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Volumn 692, Issue , 2011, Pages 275-290

Heterologous Overexpression, Purification, and In Vitro Characterization of AHL Lactonases

Author keywords

Enzyme kinetics; Lactonase; Metalloprotein; N acyl l homoserine lactone; Protein purification; Quorum quenching

Indexed keywords

AIIA PROTEIN, BACILLUS; BACTERIAL PROTEIN; CARBOXYLESTERASE; METAL; METALLOPROTEINASE; N ACYL HOMOSERINE LACTONASE; N-ACYL HOMOSERINE LACTONASE;

EID: 79952198419     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-60761-971-0_20     Document Type: Chapter
Times cited : (12)

References (25)
  • 1
    • 34447576760 scopus 로고    scopus 로고
    • Quorum-quenching microbial infections: Mechanisms and implications
    • Dong, Y. H., Wang, L. H., and Zhang, L. H. (2007) Quorum-quenching microbial infections: mechanisms and implications, Philos. Trans. R. Soc. Lond. B Biol. Sci. 362, 1201–1211.
    • (2007) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.362 , pp. 1201-1211
    • Dong, Y.H.1    Wang, L.H.2    Zhang, L.H.3
  • 2
    • 45549098790 scopus 로고    scopus 로고
    • Bacterial quorum sensing: A new target for anti-infective immunotherapy
    • Kaufmann, G. F., Park, J., and Janda, K. D. (2008) Bacterial quorum sensing: a new target for anti-infective immunotherapy, Expert Opin. Biol. Ther. 8, 719–724.
    • (2008) Expert Opin. Biol. Ther. , vol.8 , pp. 719-724
    • Kaufmann, G.F.1    Park, J.2    Janda, K.D.3
  • 5
    • 77449107859 scopus 로고    scopus 로고
    • Cross species quorum quenching using a native AI-2 processing enzyme
    • Roy, V., Fernandes, R., Tsao, C. Y., and Bentley, W. E. (2010) Cross species quorum quenching using a native AI-2 processing enzyme, ACS Chem. Biol. 5(2), 223–232.
    • (2010) ACS Chem. Biol. , vol.5 , Issue.2 , pp. 223-232
    • Roy, V.1    Fernandes, R.2    Tsao, C.Y.3    Bentley, W.E.4
  • 6
    • 0037468237 scopus 로고    scopus 로고
    • Degradation of N-acylhomoserine lactones, the bacterial quorum-sensing molecules, by acylase
    • Xu, F., Byun, T., Deussen, H. J., and Duke, K. R. (2003) Degradation of N-acylhomoserine lactones, the bacterial quorum-sensing molecules, by acylase, J. Biotechnol. 101, 89–96.
    • (2003) J. Biotechnol. , vol.101 , pp. 89-96
    • Xu, F.1    Byun, T.2    Deussen, H.J.3    Duke, K.R.4
  • 7
    • 18444375881 scopus 로고    scopus 로고
    • Identification of extracellular N-acylhomoserine lactone acylase from a Streptomyces sp. and its application to quorum quenching
    • Park, S. Y., Kang, H. O., Jang, H. S., Lee, J. K., Koo, B. T., and Yum, D. Y. (2005) Identification of extracellular N-acylhomoserine lactone acylase from a Streptomyces sp. and its application to quorum quenching, Appl. Environ. Microbiol. 71, 2632–2641.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2632-2641
    • Park, S.Y.1    Kang, H.O.2    Jang, H.S.3    Lee, J.K.4    Koo, B.T.5    Yum, D.Y.6
  • 8
    • 46249112510 scopus 로고    scopus 로고
    • Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-L-homoserine lactone
    • Teiber, J. F., Horke, S., Haines, D. C., Chowdhary, P. K., Xiao, J., Kramer, G. L., Haley, R. W., and Draganov, D. I. (2008) Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-L-homoserine lactone, Infect. Immun. 76, 2512–2519.
    • (2008) Infect. Immun. , vol.76 , pp. 2512-2519
    • Teiber, J.F.1    Horke, S.2    Haines, D.C.3    Chowdhary, P.K.4    Xiao, J.5    Kramer, G.L.6    Haley, R.W.7    Draganov, D.I.8
  • 9
    • 33750695657 scopus 로고    scopus 로고
    • The quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect
    • Momb, J., Thomas, P. W., Breece, R. M., Tierney, D. L., and Fast, W. (2006) The quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect, Biochemistry 45, 13385–13393.
    • (2006) Biochemistry , vol.45 , pp. 13385-13393
    • Momb, J.1    Thomas, P.W.2    Breece, R.M.3    Tierney, D.L.4    Fast, W.5
  • 10
    • 33847079152 scopus 로고    scopus 로고
    • Antibody catalyzed hydrolysis of a quorum sensing signal found in Gram-negative bacteria
    • De Lamo Marin, S., Xu, Y., Meijler, M. M., and Janda, K. D. (2007) Antibody catalyzed hydrolysis of a quorum sensing signal found in Gram-negative bacteria, Bioorg. Med. Chem. Lett. 17, 1549–1552.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1549-1552
    • de Lamo Marin, S.1    Xu, Y.2    Meijler, M.M.3    Janda, K.D.4
  • 11
    • 66149192520 scopus 로고    scopus 로고
    • Directed evolution of a quorum-quenching lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the amidohydrolase superfamily
    • Chow, J. Y., Wu, L., and Yew, W. S. (2009) Directed evolution of a quorum-quenching lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the amidohydrolase superfamily, Biochemistry 48, 4344–4353.
    • (2009) Biochemistry , vol.48 , pp. 4344-4353
    • Chow, J.Y.1    Wu, L.2    Yew, W.S.3
  • 12
    • 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
  • 13
    • 23844552796 scopus 로고    scopus 로고
    • Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis
    • Liu, D., Lepore, B. W., Petsko, G. A., Thomas, P. W., Stone, E. M., Fast, W., and Ringe, D. (2005) Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis, Proc. Natl. Acad. Sci. U. S. A. 102, 11882–11887.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11882-11887
    • Liu, D.1    Lepore, B.W.2    Petsko, G.A.3    Thomas, P.W.4    Stone, E.M.5    Fast, W.6    Ringe, D.7
  • 14
    • 47649131677 scopus 로고    scopus 로고
    • Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures
    • Liu, D., Momb, J., Thomas, P. W., Moulin, A., Petsko, G. A., Fast, W., and Ringe, D. (2008) Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures, Biochemistry 47, 7706–7714.
    • (2008) Biochemistry , vol.47 , pp. 7706-7714
    • Liu, D.1    Momb, J.2    Thomas, P.W.3    Moulin, A.4    Petsko, G.A.5    Fast, W.6    Ringe, D.7
  • 15
    • 47649125426 scopus 로고    scopus 로고
    • On the mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis: 2. Substrate modeling and active site mutations
    • Momb, J., Wang, C., Liu, D., Thomas, P. W., Petsko, G. A., Guo, H., Ringe, D., and Fast, W. (2008) On the mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis: 2. Substrate modeling and active site mutations, Biochemistry 47, 7715–7725.
    • (2008) Biochemistry , vol.47 , pp. 7715-7725
    • Momb, J.1    Wang, C.2    Liu, D.3    Thomas, P.W.4    Petsko, G.A.5    Guo, H.6    Ringe, D.7    Fast, W.8
  • 17
    • 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
  • 18
    • 18844433603 scopus 로고    scopus 로고
    • The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein
    • Thomas, P. W., Stone, E. M., Costello, A. L., Tierney, D. L., and Fast, W. (2005) The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein, Biochemistry 44, 7559–7569.
    • (2005) Biochemistry , vol.44 , pp. 7559-7569
    • Thomas, P.W.1    Stone, E.M.2    Costello, A.L.3    Tierney, D.L.4    Fast, W.5
  • 21
    • 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
  • 24
    • 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


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