메뉴 건너뛰기




Volumn 189, Issue 2, 2007, Pages 522-530

Substrate specificity of the Escherichia coli outer membrane protease OmpP

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ARGININE; BACTERIAL ENZYME; BACTERIAL PROTEIN; GLUTAMIC ACID; LEUCINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN OMPP; PROTEIN OMPT; PROTEINASE; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 33846217757     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01493-06     Document Type: Article
Times cited : (33)

References (39)
  • 1
    • 33745512801 scopus 로고    scopus 로고
    • Growth of Escherichia coli MG1655 on LB medium: Monitoring utilization of amino acids, peptides, and nucleotides with transcriptional microarrays
    • Baev, M. V., D. Baev, A. J. Radek, and J. W. Campbell. 2006. Growth of Escherichia coli MG1655 on LB medium: monitoring utilization of amino acids, peptides, and nucleotides with transcriptional microarrays. Appl. Microbiol. Biotechnol. 71:323-328.
    • (2006) Appl. Microbiol. Biotechnol , vol.71 , pp. 323-328
    • Baev, M.V.1    Baev, D.2    Radek, A.J.3    Campbell, J.W.4
  • 2
    • 0025057970 scopus 로고
    • In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT
    • Baneyx, F., and G. Georgiou. 1990. In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. J. Bacteriol. 172:491-494.
    • (1990) J. Bacteriol , vol.172 , pp. 491-494
    • Baneyx, F.1    Georgiou, G.2
  • 3
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casabadan, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol , vol.138 , pp. 179-207
    • Casabadan, M.J.1    Cohen, S.N.2
  • 4
    • 0035852860 scopus 로고    scopus 로고
    • Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries
    • Dekker, N., C. C. Ruud, R. A. Kramer, and M. R. Egmond. 2001. Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. Biochemistry 40:1694-1701.
    • (2001) Biochemistry , vol.40 , pp. 1694-1701
    • Dekker, N.1    Ruud, C.C.2    Kramer, R.A.3    Egmond, M.R.4
  • 5
    • 1842864784 scopus 로고    scopus 로고
    • Phage display substrate: A blind method for determining protease specificity
    • Deperthes, D. 2002. Phage display substrate: a blind method for determining protease specificity. Biol. Chem. 383:1107-1112.
    • (2002) Biol. Chem , vol.383 , pp. 1107-1112
    • Deperthes, D.1
  • 6
    • 0025486840 scopus 로고
    • Overproduction and purification of the omega subunit of Escherichia coli RNA polymerase
    • Gentry, D. R., and R. R. Burgess. 1990. Overproduction and purification of the omega subunit of Escherichia coli RNA polymerase. Protein Expr. Purif. 1:81-86.
    • (1990) Protein Expr. Purif , vol.1 , pp. 81-86
    • Gentry, D.R.1    Burgess, R.R.2
  • 8
    • 0023840230 scopus 로고
    • OmpT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg, J., and J. J. Dunn. 1988. OmpT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification J. Bacteriol. 170:1245-1253.
    • (1988) J. Bacteriol , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 9
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 10
    • 0028040011 scopus 로고
    • New outer membrane-associated protease of Escherichia coli K-12
    • Kaufmann, A., Y. D. Stierhof, and U. Henning. 1994. New outer membrane-associated protease of Escherichia coli K-12. J. Bacteriol. 176:359-367.
    • (1994) J. Bacteriol , vol.176 , pp. 359-367
    • Kaufmann, A.1    Stierhof, Y.D.2    Henning, U.3
  • 13
    • 3142737933 scopus 로고    scopus 로고
    • The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia coli to systemic spread of Yersinia pestis
    • Kukkonen, M., and T. K. Korhonen. 2004. The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis. Int. J. Med. Microbiol. 294:7-14.
    • (2004) Int. J. Med. Microbiol , vol.294 , pp. 7-14
    • Kukkonen, M.1    Korhonen, T.K.2
  • 14
    • 1142306001 scopus 로고    scopus 로고
    • Keratinocyte growth factor-2 production in an ompT-deficient Escherichia coli K-12 mutant
    • Laird, M. W., K. Cope, R. Atkinson, M. Donahoe, K. Johnson, and M. Melick. 2004. Keratinocyte growth factor-2 production in an ompT-deficient Escherichia coli K-12 mutant. Biotechnol. Prog. 20:44-50.
    • (2004) Biotechnol. Prog , vol.20 , pp. 44-50
    • Laird, M.W.1    Cope, K.2    Atkinson, R.3    Donahoe, M.4    Johnson, K.5    Melick, M.6
  • 15
    • 0026774464 scopus 로고
    • OmpT proteolysis of E. coli initiation factor IF2. Elimination of a cleavage site by site-directed mutagenesis
    • Lassen, S. F., K. K. Mortensen, and H. U. Sperling-Petersen. 1992. OmpT proteolysis of E. coli initiation factor IF2. Elimination of a cleavage site by site-directed mutagenesis. Biochem. Int. 27:601-611.
    • (1992) Biochem. Int , vol.27 , pp. 601-611
    • Lassen, S.F.1    Mortensen, K.K.2    Sperling-Petersen, H.U.3
  • 16
    • 0344629200 scopus 로고    scopus 로고
    • Processing of XynE (110-kDa) of Aeromonas caviae ME-1 to 72-kDa xylanase in Escherichia coli transformant
    • Liu, C. J., T. Suzuki, S. Hirata, and K. Kawai. 2003. Processing of XynE (110-kDa) of Aeromonas caviae ME-1 to 72-kDa xylanase in Escherichia coli transformant. J. Biosci. Bioeng. 96:406-408.
    • (2003) J. Biosci. Bioeng , vol.96 , pp. 406-408
    • Liu, C.J.1    Suzuki, T.2    Hirata, S.3    Kawai, K.4
  • 17
    • 0028672746 scopus 로고
    • Omptin: An Escherichia coli outer membrane proteinase that activates plasminogen
    • Mangel, W. F., D. L. Toledo, M. T. Brown, K. Worzalla, M. Kee, and J. J. Dunn. 1994. Omptin: an Escherichia coli outer membrane proteinase that activates plasminogen. Methods Enzymol. 244:384-399.
    • (1994) Methods Enzymol , vol.244 , pp. 384-399
    • Mangel, W.F.1    Toledo, D.L.2    Brown, M.T.3    Worzalla, K.4    Kee, M.5    Dunn, J.J.6
  • 18
    • 0032705124 scopus 로고    scopus 로고
    • The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production
    • Matsuo, E., G. Sampei, K. Mizobuchi, and K. Ito. 1999. The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production. FEBS Lett. 461:6-8.
    • (1999) FEBS Lett , vol.461 , pp. 6-8
    • Matsuo, E.1    Sampei, G.2    Mizobuchi, K.3    Ito, K.4
  • 19
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews, D. J., and J. A. Wells. 1993. Substrate phage: selection of protease substrates by monovalent phage display. Science 260:1113-1117.
    • (1993) Science , vol.260 , pp. 1113-1117
    • Matthews, D.J.1    Wells, J.A.2
  • 21
    • 0023617973 scopus 로고
    • Phosphate regulation of gene expression in Vibrio parahaemolyticus
    • McCarter, L. L., and M. Silverman. 1987. Phosphate regulation of gene expression in Vibrio parahaemolyticus. J. Bacteriol. 169:3441-3449.
    • (1987) J. Bacteriol , vol.169 , pp. 3441-3449
    • McCarter, L.L.1    Silverman, M.2
  • 22
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. coli strains defective in all known loci effecting the proteolytic stability of secreted recombinant proteins
    • Meerman, H. J., and G. Georgiou. 1994. Construction and characterization of a set of E. coli strains defective in all known loci effecting the proteolytic stability of secreted recombinant proteins. Bio/Technology 12:1107-1110.
    • (1994) Bio/Technology , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgiou, G.2
  • 23
  • 24
    • 0036794384 scopus 로고    scopus 로고
    • An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: Efficient cleavage of substrates with basic amino acids at the P4 and P6 positions
    • Okuno, K., M. Yabuta, K. Ohsuye, T. Ooi, and S. Kinoshita. 2002. An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: efficient cleavage of substrates with basic amino acids at the P4 and P6 positions. Biotechnol. Appl. Biochem. 36:77-84.
    • (2002) Biotechnol. Appl. Biochem , vol.36 , pp. 77-84
    • Okuno, K.1    Yabuta, M.2    Ohsuye, K.3    Ooi, T.4    Kinoshita, S.5
  • 26
    • 0036430140 scopus 로고    scopus 로고
    • The determination and use of optimized protease substrates in drug discovery and development
    • Richardson, P. L. 2002. The determination and use of optimized protease substrates in drug discovery and development. Curr. Pharm. Des. 8:2559-2581.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 2559-2581
    • Richardson, P.L.1
  • 28
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J. K., and G. P. Smith. 1990. Searching for peptide ligands with an epitope library. Science 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 29
    • 15244354461 scopus 로고    scopus 로고
    • Screening for protease substrate by polyvalent phage display
    • Sedlacek, R., and E. Chen. 2005. Screening for protease substrate by polyvalent phage display. Comb. Chem. High-Throughput Screen. 8:197-203.
    • (2005) Comb. Chem. High-Throughput Screen , vol.8 , pp. 197-203
    • Sedlacek, R.1    Chen, E.2
  • 30
    • 0033564401 scopus 로고    scopus 로고
    • Eukaryotic precursor proteins are processed by Escherichia coli outer membrane protein OmpP
    • Striebel, H.-M., and F. Kalousek. 1999. Eukaryotic precursor proteins are processed by Escherichia coli outer membrane protein OmpP. Eur. J. Biochem. 262:832-839.
    • (1999) Eur. J. Biochem , vol.262 , pp. 832-839
    • Striebel, H.-M.1    Kalousek, F.2
  • 32
    • 0030933618 scopus 로고    scopus 로고
    • Requirement of a large K+-uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli
    • Stumpe, S., and E. P. Bakker. 1997. Requirement of a large K+-uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli. Arch. Microbiol. 167:126-136.
    • (1997) Arch. Microbiol , vol.167 , pp. 126-136
    • Stumpe, S.1    Bakker, E.P.2
  • 33
    • 0031831037 scopus 로고    scopus 로고
    • Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli
    • Stumpe, S., R. Schmid, D. L. Stephens, G. Georgiou, and E. P. Bakker. 1998. Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. J. Bacteriol. 180:4002-4006.
    • (1998) J. Bacteriol , vol.180 , pp. 4002-4006
    • Stumpe, S.1    Schmid, R.2    Stephens, D.L.3    Georgiou, G.4    Bakker, E.P.5
  • 34
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten, L., R. A. Kramer, J. Kroon, N. Dekker, M. R. Egmond, and P. Gros. 2001. Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 20:5033-5039.
    • (2001) EMBO J , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 35
    • 0033957876 scopus 로고    scopus 로고
    • Update on meningococcal disease with emphasis on pathogenesis and clinical management
    • van Deuren, M., P. Brandtzaeg, and J. W. M. van der Meer. 2000. Update on meningococcal disease with emphasis on pathogenesis and clinical management. Clin. Microbiol. Rev. 13:144-166.
    • (2000) Clin. Microbiol. Rev , vol.13 , pp. 144-166
    • van Deuren, M.1    Brandtzaeg, P.2    van der Meer, J.W.M.3
  • 36
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan, N., J. Gam, M. J. Olsen, G. Georgiou, and B. L. Iverson. 2005. Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc. Natl. Acad. Sci. USA 102:6855-6860.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 37
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner, M. P., G. L. Costa, W. Schoettlin, J. Cline, E. Mathur, and J. C. Bauer. 1994. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151:119-123.
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.