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Volumn 48, Issue 3, 2004, Pages 897-902

Fluorescence Detection-Based Functional Assay for High-Throughput Screening for MraY

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; ENZYME INHIBITOR; MUREIDOMYCIN B; PEPTIDOGLYCAN; PROTEIN MRAY; RU 64957; RU 66950; RU 70157; RU 72143; RU 72839; RU 74709; RU 74854; RU 75413; RU 76491; RU 76492; RU 77254; RU 78695; RU 80303; RU 88108; RU 88110; RU 88114; RU 88155; TUNICAMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLMURAMIC ACID;

EID: 1442349130     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.48.3.897-902.2004     Document Type: Article
Times cited : (67)

References (30)
  • 1
    • 0001195822 scopus 로고    scopus 로고
    • Synthesis of an analogue of the lipoglycopeptide membrane intermediate I of peptidoglycan biosynthesis
    • Auger, G., M. Crouvoisier, M. Caroff, J. van Heijenoort, and D. Blanot. 1997. Synthesis of an analogue of the lipoglycopeptide membrane intermediate I of peptidoglycan biosynthesis. Lett. Peptide Sci. 4:371-376.
    • (1997) Lett. Peptide Sci. , vol.4 , pp. 371-376
    • Auger, G.1    Crouvoisier, M.2    Caroff, M.3    Van Heijenoort, J.4    Blanot, D.5
  • 4
    • 0032746748 scopus 로고    scopus 로고
    • Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis
    • Bouhss, A., D. Mengin-Lecreulx, D. Le Beller, and J. van Heijenoort. 1999. Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis. Mol. Microbiol. 34:576-585.
    • (1999) Mol. Microbiol. , vol.34 , pp. 576-585
    • Bouhss, A.1    Mengin-Lecreulx, D.2    Le Beller, D.3    Van Heijenoort, J.4
  • 5
    • 0031725647 scopus 로고    scopus 로고
    • mraY is an essential gene for cell growth in Escherichia coli
    • Boyle, D. S., and W. D. Donachie. 1998. mraY is an essential gene for cell growth in Escherichia coli. J. Bacteriol. 180:6429-6432.
    • (1998) J. Bacteriol. , vol.180 , pp. 6429-6432
    • Boyle, D.S.1    Donachie, W.D.2
  • 6
    • 0030004930 scopus 로고    scopus 로고
    • Slow binding inhibition of phospho-N-acetylmuramyl-pentapeptide-translocase (Escherichia coli) by mureidomycin A
    • Brandish, P. E., M. K. Burnham, J. T. Lonsdale, R. Southgate, M. Inukai, and T. D. H. Bugg. 1996. Slow binding inhibition of phospho-N-acetylmuramyl-pentapeptide-translocase (Escherichia coli) by mureidomycin A. J. Biol. Chem. 271:7609-7614.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7609-7614
    • Brandish, P.E.1    Burnham, M.K.2    Lonsdale, J.T.3    Southgate, R.4    Inukai, M.5    Bugg, T.D.H.6
  • 7
    • 0029902635 scopus 로고    scopus 로고
    • Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli
    • Brandish, P. E., K. I. Kimura, M. Inukai, R. Southgate, J. T. Lonsdale, and T. D. H. Bugg. 1996. Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob. Agents Chemother. 40:1640-1644.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1640-1644
    • Brandish, P.E.1    Kimura, K.I.2    Inukai, M.3    Southgate, R.4    Lonsdale, J.T.5    Bugg, T.D.H.6
  • 8
    • 0034192601 scopus 로고    scopus 로고
    • Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase
    • Brandstrom, A. A., S. Midha, C. B. Longley, K. Han, E. R. Baizman, and H. R. Axelrod. 2000. Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase. Anal. Biochem. 280:315-319.
    • (2000) Anal. Biochem. , vol.280 , pp. 315-319
    • Brandstrom, A.A.1    Midha, S.2    Longley, C.B.3    Han, K.4    Baizman, E.R.5    Axelrod, H.R.6
  • 9
    • 0028365984 scopus 로고
    • From peptidoglycan to glycoproteins: Common features of lipid-linked oligosaccharide biosynthesis
    • Bugg, T. D. H., and P. E. Brandish. 1994. From peptidoglycan to glycoproteins: common features of lipid-linked oligosaccharide biosynthesis. FEMS Microbiol. Lett. 119:255-262.
    • (1994) FEMS Microbiol. Lett. , vol.119 , pp. 255-262
    • Bugg, T.D.H.1    Brandish, P.E.2
  • 10
    • 0021763813 scopus 로고
    • Purification of β-lactamases by affinity chromatography on phenylboronic acid-agarose
    • Cartwright, S. J., and S. G. Waley. 1984. Purification of β-lactamases by affinity chromatography on phenylboronic acid-agarose. Biochem. J. 221: 505-512.
    • (1984) Biochem. J. , vol.221 , pp. 505-512
    • Cartwright, S.J.1    Waley, S.G.2
  • 12
    • 0018365125 scopus 로고
    • Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells
    • Dagert, M., and S. D. Ehrlich. 1979. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene 6:23-28.
    • (1979) Gene , vol.6 , pp. 23-28
    • Dagert, M.1    Ehrlich, S.D.2
  • 13
    • 0034698781 scopus 로고    scopus 로고
    • Synthesis of the nucleoside moiety of liposidomycins: Elucidation of the pharmacophore of this family of MraY inhibitors
    • Dini, C., P. Collette, N. Drochon, J. C. Guillot, G. Lemoine, P. Mauvais, and J. Aszodi. 2000. Synthesis of the nucleoside moiety of liposidomycins: elucidation of the pharmacophore of this family of MraY inhibitors. Bioorg. Med. Chem. Lett. 10:1839-1843.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1839-1843
    • Dini, C.1    Collette, P.2    Drochon, N.3    Guillot, J.C.4    Lemoine, G.5    Mauvais, P.6    Aszodi, J.7
  • 14
    • 0037156358 scopus 로고    scopus 로고
    • Synthesis of sub-micromolar inhibitors of MraY by exploring the region originally occupied by the diazepanone ring in the liposidomycin structure
    • Dini, C., S. Didier-Laurent, N. Drochon, S. Feteanu, J. C. Guillot, F. Monti, E. Uridat, J. Zhang, and J. Aszodi, 2002. Synthesis of sub-micromolar inhibitors of MraY by exploring the region originally occupied by the diazepanone ring in the liposidomycin structure. Bioorg. Med. Chem. Lett. 12:1209-1213.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1209-1213
    • Dini, C.1    Didier-Laurent, S.2    Drochon, N.3    Feteanu, S.4    Guillot, J.C.5    Monti, F.6    Uridat, E.7    Zhang, J.8    Aszodi, J.9
  • 15
    • 0035952253 scopus 로고    scopus 로고
    • Synthesis of analogues of the O-β-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 1. Contribution of the amino group and the uracil moiety upon the inhibition of MraY
    • Dini, C., N. Drochon, S. Feteanu, J. C. Guillot, C. Peixoto, and J. Aszodi. 2001. Synthesis of analogues of the O-β-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 1. Contribution of the amino group and the uracil moiety upon the inhibition of MraY. Bioorg. Med. Chem. Lett. 11:529-531.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 529-531
    • Dini, C.1    Drochon, N.2    Feteanu, S.3    Guillot, J.C.4    Peixoto, C.5    Aszodi, J.6
  • 16
    • 0035952292 scopus 로고    scopus 로고
    • Synthesis of analogues of the O-β-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 2: Role of the hydroxyl groups upon the inhibition of MraY
    • Dini, C., N. Drochon, J. C. Guillot, P. Mauvais, P. Walter, and J. Aszodi. 2001. Synthesis of analogues of the O-β-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 2: role of the hydroxyl groups upon the inhibition of MraY. Bioorg. Med. Chem. Lett. 11:533-536.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 533-536
    • Dini, C.1    Drochon, N.2    Guillot, J.C.3    Mauvais, P.4    Walter, P.5    Aszodi, J.6
  • 17
    • 0038296043 scopus 로고    scopus 로고
    • A high-throughput solid-phase extraction assay capable of measuring diverse polyprenyl phosphate: Sugar-1-phosphate transferases as exemplified by the WecA, MraY, and MurG proteins
    • Hyland, S. A., and M. S. Anderson. 2003. A high-throughput solid-phase extraction assay capable of measuring diverse polyprenyl phosphate: sugar-1-phosphate transferases as exemplified by the WecA, MraY, and MurG proteins. Anal. Biochem. 317:156-164.
    • (2003) Anal. Biochem. , vol.317 , pp. 156-164
    • Hyland, S.A.1    Anderson, M.S.2
  • 18
    • 0027233035 scopus 로고
    • Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins
    • Inukai, M., F. Ishino, and A. Takaitsuld. 1993. Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins. Antimicrob. Agents Chemother. 37:980-983.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 980-983
    • Inukai, M.1    Ishino, F.2    Takaitsuld, A.3
  • 19
    • 0027504659 scopus 로고
    • Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling the pathogenicity of Pseudomonas syringae
    • Loubens, L., L. Debardieux, A. Bohin, J.-M. Lacroix, and J.-P. Bohin. 1993. Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling the pathogenicity of Pseudomonas syringae. Mol. Microbiol. 10:329-340.
    • (1993) Mol. Microbiol. , vol.10 , pp. 329-340
    • Loubens, L.1    Debardieux, L.2    Bohin, A.3    Lacroix, J.-M.4    Bohin, J.-P.5
  • 20
    • 0015133172 scopus 로고
    • In vivo and in vitro action of new antibiotics interfering with the utilization of N-acetyl-glucosamine-N-acetyl-muramyl-pentapeptide
    • Lugtenberg, E. J. J., A. van SchUndel-van Dam, and T. H. M. van Bellegem. 1971. In vivo and in vitro action of new antibiotics interfering with the utilization of N-acetyl-glucosamine-N-acetyl-muramyl-pentapeptide. J. Bacteriol. 108:20-29.
    • (1971) J. Bacteriol. , vol.108 , pp. 20-29
    • Lugtenberg, E.J.J.1    Van SchUndel-van Dam, A.2    Van Bellegem, T.H.M.3
  • 21
    • 0019771584 scopus 로고
    • Murein biosynthesis in ether permeabilized Escherichia coli starting from early peptidoglycan precursors
    • Maass, D., and H. Pelzer. 1981. Murein biosynthesis in ether permeabilized Escherichia coli starting from early peptidoglycan precursors. Arch. Microbiol. 130:301-306.
    • (1981) Arch. Microbiol. , vol.130 , pp. 301-306
    • Maass, D.1    Pelzer, H.2
  • 23
    • 0000358235 scopus 로고
    • Initial translocation reaction in the biosynthesis of peptidoglycan by bacterial membranes
    • Neuhaus, F. C. 1971. Initial translocation reaction in the biosynthesis of peptidoglycan by bacterial membranes. Acc. Chem. Res. 4:297-303.
    • (1971) Acc. Chem. Res. , vol.4 , pp. 297-303
    • Neuhaus, F.C.1
  • 24
    • 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
  • 27
    • 0025093558 scopus 로고
    • Inhibition of peptidoglycan biosynthesis by ramoplanin
    • Somner, E. A., and P. E. Reynolds. 1990. Inhibition of peptidoglycan biosynthesis by ramoplanin. Antimicrob. Agents Chemother. 34:423-429.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 423-429
    • Somner, E.A.1    Reynolds, P.E.2
  • 28
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of bacterial peptidoglycan monomer unit
    • van Heijenoort, J. 2001. Recent advances in the formation of bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18:503-519.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 503-519
    • Van Heijenoort, J.1
  • 29
    • 0017355389 scopus 로고
    • ε -5-dimethylaminonaphthalene-1-sulfonyl)pentapeptide
    • ε-5-dimethylaminonaphthalene-1-sulfonyl)pentapeptide. J. Biol. Chem. 252:2296-2303.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2296-2303
    • Weppner, W.A.1    Neuhaus, F.C.2


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