoding UDP-N-acetylmuramate:L-alanyl- γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan
    • Mengin-Lecreulx, D., J. van Heijenoort, and J. T. Park. 1996. Identification of the mpl gene encoding UDP-N-acetylmuramate:L-alanyl-γ-D- glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan. J. Bacteriol. 178:5347-5352.
    • (1996) J. Bacteriol. , vol.178 , pp. 5347-5352
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2    Park, J.T.3
  • 15
    • 14844347076 scopus 로고    scopus 로고
    • UDP-N-acetylmuramic acid (UDP-MurNAc) is a potent inhibitor of MurA (enolpyruvyl-UDP-GlcNAc synthase)
    • Mizyed, S., A. Oddone, B. Byczynski, D. W. Hughes, and P. J. Berti. 2005. UDP-N-acetylmuramic acid (UDP-MurNAc) is a potent inhibitor of MurA (enolpyruvyl-UDP-GlcNAc synthase). Biochemistry 44:4011-4017.
    • (2005) Biochemistry , vol.44 , pp. 4011-4017
    • Mizyed, S.1    Oddone, A.2    Byczynski, B.3    Hughes, D.W.4    Berti, P.J.5
  • 17
    • 0024357294 scopus 로고
    • Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide synthetase of Escherichia coli
    • Parquet, C., B. Flouret, D. Mengin-Lecreulx, and J. Van Heijenoort. 1989. Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide synthetase of Escherichia coli. Nucleic Acids Res. 17:5379.
    • (1989) Nucleic Acids Res , vol.17 , pp. 5379
    • Parquet, C.1    Flouret, B.2    Mengin-Lecreulx, D.3    Van Heijenoort, J.4
  • 18
    • 0036791627 scopus 로고    scopus 로고
    • New (and not so new) antibacterial targets-from where and when will the novel drugs come?
    • Projan, S. J. 2002. New (and not so new) antibacterial targets-from where and when will the novel drugs come? Curr. Opin. Pharmacol. 2:513-522.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 513-522
    • Projan, S.J.1
  • 19
    • 0033576995 scopus 로고    scopus 로고
    • Preparative enzymatic synthesis and characterization of the cytoplasmic intermediates of murein biosynthesis
    • Reddy, S. G., S. T. Waddell, D. W. Kuo, K. K. Wong, and D. L. Pompliano. 1999. Preparative enzymatic synthesis and characterization of the cytoplasmic intermediates of murein biosynthesis. J. Am. Chem. Soc. 121:1175-1178.
    • (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
  • 20
    • 0041353701 scopus 로고    scopus 로고
    • Normally functioning murF is essential for the optimal expression of methicillin resistance in Staphylococcus aureus
    • Sobral, R. G., A. M. Ludovice, S. Gardete, K. Tabei, H. De Lencastre, and A Tomasz. 2003. Normally functioning murF is essential for the optimal expression of methicillin resistance in Staphylococcus aureus. Microb. Drug Resist. 9:231-241.
    • (2003) Microb. Drug Resist. , vol.9 , pp. 231-241
    • Sobral, R.G.1    Ludovice, A.M.2    Gardete, S.3    Tabei, K.4    De Lencastre, H.5    Tomasz, A.6
  • 21
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 22
    • 0033517146 scopus 로고    scopus 로고
    • A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli
    • Templin, M. F., A. Ursinus, and J.-V. Holtje. 1999. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. EMBO J. 18:4108-4117.
    • (1999) EMBO J , vol.18 , pp. 4108-4117
    • Templin, M.F.1    Ursinus, A.2    Holtje, J.-V.3
  • 23
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of the bacterial peptidoglycan monomer unit
    • van Heijenoort, J. 2001. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18:503-519.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 503-519
    • Van Heijenoort, J.1
  • 25
    • 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., S. Munshi, B. Leiting, M. S. Anderson, J. Chrzas, and Z. Chen. 2000. Crystal structure of Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF) at 2.3. A resolution. J. Mol. Biol. 304:435-445.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.