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Volumn 19, Issue 2, 2012, Pages 186-193

Pseudomonas aeruginosa cif defines a distinct class of α/ βepoxide hydrolases utilizing a his/tyr ring-opening pair

Author keywords

; Cystic fibrosis; Dehalogenases; Enzyme mechanism; Epoxide hydrolases; Hydrolase phylogeny; Protein structure; Site directed mutagenesis; X ray crystallography

Indexed keywords

ALPHA EPOXIDE HYDROLASE; BETA EPOXIDE HYDROLASE; EPOXIDE HYDROLASE; EPOXIDE HYDROLASE CIF; HISTIDINE; TYROSINE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84858830632     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986612799080392     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0031002998 scopus 로고    scopus 로고
    • Genetic toxicology of epichlorohydrin: A review
    • DOI 10.1016/S1383-5742(96)00042-7, PII S1383574296000425
    • Giri, A. Genetic toxicology of epichlorohydrin: a review. Mutat Res, 1997, 386, 25-38. (Pubitemid 27195023)
    • (1997) Mutation Research - Reviews in Mutation Research , vol.386 , Issue.1 , pp. 25-38
    • Giri, A.K.1
  • 3
    • 0014690413 scopus 로고
    • Tartaric acid metabolism. IX. Synthesis with tartrate epoxidase
    • Allen, R. H.; Jakoby, W. B. Tartaric acid metabolism. IX. Synthesis with tartrate epoxidase. J. Biol. Chem., 1969, 244, 2078-84.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2078-2084
    • Allen, R.H.1    Jakoby, W.B.2
  • 4
    • 0016030295 scopus 로고
    • Biosynthesis of fosfomycin by Streptomyces fradiae
    • Rogers, T. O.; Birnbaum, J. Biosynthesis of fosfomycin by Streptomyces fradiae. Antimicrob. Agents Chemother., 1974, 5, 121-32.
    • (1974) Antimicrob. Agents Chemother. , vol.5 , pp. 121-132
    • Rogers, T.O.1    Birnbaum, J.2
  • 5
    • 0026348175 scopus 로고
    • Characterization of the epoxide hydrolase from an epichlorohydrin- degrading Pseudomonas sp
    • Jacobs, M. H.; Van den Wijngaard, A. J.; Pentenga, M.; Janssen, D. B. Characterization of the epoxide hydrolase from an epichlorohydrin-degrading Pseudomonas sp. Eur. J. Biochem., 1991, 202, 1217-22.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1217-1222
    • Jacobs, M.H.1    Van Den Wijngaard, A.J.2    Pentenga, M.3    Janssen, D.B.4
  • 6
    • 46449128551 scopus 로고    scopus 로고
    • Cif is negatively regulated by the TetR family repressor CifR
    • MacEachran, D. P.; Stanton, B. A.; O'Toole, G. A. Cif is negatively regulated by the TetR family repressor CifR. Infect. Immun., 2008, 76, 3197-206.
    • (2008) Infect. Immun. , vol.76 , pp. 3197-3206
    • MacEachran, D.P.1    Stanton, B.A.2    O'Toole, G.A.3
  • 7
    • 77949761912 scopus 로고    scopus 로고
    • Crystal structure of the Cystic Fibrosis Transmembrane Conductance Regulator Inhibitory Factor Cif reveals novel active-site features of an epoxide hydrolase virulence factor
    • Bahl, C. D.; Morisseau, C.; Bomberger, J. M.; Stanton, B. A.; Hammock, B. D.; O'Toole, G. A.; Madden, D. R. Crystal structure of the Cystic Fibrosis Transmembrane Conductance Regulator Inhibitory Factor Cif reveals novel active-site features of an epoxide hydrolase virulence factor. J. Bacteriol., 2010, 192, 1785-1795.
    • (2010) J. Bacteriol. , vol.192 , pp. 1785-1795
    • Bahl, C.D.1    Morisseau, C.2    Bomberger, J.M.3    Stanton, B.A.4    Hammock, B.D.5    O'Toole, G.A.6    Madden, D.R.7
  • 8
    • 34547645814 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa secreted protein PA2934 decreases apical membrane expression of the cystic fibrosis transmembrane conductance regulator
    • DOI 10.1128/IAI.00338-07
    • MacEachran, D. P.; Ye, S.; Bomberger, J. M.; Hogan, D. A.; Swiatecka-Urban, A.; Stanton, B. A.; O'Toole, G. A. The Pseudomonas aeruginosa secreted protein PA2934 decreases apical membrane expression of the cystic fibrosis transmembrane conductance regulator. Infect. Immun., 2007, 75, 3902-12. (Pubitemid 47206288)
    • (2007) Infection and Immunity , vol.75 , Issue.8 , pp. 3902-3912
    • MacEachran, D.P.1    Ye, S.2    Bomberger, J.M.3    Hogan, D.A.4    Swiatecka-Urban, A.5    Stanton, B.A.6    O'Toole, G.A.7
  • 10
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: The family keeps growing
    • Nardini, M.; Dijkstra, B. W.α/β hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol., 1999, 9, 732-7.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 11
    • 30144442042 scopus 로고    scopus 로고
    • Epoxide hydrolases: Structure, function, mechanism, and assay
    • Arand, M.; Cronin, A.; Adamska, M.; Oesch, F. Epoxide hydrolases: structure, function, mechanism, and assay. Methods Enzymol., 2005, 400, 569-88.
    • (2005) Methods Enzymol. , vol.400 , pp. 569-588
    • Arand, M.1    Cronin, A.2    Adamska, M.3    Oesch, F.4
  • 12
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases: Mechanisms, inhibitor designs, and biological roles
    • DOI 10.1146/annurev.pharmtox.45.120403.095920
    • Morisseau, C.; Hammock, B. D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol., 2005, 45, 311-33. (Pubitemid 40261808)
    • (2005) Annual Review of Pharmacology and Toxicology , vol.45 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 14
    • 0034725581 scopus 로고    scopus 로고
    • Biochemical evidence for the involvement of tyrosine in epoxide activation during the catalytic cycle of epoxide hydrolase
    • DOI 10.1074/jbc.M001464200
    • Yamada, T.; Morisseau, C.; Maxwell, J. E.; Argiriadi, M. A.; Christianson, D. W.; Hammock, B. D. Biochemical evidence for the involvement of tyrosine in epoxide activation during the catalytic cycle of epoxide hydrolase. J. Biol. Chem., 2000, 275, 23082-8. (Pubitemid 30646199)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 23082-23088
    • Yamada, T.1    Morisseau, C.2    Maxwell, J.E.3    Argiriadi, M.A.4    Christianson, D.W.5    Hammock, B.D.6
  • 15
    • 0345624451 scopus 로고    scopus 로고
    • Mutation of tyrosine residues involved in the alkylation half reaction of epoxide hydrolase from Agrobacterium radiobacter AD1 results in improved enantioselectivity [7]
    • DOI 10.1021/ja990501o
    • Rink, R.; Lutje Spelberg, J. H.; Pieters, R. J.; Kingma, J.; Nardini, M.; Kellogg, R. M.; Dijkstra, B. W.; Janssen, D. B. Mutation of Tyrosine Residues Involved in the Alkylation Half Reaction of Epoxide Hydrolase from Agrobacterium radiobacter AD1 Results in Improved Enantioselectivity. J. Am. Chem. Soc., 1999, 121, 7417-7418. (Pubitemid 29400172)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.32 , pp. 7417-7418
    • Rink, R.1    Lutje Spelberg, J.H.2    Pieters, R.J.3    Kingma, J.4    Nardini, M.5    Kellogg, R.M.6    Dijkstra, B.W.7    Janssen, D.B.8
  • 16
    • 33646084392 scopus 로고    scopus 로고
    • Diversity and biocatalytic potential of epoxide hydrolases identified by genome analysis
    • van Loo, B.; Kingma, J.; Arand, M.; Wubbolts, M. G.; Janssen, D. B. Diversity and biocatalytic potential of epoxide hydrolases identified by genome analysis. Appl. Environ. Microbiol., 2006, 72, 2905-17.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2905-2917
    • Van Loo, B.1    Kingma, J.2    Arand, M.3    Wubbolts, M.G.4    Janssen, D.B.5
  • 17
    • 75149129980 scopus 로고    scopus 로고
    • Purification crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa
    • Bahl, C. D.; MacEachran, D. P.; O'Toole, G. A.; Madden, D. R. Purification, crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa. Acta. Crystallogr., 2010, F66, 26-28.
    • (2010) Acta. Crystallogr. , vol.F66 , pp. 26-28
    • Bahl, C.D.1    MacEachran, D.P.2    O'Toole, G.A.3    Madden, D.R.4
  • 18
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst., 1993, 26, 795-800.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 23
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm, L.; Kaariainen, S.; Rosenstrom, P.; Schenkel, A. Searching protein structure databases with DaliLite v.3. Bioinformatics, 2008, 24, 2780-1. (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 24
    • 28444455635 scopus 로고    scopus 로고
    • Colorimetric assays for quantitative analysis and screening of epoxide hydrolase activity
    • DOI 10.1007/s10529-005-3904-1
    • Cedrone, F.; Bhatnagar, T.; Baratti, J. C. Colorimetric assays for quantitative analysis and screening of epoxide hydrolase activity. Biotechnol. Lett., 2005, 27, 1921-7. (Pubitemid 41740488)
    • (2005) Biotechnology Letters , vol.27 , Issue.23-24 , pp. 1921-1927
    • Cedrone, F.1    Bhatnagar, T.2    Baratti, J.C.3
  • 26
    • 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.; Gibson, T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 1994, 22, 4673-80. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 77956658765 scopus 로고    scopus 로고
    • Salzberg, S.L. ; Searls, D.B.; Kasif S., Eds.;Elsevier Science B. V: Amsterdam
    • Jones, D.; Steven L. Salzberg, D. B. S.; Simon, K. In: New Comprehensive Biochemistry; Salzberg, S.L. ; Searls, D.B.; Kasif S., Eds.; Elsevier Science B. V: Amsterdam, 1998; Vol. 32, pp. 285-311.
    • (1998) New Comprehensive Biochemistry , vol.32 , pp. 285-311
    • Jones, D.1    Steven, L.2    Salzberg, D.B.S.3    Simon, K.4
  • 28
    • 1942438591 scopus 로고    scopus 로고
    • Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis
    • DOI 10.1021/bi036189j
    • Gomez, G. A.; Morisseau, C.; Hammock, B. D.; Christianson, D. W. Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis. Biochemistry, 2004, 43, 4716-23. (Pubitemid 38509092)
    • (2004) Biochemistry , vol.43 , Issue.16 , pp. 4716-4723
    • Gomez, G.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 29
    • 0034651639 scopus 로고    scopus 로고
    • Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: Implications for the structure and function of the mammalian microsomal class of epoxide hydrolases
    • DOI 10.1016/S0969-2126(00)00087-3
    • Zou, J.; Hallberg, B. M.; Bergfors, T.; Oesch, F.; Arand, M.; Mowbray, S. L.; Jones, T. A. Structure of Aspergillus niger epoxide hydrolase at 1.8 Å resolution: implications for the structure and function of the mammalian microsomal class of epoxide hydrolases. Structure, 2000, 8, 111-22. (Pubitemid 30097357)
    • (2000) Structure , vol.8 , Issue.2 , pp. 111-122
    • Zou, J.1    Hallberg, B.M.2    Bergfors, T.3    Oesch, F.4    Arand, M.5    Mowbray, S.L.6    Jones, T.A.7
  • 30
    • 0033591361 scopus 로고    scopus 로고
    • The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides
    • Nardini, M.; Ridder, I. S.; Rozeboom, H. J.; Kalk, K. H.; Rink, R.; Janssen, D. B.; Dijkstra, B. W. The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides. J. Biol. Chem., 1999, 274, 14579-86.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14579-14586
    • Nardini, M.1    Ridder, I.S.2    Rozeboom, H.J.3    Kalk, K.H.4    Rink, R.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 31
    • 29344455172 scopus 로고    scopus 로고
    • Human soluble epoxide hydrolase: Structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids
    • DOI 10.1110/ps.051720206
    • Gomez, G. A.; Morisseau, C.; Hammock, B. D.; Christianson, D. W. Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids. Protein Sci., 2006, 15, 58-64. (Pubitemid 43004233)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 58-64
    • Gomez, G.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 32
    • 65249098870 scopus 로고    scopus 로고
    • X-Ray crystallographic and mutational studies of fluoroacetate dehalogenase from Burkholderia sp. strain FA1
    • Jitsumori, K.; Omi, R.; Kurihara, T.; Kurata, A.; Mihara, H.; Miyahara, I.; Hirotsu, K.; Esaki, N. X-Ray crystallographic and mutational studies of fluoroacetate dehalogenase from Burkholderia sp. strain FA1. J. Bacteriol., 2009, 191, 2630-7.
    • (2009) J. Bacteriol. , vol.191 , pp. 2630-2637
    • Jitsumori, K.1    Omi, R.2    Kurihara, T.3    Kurata, A.4    Mihara, H.5    Miyahara, I.6    Hirotsu, K.7    Esaki, N.8
  • 35
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • DOI 10.1038/nsb0497-269
    • Diederichs, K.; Karplus, P. A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol., 1997, 4, 269-75. (Pubitemid 27157198)
    • (1997) Nature Structural Biology , vol.4 , Issue.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2


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