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Volumn 181, Issue 21, 1999, Pages 6797-6805

Outer membrane lipoprotein e (P4) of Haemophilus influenzae is a novel phosphomonoesterase

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; EDETIC ACID; HEME; LIPOPROTEIN; MOLYBDIC ACID; OUTER MEMBRANE PROTEIN; PHOSPHATASE; PHOSPHATE; TARTARIC ACID; VANADIC ACID;

EID: 0032730441     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.21.6797-6805.1999     Document Type: Article
Times cited : (46)

References (40)
  • 2
    • 0026471741 scopus 로고
    • The Yersinia tyrosine phosphatase: Specificity of a bacterial virulence determinant for phosphoproteins in the J774a.1 macrophage
    • Bliska, J. B., J. C. Clemens, J. E. Dixon, and S. Falkow. 1992. The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774a.1 macrophage. J. Exp. Med. 176:1625-1630.
    • (1992) J. Exp. Med. , vol.176 , pp. 1625-1630
    • Bliska, J.B.1    Clemens, J.C.2    Dixon, J.E.3    Falkow, S.4
  • 3
    • 77956860575 scopus 로고
    • Lipoproteins, structure, function, biosynthesis and model for protein export
    • Braun, V., and H. C. Wu. 1994. Lipoproteins, structure, function, biosynthesis and model for protein export. New Comp. Biochem. 27:319-341.
    • (1994) New Comp. Biochem. , vol.27 , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 4
    • 0027092553 scopus 로고
    • A simple computer program with statistical tests for the analysis of enzyme kinetics
    • Brooks, S. P. J. 1992. A simple computer program with statistical tests for the analysis of enzyme kinetics. BioTechniques 13:906-911.
    • (1992) BioTechniques , vol.13 , pp. 906-911
    • Brooks, S.P.J.1
  • 5
    • 17644449014 scopus 로고    scopus 로고
    • Temperature dependent expression of an acid phosphatase by Bordeiella bronchiseptica: Role in intracellular survival
    • Chhatwal, G. S., M. J. Walker, H. Yan, K. N. Timmis, and C. A. Guzman. 1997. Temperature dependent expression of an acid phosphatase by Bordeiella bronchiseptica: role in intracellular survival. Microb. Pathog. 22:257-264.
    • (1997) Microb. Pathog. , vol.22 , pp. 257-264
    • Chhatwal, G.S.1    Walker, M.J.2    Yan, H.3    Timmis, K.N.4    Guzman, C.A.5
  • 6
    • 77956859072 scopus 로고
    • Phosphomonoesterases
    • A. Neuberger and K. Brocklenhurst (ed.). Elsevier Science, New York, N.Y.
    • Coleman, J. E., and M. J. Besman. 1987. Phosphomonoesterases, p. 377-406. In A. Neuberger and K. Brocklenhurst (ed.), Hydrolytic enzymes. Elsevier Science, New York, N.Y.
    • (1987) Hydrolytic Enzymes , pp. 377-406
    • Coleman, J.E.1    Besman, M.J.2
  • 7
    • 0026589122 scopus 로고
    • Pseudomonas aeruginosa acid phosphatase: Activation by divalent cations and inhibition by aluminum ion
    • Domenich, C. E., A. L. Teresita, M. A. Salvano, and M. N. Garrido. 1992. Pseudomonas aeruginosa acid phosphatase: activation by divalent cations and inhibition by aluminum ion. FEBS Lett. 299:96-98.
    • (1992) FEBS Lett. , vol.299 , pp. 96-98
    • Domenich, C.E.1    Teresita, A.L.2    Salvano, M.A.3    Garrido, M.N.4
  • 9
    • 0030738452 scopus 로고    scopus 로고
    • The lppC gene of Streptococcus equisimilis encodes a lipoprotein that is homologous to the e (P4) outer membrane protein from Haemophilus influenzae
    • Gase, K., G. Liu, A. Bruckmann, K. Steiner, J. Ozegowski, and H. Malke. 1997. The lppC gene of Streptococcus equisimilis encodes a lipoprotein that is homologous to the e (P4) outer membrane protein from Haemophilus influenzae. Med. Microbiol. Immunol. 184:63-73.
    • (1997) Med. Microbiol. Immunol. , vol.184 , pp. 63-73
    • Gase, K.1    Liu, G.2    Bruckmann, A.3    Steiner, K.4    Ozegowski, J.5    Malke, H.6
  • 11
    • 0025866724 scopus 로고
    • The e (P4) outer membrane protein of Haemophilus influenzae; biologic activity of anti-e serum and cloning and sequencing of the structural gene
    • Green, B. A., J. E. Parley, T. Quinn-Dey, R. A. Deich, and G. W. Zlotnick. 1991. The e (P4) outer membrane protein of Haemophilus influenzae; biologic activity of anti-e serum and cloning and sequencing of the structural gene. Infect. Immun. 59:3191-3198.
    • (1991) Infect. Immun. , vol.59 , pp. 3191-3198
    • Green, B.A.1    Parley, J.E.2    Quinn-Dey, T.3    Deich, R.A.4    Zlotnick, G.W.5
  • 12
    • 0029052471 scopus 로고
    • Mechanism-based inactivation of porcine kidney diamine oxidase by 1,4-diamino-2-butene
    • He, Z., Y. Zou, and F. T. Greenaway. 1995. Mechanism-based inactivation of porcine kidney diamine oxidase by 1,4-diamino-2-butene. Arch. Biochem. Biophys. 319:185-195.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 185-195
    • He, Z.1    Zou, Y.2    Greenaway, F.T.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-695.
    • (1970) Nature , vol.227 , pp. 680-695
    • Laemmli, U.K.1
  • 14
  • 15
    • 0019191873 scopus 로고
    • Outer membrane protein composition in disease isolates of Haemophilus influenzae: Pathogenic and epidemiological implications
    • Loeb, M. R., and D. H. Smith. 1980. Outer membrane protein composition in disease isolates of Haemophilus influenzae: pathogenic and epidemiological implications. Infect. Immun. 30:709-717.
    • (1980) Infect. Immun. , vol.30 , pp. 709-717
    • Loeb, M.R.1    Smith, D.H.2
  • 16
    • 0031813761 scopus 로고    scopus 로고
    • Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase
    • Malke, H. 1998. Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase. Appl. Environ. Microbiol. 64: 2439-2442.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2439-2442
    • Malke, H.1
  • 18
    • 0028219490 scopus 로고
    • Purification and characterization of an acid phosphatase from Mycoplasma fermentans
    • Noda, M., K. Shibata, Y. Sawa, H. Shimokoube, and T. Watanabe. 1994. Purification and characterization of an acid phosphatase from Mycoplasma fermentans. Microbiol. Immunol. 38:103-107.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 103-107
    • Noda, M.1    Shibata, K.2    Sawa, Y.3    Shimokoube, H.4    Watanabe, T.5
  • 19
    • 0023000993 scopus 로고
    • [Phosphotyrosine] protein phosphatase in rat brain: A major phosphotyrosine protein phosphatase is a 23 kD protein distinct from acid phosphatase
    • Okada, M., K. Owada, and H. Nakagawa. 1986. [Phosphotyrosine] protein phosphatase in rat brain: a major phosphotyrosine protein phosphatase is a 23 kD protein distinct from acid phosphatase. Biochem. J. 289:155-162.
    • (1986) Biochem. J. , vol.289 , pp. 155-162
    • Okada, M.1    Owada, K.2    Nakagawa, H.3
  • 20
    • 0030046924 scopus 로고    scopus 로고
    • Lipoprotein e(P4) is essential for hemin uptake by Haemophilus influenzae
    • Reidl, J., and J. J. Mekalanos. 1996. Lipoprotein e(P4) is essential for hemin uptake by Haemophilus influenzae. J. Exp. Med. 183:621-629.
    • (1996) J. Exp. Med. , vol.183 , pp. 621-629
    • Reidl, J.1    Mekalanos, J.J.2
  • 21
    • 0345200583 scopus 로고    scopus 로고
    • Identification and partial purification and characterization of an outer membrane phosphomonoesterase from a nontypeable Haemophilus influenzae
    • Washington, D.C.
    • Reilly, T. J., D. L. Chance, and A. L. Smith. 1998. Identification and partial purification and characterization of an outer membrane phosphomonoesterase from a nontypeable Haemophilus influenzae, p. 300. In Abstracts of the 98th General Meeting of the American Society for Microbiology, Washington, D.C.
    • (1998) Abstracts of the 98th General Meeting of the American Society for Microbiology , pp. 300
    • Reilly, T.J.1    Chance, D.L.2    Smith, A.L.3
  • 22
    • 15844404772 scopus 로고    scopus 로고
    • Characterization and sequencing of a respiratory burst-inhibiting acid phosphatase from Francisella tularensis
    • Reilly, T. J., G. S. Baron, F. E. Nano, and M. S. Kuhlenschmidt. 1996. Characterization and sequencing of a respiratory burst-inhibiting acid phosphatase from Francisella tularensis. J. Biol. Chem. 271:10973-10983.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10973-10983
    • Reilly, T.J.1    Baron, G.S.2    Nano, F.E.3    Kuhlenschmidt, M.S.4
  • 24
    • 0031689411 scopus 로고    scopus 로고
    • Bacterial nonspecific acid phosphohydrolases: Physiology, evolution, and use as tools in microbial biotechnology
    • Rossolini, G. M., S. Schippa, M. L. Riccio, F. Berlutti, L. E. Macaskie, and M. C. Thaller. 1998. Bacterial nonspecific acid phosphohydrolases: physiology, evolution, and use as tools in microbial biotechnology. Cell. Mol. Life Sci. 54:833-850.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 833-850
    • Rossolini, G.M.1    Schippa, S.2    Riccio, M.L.3    Berlutti, F.4    Macaskie, L.E.5    Thaller, M.C.6
  • 25
    • 0022398312 scopus 로고
    • Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils
    • Saha, A. K., J. N. Dowling, K. L. LaMarco, S. Das, A. T. Remaley, N. Olomu, M. T. Pope, and R. H. Glew. 1985. Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils. Arch. Biochem. Biophys. 243:150-160.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 150-160
    • Saha, A.K.1    Dowling, J.N.2    LaMarco, K.L.3    Das, S.4    Remaley, A.T.5    Olomu, N.6    Pope, M.T.7    Glew, R.H.8
  • 27
    • 0014879933 scopus 로고
    • Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli
    • Schnaitman, C. A. 1970. Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli. J. Bacteriol. 104:890-901.
    • (1970) J. Bacteriol. , vol.104 , pp. 890-901
    • Schnaitman, C.A.1
  • 29
    • 0030038220 scopus 로고    scopus 로고
    • Progress towards a vaccine for nontypeable Haemophilus influenzae
    • St. Geme, J. W. 1996. Progress towards a vaccine for nontypeable Haemophilus influenzae. Ann. Med. 28:31-37.
    • (1996) Ann. Med. , vol.28 , pp. 31-37
    • St. Geme, J.W.1
  • 30
    • 0031820043 scopus 로고    scopus 로고
    • Conserved sequence motifs among bacterial eukaryotic and archaeal phosphatases that define a new phosphohydrolase superfamily
    • Thaller, M. C., S. Schippa, and G. M. Rossolini. 1998. Conserved sequence motifs among bacterial eukaryotic and archaeal phosphatases that define a new phosphohydrolase superfamily. Protein Sci. 7:1647-1652.
    • (1998) Protein Sci. , vol.7 , pp. 1647-1652
    • Thaller, M.C.1    Schippa, S.2    Rossolini, G.M.3
  • 32
    • 0021235776 scopus 로고
    • Pathogenicity of Haemophilus influenzae
    • Turk, D. C. 1984. Pathogenicity of Haemophilus influenzae. J. Med. Microbiol. 18:1-16.
    • (1984) J. Med. Microbiol. , vol.18 , pp. 1-16
    • Turk, D.C.1
  • 33
    • 0001929689 scopus 로고
    • Clinical importance of Haemophilus influenzae - 1981
    • S. H. Sell and P. F. Wright (ed.). Elsevier Biomedical, New York, N.Y.
    • Turk, D. C. 1982. Clinical importance of Haemophilus influenzae - 1981, p. 3-9. In S. H. Sell and P. F. Wright (ed.), Haemophilus influenzae: epidemiology, immunology and prevention of disease. Elsevier Biomedical, New York, N.Y.
    • (1982) Haemophilus Influenzae: Epidemiology, Immunology and Prevention of Disease , pp. 3-9
    • Turk, D.C.1
  • 34
    • 0021835799 scopus 로고
    • Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b
    • Vachon, V. D., J. Lyew, and J. W. Coulton. 1985. Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b. J. Bacteriol. 162:918-925.
    • (1985) J. Bacteriol. , vol.162 , pp. 918-925
    • Vachon, V.D.1    Lyew, J.2    Coulton, J.W.3
  • 35
    • 0026075511 scopus 로고
    • Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen
    • Vincent, J. B., M. W. Crowder, and B. A. Averill. 1991. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. J. Biol. Chem. 266:17737-17740.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17737-17740
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 36
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • Vincent, J. B., M. W. Crowder, and B. A. Averill. 1992. Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends Biochem. Sci. 17:105-110.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 37
    • 0023908621 scopus 로고
    • Purification and physiochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity
    • Waheed, A., P. M. Laidler, Y. Y. P. Wo, and R. L. Van Etten. 1988. Purification and physiochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity. Biochemistry 27:4265-4273.
    • (1988) Biochemistry , vol.27 , pp. 4265-4273
    • Waheed, A.1    Laidler, P.M.2    Wo, Y.Y.P.3    Van Etten, R.L.4
  • 38
    • 0016768240 scopus 로고
    • Isolation and characterization of mutants of Haemophilus influenzae deficient in an adenosine 5′-triphosphate-dependent deoxyribonuclease activity
    • Wilcox, K. W., and H. O. Smith. 1975. Isolation and characterization of mutants of Haemophilus influenzae deficient in an adenosine 5′-triphosphate-dependent deoxyribonuclease activity. J. Bacteriol. 122:443-453.
    • (1975) J. Bacteriol. , vol.122 , pp. 443-453
    • Wilcox, K.W.1    Smith, H.O.2
  • 39
    • 0029005376 scopus 로고
    • Affinity, conservation, and surface exposure of hemopexin binding proteins in Haemophilus influenzae
    • Wong, J. C., Y. R. Patel, D. Kendall, P. W. Whitby, A. Smith, J. Holland, and P. Williams. 1995. Affinity, conservation, and surface exposure of hemopexin binding proteins in Haemophilus influenzae. Infect. Immun. 63:2327-2333.
    • (1995) Infect. Immun. , vol.63 , pp. 2327-2333
    • Wong, J.C.1    Patel, Y.R.2    Kendall, D.3    Whitby, P.W.4    Smith, A.5    Holland, J.6    Williams, P.7
  • 40
    • 0024995069 scopus 로고
    • Purification and characterization of a low molecular weight acid phosphatase-A phosphotyrosyl protein phosphatase from bovine heart
    • Zhang, Z. Y., and R. L. Van Etten. 1990. Purification and characterization of a low molecular weight acid phosphatase-A phosphotyrosyl protein phosphatase from bovine heart. Arch. Biochem. Biophys. 282:39-49.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 39-49
    • Zhang, Z.Y.1    Van Etten, R.L.2


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