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Volumn 78, Issue 2, 2009, Pages 231-237

An easy and fast method for the evaluation of Staphylococcus epidermidis type I signal peptidase inhibitors

Author keywords

FRET; Inhibitor; Protein secretion; Staphylococcus epidermidis; Type I signal peptidase

Indexed keywords

AMINO ACID; ENZYME INHIBITOR; PROTEIN PRECURSOR; SIGNAL PEPTIDASE I; SYNTHETIC PEPTIDE;

EID: 67650131333     PISSN: 01677012     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mimet.2009.06.006     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0029923991 scopus 로고    scopus 로고
    • Inhibitors of bacterial signal peptidase: a series of 6-(substituted oxyethyl)penems
    • Allsop A., Brooks G., Edwards P.D., Kaura A.C., and Southgate R. Inhibitors of bacterial signal peptidase: a series of 6-(substituted oxyethyl)penems. J. Antibiot. (Tokyo) 49 (1996) 921-928
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 921-928
    • Allsop, A.1    Brooks, G.2    Edwards, P.D.3    Kaura, A.C.4    Southgate, R.5
  • 2
    • 9944226776 scopus 로고    scopus 로고
    • A solid phase linker strategy for the direct synthesis of EDANS-labelled peptide substrates
    • Beythien J., and White P.D. A solid phase linker strategy for the direct synthesis of EDANS-labelled peptide substrates. Tetrahedron Lett. 46 (2005) 101-104
    • (2005) Tetrahedron Lett. , vol.46 , pp. 101-104
    • Beythien, J.1    White, P.D.2
  • 3
    • 0027291327 scopus 로고
    • Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad
    • Black M.T. Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad. J. Bacteriol. 175 (1993) 4957-4961
    • (1993) J. Bacteriol. , vol.175 , pp. 4957-4961
    • Black, M.T.1
  • 4
    • 0031950203 scopus 로고    scopus 로고
    • Inhibitors of bacterial signal peptidases
    • Black M.T., and Bruton G. Inhibitors of bacterial signal peptidases. Curr. Pharm. Des. 4 (1998) 133-154
    • (1998) Curr. Pharm. Des. , vol.4 , pp. 133-154
    • Black, M.T.1    Bruton, G.2
  • 5
    • 67650115297 scopus 로고    scopus 로고
    • of the type I signal peptidases as antibacterial target for biofilm-associated infections of Staphylococcus epidermidis. Microbiol, submitted for publication
    • Bockstael, K., Geukens, N., Van Mellaert, L., Herdewijn, P., Anné, J., Van Aerschot, A., submitted for publication. Evaluation of the type I signal peptidases as antibacterial target for biofilm-associated infections of Staphylococcus epidermidis. Microbiol.
    • Evaluation
    • Bockstael, K.1    Geukens, N.2    Van Mellaert, L.3    Herdewijn, P.4    Anné, J.5    Van Aerschot, A.6
  • 7
    • 65349139603 scopus 로고    scopus 로고
    • Substrate based peptide aldehyde inhibits bacterial type I signal peptidase
    • Buzder-Lantos P., Bockstael K., Anne J., and Herdewijn P. Substrate based peptide aldehyde inhibits bacterial type I signal peptidase. Bioorg. Med. Chem. Lett. 19 (2009) 2880-2883
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2880-2883
    • Buzder-Lantos, P.1    Bockstael, K.2    Anne, J.3    Herdewijn, P.4
  • 9
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: a common cause of persistent infections
    • Costerton J.W., Stewart P.S., and Greenberg E.P. Bacterial biofilms: a common cause of persistent infections. Science 284 (1999) 1318-1322
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 10
    • 0022400507 scopus 로고
    • Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane
    • Dalbey R.E., and Wickner W. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. J. Biol. Chem. 260 (1985) 15925-15931
    • (1985) J. Biol. Chem. , vol.260 , pp. 15925-15931
    • Dalbey, R.E.1    Wickner, W.2
  • 11
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., and van Dijl J.M. The chemistry and enzymology of the type I signal peptidases. Protein Sci. 6 (1997) 1129-1138
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    van Dijl, J.M.4
  • 12
    • 0020584151 scopus 로고
    • Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli
    • Date T. Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli. J. Bacteriol. 154 (1983) 76-83
    • (1983) J. Bacteriol. , vol.154 , pp. 76-83
    • Date, T.1
  • 13
    • 33746738866 scopus 로고    scopus 로고
    • Antimicrobial resistance and production of biofilms in clinical isolates of coagulase-negative Staphylococcus strains
    • de Allori M.C., Jure M.A., Romero C., and de Castillo M.E. Antimicrobial resistance and production of biofilms in clinical isolates of coagulase-negative Staphylococcus strains. Biol. Pharm. Bull. 29 (2006) 1592-1596
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 1592-1596
    • de Allori, M.C.1    Jure, M.A.2    Romero, C.3    de Castillo, M.E.4
  • 14
    • 0025202766 scopus 로고
    • Minimum substrate sequence for signal peptidase I of Escherichia coli
    • Dev I.K., Ray P.H., and Novak P. Minimum substrate sequence for signal peptidase I of Escherichia coli. J. Biol. Chem. 265 (1990) 20069-20072
    • (1990) J. Biol. Chem. , vol.265 , pp. 20069-20072
    • Dev, I.K.1    Ray, P.H.2    Novak, P.3
  • 15
    • 0027967844 scopus 로고
    • How proteins cross the bacterial cytoplasmic membrane
    • Driessen A.J. How proteins cross the bacterial cytoplasmic membrane. J. Membr. Biol. 142 (1994) 145-159
    • (1994) J. Membr. Biol. , vol.142 , pp. 145-159
    • Driessen, A.J.1
  • 19
    • 0020980478 scopus 로고
    • Quantitative assay for signal peptidase
    • Jackson R.C. Quantitative assay for signal peptidase. Methods Enzymol. 96 (1983) 784-794
    • (1983) Methods Enzymol. , vol.96 , pp. 784-794
    • Jackson, R.C.1
  • 20
    • 0022343605 scopus 로고
    • Conserved residues of the leader peptide are essential for cleavage by leader peptidase
    • Kuhn A., and Wickner W. Conserved residues of the leader peptide are essential for cleavage by leader peptidase. J. Biol. Chem. 260 (1985) 15914-15918
    • (1985) J. Biol. Chem. , vol.260 , pp. 15914-15918
    • Kuhn, A.1    Wickner, W.2
  • 22
    • 0026483377 scopus 로고
    • A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis
    • Maggiora L.L., Smith C.W., and Zhang Z.Y. A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis. J. Med. Chem. 35 (1992) 3727-3730
    • (1992) J. Med. Chem. , vol.35 , pp. 3727-3730
    • Maggiora, L.L.1    Smith, C.W.2    Zhang, Z.Y.3
  • 24
    • 0023664531 scopus 로고
    • A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli
    • Moore K.E., and Miura S. A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 262 (1987) 8806-8813
    • (1987) J. Biol. Chem. , vol.262 , pp. 8806-8813
    • Moore, K.E.1    Miura, S.2
  • 25
    • 3142715940 scopus 로고    scopus 로고
    • Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor
    • Paetzel M., Goodall J.J., Kania M., Dalbey R.E., and Page M.G. Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor. J. Biol. Chem. 279 (2004) 30781-30790
    • (2004) J. Biol. Chem. , vol.279 , pp. 30781-30790
    • Paetzel, M.1    Goodall, J.J.2    Kania, M.3    Dalbey, R.E.4    Page, M.G.5
  • 26
    • 0035368651 scopus 로고    scopus 로고
    • Development of an internally quenched fluorescent substrate and a continuous fluorimetric assay for Streptococcus pneumoniae signal peptidase I
    • Peng S.B., Zheng F., Angleton E.L., Smiley D., Carpenter J., and Scott J.E. Development of an internally quenched fluorescent substrate and a continuous fluorimetric assay for Streptococcus pneumoniae signal peptidase I. Anal. Biochem. 293 (2001) 88-95
    • (2001) Anal. Biochem. , vol.293 , pp. 88-95
    • Peng, S.B.1    Zheng, F.2    Angleton, E.L.3    Smiley, D.4    Carpenter, J.5    Scott, J.E.6
  • 27
    • 0028694356 scopus 로고
    • Site-specific chemical modification procedures
    • Pennington M.W., and Dunn B.M. (Eds), Humana Press Inc., Totowa, New Jersey
    • Pennington M.W. Site-specific chemical modification procedures. In: Pennington M.W., and Dunn B.M. (Eds). Peptide Synthesis Protocols. 1st edn (1994), Humana Press Inc., Totowa, New Jersey 171-185
    • (1994) Peptide Synthesis Protocols. 1st edn , pp. 171-185
    • Pennington, M.W.1
  • 28
    • 66249126841 scopus 로고    scopus 로고
    • Enzymatic investigation of the Staphylococcus aureus type I signal peptidase SpsB - implications for the search for novel antibiotics
    • Rao C.V. S., Bockstael K., Nath S., Engelborghs Y., Anne J., and Geukens N. Enzymatic investigation of the Staphylococcus aureus type I signal peptidase SpsB - implications for the search for novel antibiotics. FEBS J. 276 (2009) 3222-3234
    • (2009) FEBS J. , vol.276 , pp. 3222-3234
    • Rao C.V., S.1    Bockstael, K.2    Nath, S.3    Engelborghs, Y.4    Anne, J.5    Geukens, N.6
  • 31
    • 0024465189 scopus 로고
    • Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase
    • San Millan J.L., Boyd D., Dalbey R., Wickner W., and Beckwith J. Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J. Bacteriol. 171 (1989) 5536-5541
    • (1989) J. Bacteriol. , vol.171 , pp. 5536-5541
    • San Millan, J.L.1    Boyd, D.2    Dalbey, R.3    Wickner, W.4    Beckwith, J.5
  • 32
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., and Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189 (1986) 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 34
    • 0020453360 scopus 로고
    • Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase
    • Tokunaga M., Loranger J.M., Wolfe P.B., and Wu H.C. Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase. J. Biol. Chem. 257 (1982) 9922-9925
    • (1982) J. Biol. Chem. , vol.257 , pp. 9922-9925
    • Tokunaga, M.1    Loranger, J.M.2    Wolfe, P.B.3    Wu, H.C.4
  • 35
    • 0027733662 scopus 로고
    • A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase
    • Tschantz W.R., Sung M., Delgado-Partin V.M., and Dalbey R.E. A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase. J. Biol. Chem. 268 (1993) 27349-27354
    • (1993) J. Biol. Chem. , vol.268 , pp. 27349-27354
    • Tschantz, W.R.1    Sung, M.2    Delgado-Partin, V.M.3    Dalbey, R.E.4
  • 37
    • 0023393136 scopus 로고
    • Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacteriophage M13 procoat
    • Wickner W., Moore K., Dibb N., Geissert D., and Rice M. Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacteriophage M13 procoat. J. Bacteriol. 169 (1987) 3821-3822
    • (1987) J. Bacteriol. , vol.169 , pp. 3821-3822
    • Wickner, W.1    Moore, K.2    Dibb, N.3    Geissert, D.4    Rice, M.5
  • 38
    • 0021100176 scopus 로고
    • Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope
    • Wolfe P.B., Wickner W., and Goodman J.M. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258 (1983) 12073-12080
    • (1983) J. Biol. Chem. , vol.258 , pp. 12073-12080
    • Wolfe, P.B.1    Wickner, W.2    Goodman, J.M.3
  • 39
    • 0020995217 scopus 로고
    • Purification and characterization of leader peptidase from Escherichia coli
    • Wolfe P.B., Zwizinski C., and Wickner W. Purification and characterization of leader peptidase from Escherichia coli. Methods Enzymol. 97 (1983) 40-46
    • (1983) Methods Enzymol. , vol.97 , pp. 40-46
    • Wolfe, P.B.1    Zwizinski, C.2    Wickner, W.3
  • 40
    • 0018388950 scopus 로고
    • Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes
    • Yaron A., Carmel A., and Katchalski-Katzir E. Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes. Anal. Biochem. 95 (1979) 228-235
    • (1979) Anal. Biochem. , vol.95 , pp. 228-235
    • Yaron, A.1    Carmel, A.2    Katchalski-Katzir, E.3
  • 42
    • 0031964283 scopus 로고    scopus 로고
    • Development of an internally quenched fluorescent substrate for Escherichia coli leader peptidase
    • Zhong W., and Benkovic S.J. Development of an internally quenched fluorescent substrate for Escherichia coli leader peptidase. Anal. Biochem. 255 (1998) 66-73
    • (1998) Anal. Biochem. , vol.255 , pp. 66-73
    • Zhong, W.1    Benkovic, S.J.2
  • 43
    • 0019129862 scopus 로고
    • Purification and characterization of leader (signal) peptidase from Escherichia coli
    • Zwizinski C., and Wickner W. Purification and characterization of leader (signal) peptidase from Escherichia coli. J. Biol. Chem. 255 (1980) 7973-7977
    • (1980) J. Biol. Chem. , vol.255 , pp. 7973-7977
    • Zwizinski, C.1    Wickner, W.2


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