메뉴 건너뛰기




Volumn 44, Issue 20, 2005, Pages 7559-7569

The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; BACTERIA; CATALYSIS; GENES; HYDROLYSIS; METALLORGANIC POLYMERS; X RAY SPECTROSCOPY;

EID: 18844433603     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050050m     Document Type: Article
Times cited : (115)

References (49)
  • 1
    • 0035675837 scopus 로고    scopus 로고
    • Regulation of gene expression by cell-to-cell communication: Acyl-homoserine lactone quorum sensing
    • Fuqua, C., Parsek, M. R., and Greenberg, E. P. (2001) Regulation of gene expression by cell-to-cell communication: acyl-homoserine lactone quorum sensing, Annu. Rev. Genet. 35, 439-468.
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 439-468
    • Fuqua, C.1    Parsek, M.R.2    Greenberg, E.P.3
  • 3
    • 0037325045 scopus 로고    scopus 로고
    • P. aeruginosa quorum-sensing systems and virulence
    • Smith, R. S., and Iglewski, B. H. (2003) P. aeruginosa quorum-sensing systems and virulence, Curr. Opin. Microbiol. 6, 56-60.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 56-60
    • Smith, R.S.1    Iglewski, B.H.2
  • 5
    • 7044220518 scopus 로고    scopus 로고
    • Quorum sensing: A transcriptional regulatory system involved in the pathogenicity of Burkholderia mallei
    • Ulrich, R. L., Deshazer, D., Hines, H. B., and Jeddeloh, J. A. (2004) Quorum sensing: a transcriptional regulatory system involved in the pathogenicity of Burkholderia mallei, Infect. Immun. 72, 6589-6596.
    • (2004) Infect. Immun. , vol.72 , pp. 6589-6596
    • Ulrich, R.L.1    Deshazer, D.2    Hines, H.B.3    Jeddeloh, J.A.4
  • 6
    • 0038000510 scopus 로고    scopus 로고
    • Quorum quenching and proactive host defense
    • Zhang, L. H. (2003) Quorum quenching and proactive host defense, Trends Plant Sci. 8, 238-244.
    • (2003) Trends Plant Sci. , vol.8 , pp. 238-244
    • Zhang, L.H.1
  • 8
    • 0035859128 scopus 로고    scopus 로고
    • Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase
    • Dong, Y. H., Wang, L. H., Xu, J. L., Zhang, H. B., Zhang, X. F., and Zhang, L. H. (2001) Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase, Nature 411, 813-817.
    • (2001) Nature , vol.411 , pp. 813-817
    • Dong, Y.H.1    Wang, L.H.2    Xu, J.L.3    Zhang, H.B.4    Zhang, X.F.5    Zhang, L.H.6
  • 9
    • 8144220509 scopus 로고    scopus 로고
    • Quorum quenching: Enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis
    • Ulrich, R. L. (2004) Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis, Appl. Environ. Microbiol. 70, 6173-6180.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6173-6180
    • Ulrich, R.L.1
  • 10
    • 0034724191 scopus 로고    scopus 로고
    • AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora
    • Dong, Y. H., Xu, J. L., Li, X. Z., and Zhang, L. H. (2000) AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora, Proc. Natl. Acad. Sci. U.S.A. 97, 3526-3531.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3526-3531
    • Dong, Y.H.1    Xu, J.L.2    Li, X.Z.3    Zhang, L.H.4
  • 11
    • 0033302071 scopus 로고    scopus 로고
    • An evolutionary classification of the metallo-beta-lactamase fold proteins
    • Aravind, L. (1999) An evolutionary classification of the metallo-beta-lactamase fold proteins, In Silico Biol. 1, 69-91.
    • (1999) In Silico Biol. , vol.1 , pp. 69-91
    • Aravind, L.1
  • 12
    • 1842791546 scopus 로고    scopus 로고
    • Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
    • Wang, L. H., Weng, L. X., Dong, Y. H., and Zhang, L. H. (2004) Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase), J. Biol. Chem. 279, 13645-13651.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13645-13651
    • Wang, L.H.1    Weng, L.X.2    Dong, Y.H.3    Zhang, L.H.4
  • 14
    • 0036205598 scopus 로고    scopus 로고
    • Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species
    • Dong, Y. H., Gusti, A. R., Zhang, Q., Xu, J. L., and Zhang, L. H. (2002) Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species, Appl. Environ. Microbiol. 68, 1754-1759.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1754-1759
    • Dong, Y.H.1    Gusti, A.R.2    Zhang, Q.3    Xu, J.L.4    Zhang, L.H.5
  • 16
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust, R. B., Tozser, J., Fox, J. D., Anderson, D. E., Cherry, S., Copeland, T. D., and Waugh, D. S. (2001) Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency, Protein Eng. 14, 993-1000.
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 17
    • 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, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0041846667 scopus 로고    scopus 로고
    • Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: Consequences of and evidence for a hydration reaction
    • Wang, S. C., Person, M. D., Johnson, W. H., Jr., and Whitman, C. P. (2003) Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence for a hydration reaction, Biochemistry 42, 8762-8773.
    • (2003) Biochemistry , vol.42 , pp. 8762-8773
    • Wang, S.C.1    Person, M.D.2    Johnson Jr., W.H.3    Whitman, C.P.4
  • 19
    • 0037413582 scopus 로고    scopus 로고
    • Synthetic analogues of the bacterial signal (quorum sensing) molecule N-(3-oxododecanoyl)-L-homoserine lactone as immune modulators
    • Chhabra, S. R., Harty, C., Hooi, D. S., Daykin, M., Williams, P., Telford, G., Pritchard, D. I., and Bycroft, B. W. (2003) Synthetic analogues of the bacterial signal (quorum sensing) molecule N-(3-oxododecanoyl)-L-homoserine lactone as immune modulators, J. Med. Chem. 46, 97-104.
    • (2003) J. Med. Chem. , vol.46 , pp. 97-104
    • Chhabra, S.R.1    Harty, C.2    Hooi, D.S.3    Daykin, M.4    Williams, P.5    Telford, G.6    Pritchard, D.I.7    Bycroft, B.W.8
  • 20
    • 0015239422 scopus 로고
    • The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C
    • Khalifah, R. G. (1971) The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C, J. Biol. Chem. 246, 2561-2573.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2561-2573
    • Khalifah, R.G.1
  • 21
    • 0030985220 scopus 로고    scopus 로고
    • Catalytic properties of murine carbonic anhydrase IV
    • Hurt, J. D., Tu, C., Laipis, P. J., and Silverman, D. N. (1997) Catalytic properties of murine carbonic anhydrase IV, J. Biol. Chem. 272, 13512-13518.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13512-13518
    • Hurt, J.D.1    Tu, C.2    Laipis, P.J.3    Silverman, D.N.4
  • 23
    • 11744384966 scopus 로고
    • Number of relevant independent points in X-ray-absorption fine-structure spectra
    • Stern, E. A. (1993) Number of relevant independent points in X-ray-absorption fine-structure spectra, Phys. Rev. B 48, 9825-9827.
    • (1993) Phys. Rev. B , vol.48 , pp. 9825-9827
    • Stern, E.A.1
  • 24
    • 0542395209 scopus 로고    scopus 로고
    • Real space multiple scattering calculation and Interpretation of XANES
    • Ankudinov, A. L., Ravel, B., Rehr, J. J., and Condradson, S. D. (1998) Real space multiple scattering calculation and Interpretation of XANES, Phys. Rev. B 58, 7565-7576.
    • (1998) Phys. Rev. B , vol.58 , pp. 7565-7576
    • Ankudinov, A.L.1    Ravel, B.2    Rehr, J.J.3    Condradson, S.D.4
  • 26
    • 0036328528 scopus 로고    scopus 로고
    • Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis
    • Lee, S. J., Park, S. Y., Lee, J. J., Yum, D. Y., Koo, B. T., and Lee, J. K. (2002) Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis, Appl. Environ. Microbiol. 68, 3919-3924.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3919-3924
    • Lee, S.J.1    Park, S.Y.2    Lee, J.J.3    Yum, D.Y.4    Koo, B.T.5    Lee, J.K.6
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 30
    • 0037238544 scopus 로고    scopus 로고
    • Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes
    • Lin, Y. H., Xu, J. L., Hu, J., Wang, L. H., Ong, S. L., Leadbetter, J. R., and Zhang, L. H. (2003) Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes, Mol. Microbiol. 47, 849-860.
    • (2003) Mol. Microbiol. , vol.47 , pp. 849-860
    • Lin, Y.H.1    Xu, J.L.2    Hu, J.3    Wang, L.H.4    Ong, S.L.5    Leadbetter, J.R.6    Zhang, L.H.7
  • 31
    • 0031796990 scopus 로고    scopus 로고
    • Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: The "phantom" subunit and the possible role of Lys7p
    • Lyons, T. J., Nersissian, A., Goto, J. J., Zhu, H., Gralla, E. B., and Valentine, J. S. (1998) Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the "phantom" subunit and the possible role of Lys7p, J. Biol. Inorg. Chem. 3, 650-662.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 650-662
    • Lyons, T.J.1    Nersissian, A.2    Goto, J.J.3    Zhu, H.4    Gralla, E.B.5    Valentine, J.S.6
  • 32
    • 0029980095 scopus 로고    scopus 로고
    • Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates
    • More, M. I., Finger, L. D., Stryker, J. L., Fuqua, C., Eberhard, A., and Winans, S. C. (1996) Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates, Science 272, 1655-1658.
    • (1996) Science , vol.272 , pp. 1655-1658
    • More, M.I.1    Finger, L.D.2    Stryker, J.L.3    Fuqua, C.4    Eberhard, A.5    Winans, S.C.6
  • 33
    • 0037313333 scopus 로고    scopus 로고
    • Arthrobacter strain VAI-A utilizes acyl-homoserine lactone inactivation products and stimulates quorum signal biodegradation by Variovorax paradoxus
    • Flagan, S., Ching, W. K., and Leadbetter, J, R. (2003) Arthrobacter strain VAI-A utilizes acyl-homoserine lactone inactivation products and stimulates quorum signal biodegradation by Variovorax paradoxus, Appl. Environ. Microbiol. 69, 909-916.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 909-916
    • Flagan, S.1    Ching, W.K.2    Leadbetter, J.R.3
  • 35
    • 0034548838 scopus 로고    scopus 로고
    • A novel and sensitive method for the quantification of N-3-oxoacyl homoserine lactones using gas chromatography-mass spectrometry: Application to a model bacterial biofilm
    • Charlton, T. S., de Nys, R., Netting, A., Kumar, N., Hentzer, M., Givskov, M., and Kjelleberg, S. (2000) A novel and sensitive method for the quantification of N-3-oxoacyl homoserine lactones using gas chromatography-mass spectrometry: application to a model bacterial biofilm, Environ. Microbiol. 2, 530-541.
    • (2000) Environ. Microbiol. , vol.2 , pp. 530-541
    • Charlton, T.S.1    De Nys, R.2    Netting, A.3    Kumar, N.4    Hentzer, M.5    Givskov, M.6    Kjelleberg, S.7
  • 37
    • 0035895931 scopus 로고    scopus 로고
    • Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis
    • Zang, T. M., Hollman, D. A., Crawford, P. A., Crowder, M. W., and Makaroff, C. A. (2001) Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis, J. Biol. Chem. 276, 4788-4795.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4788-4795
    • Zang, T.M.1    Hollman, D.A.2    Crawford, P.A.3    Crowder, M.W.4    Makaroff, C.A.5
  • 38
    • 0033200323 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
    • Cameron, A. D., Ridderstrom, M., Olin, B., and Mannervik, B. (1999) Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue, Struct. Folding Des. 7, 1067-1078.
    • (1999) Struct. Folding Des. , vol.7 , pp. 1067-1078
    • Cameron, A.D.1    Ridderstrom, M.2    Olin, B.3    Mannervik, B.4
  • 39
    • 3142738641 scopus 로고    scopus 로고
    • Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II
    • Vogel, A., Schilling, O., and Meyer-Klaucke, W. (2004) Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II, Biochemistry 43, 10379-10386.
    • (2004) Biochemistry , vol.43 , pp. 10379-10386
    • Vogel, A.1    Schilling, O.2    Meyer-Klaucke, W.3
  • 41
    • 0032080039 scopus 로고    scopus 로고
    • The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase
    • Bounaga, S., Laws, A. P., Galleni, M., and Page, M. I. (1998) The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase, Biochem. J. 331 (Part 3), 703-711.
    • (1998) Biochem. J. , vol.331 , Issue.3 PART , pp. 703-711
    • Bounaga, S.1    Laws, A.P.2    Galleni, M.3    Page, M.I.4
  • 43
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-beta-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • Garau, G., Bebrone, C., Anne, C., Galleni, M., Frere, J. M., and Dideberg, O. (2005) A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem, J. Mol. Biol. 345, 785-795.
    • (2005) J. Mol. Biol. , vol.345 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frere, J.M.5    Dideberg, O.6
  • 44
    • 0141928715 scopus 로고    scopus 로고
    • Flexible metal binding of the metallo-beta-lactamase domain: Glyoxalase II incorporates iron, manganese, and zinc in vivo
    • Schilling, O., Wenzel, N., Naylor, M., Vogel, A., Crowder, M., Makaroff, C., and Meyer-Klaucke, W. (2003) Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo, Biochemistry 42, 11777-11786.
    • (2003) Biochemistry , vol.42 , pp. 11777-11786
    • Schilling, O.1    Wenzel, N.2    Naylor, M.3    Vogel, A.4    Crowder, M.5    Makaroff, C.6    Meyer-Klaucke, W.7
  • 45
    • 0038818560 scopus 로고    scopus 로고
    • AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria
    • Park, S. Y., Lee, S. J., Oh, T. K., Oh, J. W., Koo, B. T., Yum, D. Y., and Lee, J. K. (2003) AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria, Microbiology 149, 1541-1550.
    • (2003) Microbiology , vol.149 , pp. 1541-1550
    • Park, S.Y.1    Lee, S.J.2    Oh, T.K.3    Oh, J.W.4    Koo, B.T.5    Yum, D.Y.6    Lee, J.K.7
  • 46
    • 0037007116 scopus 로고    scopus 로고
    • Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens
    • Zhang, H. B., Wang, L. H., and Zhang, L. H. (2002) Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens, Proc. Natl. Acad. Sci. U.S.A. 99, 4638-4643.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4638-4643
    • Zhang, H.B.1    Wang, L.H.2    Zhang, L.H.3
  • 47
    • 0043030084 scopus 로고    scopus 로고
    • The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-Acyl homoserine lactonase activity
    • Carlier, A., Uroz, S., Smadja, B., Fray, R., Latour, X., Dessaux, Y., and Faure, D. (2003) The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-Acyl homoserine lactonase activity, Appl. Environ. Microbiol. 69, 4989-4993.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4989-4993
    • Carlier, A.1    Uroz, S.2    Smadja, B.3    Fray, R.4    Latour, X.5    Dessaux, Y.6    Faure, D.7
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 0033625531 scopus 로고    scopus 로고
    • TEXshade: Shading and labeling of multiple sequence alignments using LATEX2 epsilon
    • Beitz, E. (2000) TEXshade: shading and labeling of multiple sequence alignments using LATEX2 epsilon, Bioinformatics 16, 135-139.
    • (2000) Bioinformatics , vol.16 , pp. 135-139
    • Beitz, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.