메뉴 건너뛰기




Volumn 149, Issue 6, 2003, Pages 1559-1567

Site-directed mutagenesis of an extradiol dioxygenase involved in tetralin biodegradation identifies residues important for activity or substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE DERIVATIVE; OXYGENASE; POLYCYCLIC HYDROCARBON; TETRALIN DERIVATIVE;

EID: 0037804208     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26034-0     Document Type: Article
Times cited : (12)

References (32)
  • 1
    • 0026558894 scopus 로고
    • Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating
    • Adams, R. H., Huang, C.-M., Higson, F. K., Brenner, V. & Focht, D. D. (1992). Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating. Appl Environ Microbiol 58, 647-654.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 647-654
    • Adams, R.H.1    Huang, C.-M.2    Higson, F.K.3    Brenner, V.4    Focht, D.D.5
  • 3
    • 0342948903 scopus 로고    scopus 로고
    • Identification of an extradiol dioxygenase involved in tetralin biodegradation: Gene sequence analysis and purification and characterization of the gene product
    • Andújar, E., Hernáez, M. J., Kaschabek, S. R., Reineke, W. & Santero, E. (2000). Identification of an extradiol dioxygenase involved in tetralin biodegradation: gene sequence analysis and purification and characterization of the gene product. J Bacteriol 182, 789-795.
    • (2000) J. Bacteriol. , vol.182 , pp. 789-795
    • Andújar, E.1    Hernáez, M.J.2    Kaschabek, S.R.3    Reineke, W.4    Santero, E.5
  • 4
    • 0027250341 scopus 로고
    • Three different 2,3-Dihydroxybiphenyl-1,2-dioxygenase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rhodococcus globerulus P6
    • Asturias, J. A. & Timmis, K. N. (1993). Three different 2,3-Dihydroxybiphenyl-1,2-dioxygenase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rhodococcus globerulus P6. J Bacteriol 175, 4631-4640.
    • (1993) J. Bacteriol. , vol.175 , pp. 4631-4640
    • Asturias, J.A.1    Timmis, K.N.2
  • 5
    • 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
  • 6
    • 0035822094 scopus 로고    scopus 로고
    • Solving the riddle of the intradiol and extradiol catechol dioxygenases: How do enzymes control hydroperoxide rearrangements?
    • 2001
    • Bugg, T. D. H. & Lin, G. (2001). Solving the riddle of the intradiol and extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements? Chem Commun 2001, 941-952.
    • (2001) Chem. Commun. , pp. 941-952
    • Bugg, T.D.H.1    Lin, G.2
  • 7
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis, L. D. & Bolin, J. T. (1996). Evolutionary relationships among extradiol dioxygenases. J Bacteriol 178, 5930-5937.
    • (1996) J. Bacteriol. , vol.178 , pp. 5930-5937
    • Eltis, L.D.1    Bolin, J.T.2
  • 8
    • 0027509616 scopus 로고
    • Purification and crystallition of 2,3-dihydroxybiphenyl 1,2-dioxygenase
    • Eltis, L. D., Hofmann, B., Hecht, H. J., Lunsdorf, H. & Timmis, K. N. (1993). Purification and crystallition of 2,3-dihydroxybiphenyl 1,2-dioxygenase. J Biol Chem 268, 2727-2732.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2727-2732
    • Eltis, L.D.1    Hofmann, B.2    Hecht, H.J.3    Lunsdorf, H.4    Timmis, K.N.5
  • 9
    • 0029829834 scopus 로고    scopus 로고
    • Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae
    • Govantes, F., Molina-López, J. A. & Santero, E. (1996). Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae. J Bacteriol 178, 6817-6823.
    • (1996) J. Bacteriol. , vol.178 , pp. 6817-6823
    • Govantes, F.1    Molina-López, J.A.2    Santero, E.3
  • 10
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modeling
    • Guex, N. & Peitsh, M. C. (1997). SWISS-MODEL and the Swiss-Pdb viewer: an environment for comparative protein modeling. Electrophoresis 183, 2714-2723.
    • (1997) Electrophoresis , vol.183 , pp. 2714-2723
    • Guex, N.1    Peitsh, M.C.2
  • 11
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., Eltis, L. D., Timmis, K. N., Muchmore, S. W. & Bolin, J. T. (1995). Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 12
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 13
    • 0027442082 scopus 로고
    • Characterization of 2,2′,3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1
    • Happe, B., Eltis, L. D., Poth, H., Hedderich, R. & Timmis, K. N. (1993). Characterization of 2,2′,3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1. J Bacteriol 175, 7313-7320.
    • (1993) J. Bacteriol. , vol.175 , pp. 7313-7320
    • Happe, B.1    Eltis, L.D.2    Poth, H.3    Hedderich, R.4    Timmis, K.N.5
  • 14
    • 0024451702 scopus 로고
    • Bacterial aromatic ring-cleavage enzymes are classified into two different gene families
    • Harayama, S. & Rekik, M. (1989). Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J Biol Chem 264, 15328-15333.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15328-15333
    • Harayama, S.1    Rekik, M.2
  • 15
    • 0028840818 scopus 로고
    • Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalenesulfonate-degrading bacterium strain BN6
    • Heiss, G., Stolz, A., Kuhm, A. E, Müller, C., Klein, J., Altenbuchner, J. & Knackmuss, H.-J. (1995). Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalenesulfonate-degrading bacterium strain BN6. J Bacteriol 177, 5865-5871.
    • (1995) J. Bacteriol. , vol.177 , pp. 5865-5871
    • Heiss, G.1    Stolz, A.2    Kuhm, A.E.3    Müller, C.4    Klein, J.5    Altenbuchner, J.6    Knackmuss, H.-J.7
  • 16
    • 1842328640 scopus 로고    scopus 로고
    • Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad
    • Heiss, G., Müller, C., Altenbuchner, J. & Stolz, A. (1997). Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad. Microbiology 143, 1691-1699.
    • (1997) Microbiology , vol.143 , pp. 1691-1699
    • Heiss, G.1    Müller, C.2    Altenbuchner, J.3    Stolz, A.4
  • 17
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. & Pease, L. R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 0029056671 scopus 로고
    • Molecular and biochemical characterization of two meta-cleavage dioxygenases involved in biphenyl and m-xylene degradation by Beijerinckia sp. strain B1
    • Kim, E. & Zylstra, G. (1995). Molecular and biochemical characterization of two meta-cleavage dioxygenases involved in biphenyl and m-xylene degradation by Beijerinckia sp. strain B1. J Bacteriol 177, 3095-3103.
    • (1995) J. Bacteriol. , vol.177 , pp. 3095-3103
    • Kim, E.1    Zylstra, G.2
  • 19
    • 0025773011 scopus 로고
    • Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids
    • Kuhm, A. E., Stolz, A., Ngai, K. & Knackmuss, H. J. (1991). Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J Bacteriol 173, 3795-3802.
    • (1991) J. Bacteriol. , vol.173 , pp. 3795-3802
    • Kuhm, A.E.1    Stolz, A.2    Ngai, K.3    Knackmuss, H.J.4
  • 20
    • 0023613953 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotypic selection
    • Kunkel, T., Roberts, J. D. & Zakour, R. A. (1987). Rapid and efficient site-directed mutagenesis without phenotypic selection. Methods Enzymol 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.1    Roberts, J.D.2    Zakour, R.A.3
  • 21
    • 0000465301 scopus 로고
    • The nature of the defect in tyrosine metabolism in alkaptonuria
    • La Du, B. N., Zannoni, V. G., Laster, L. & Seegmiller, J. E. (1958). The nature of the defect in tyrosine metabolism in alkaptonuria. J Biol Chem 230, 251-260.
    • (1958) J. Biol. Chem. , vol.230 , pp. 251-260
    • La Du, B.N.1    Zannoni, V.G.2    Laster, L.3    Seegmiller, J.E.4
  • 22
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que, L. & Ho, R. Y. N. (1996). Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96, 2607-2624.
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que, L.1    Ho, R.Y.N.2
  • 23
    • 0024024251 scopus 로고
    • 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims
    • Schwarcz, R., Okuno, E., White, R. J., Bird, E. D. & Whetsell, W. O., Jr (1988). 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims. Proc Natl Acad Sci U S A 85, 4079-4081.
    • (1988) Proc. Natl. Acad. Sci. U S A , vol.85 , pp. 4079-4081
    • Schwarcz, R.1    Okuno, E.2    White, R.J.3    Bird, E.D.4    Whetsell W.O., Jr.5
  • 24
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
    • Senda, T., Sugiyama, K., Narita, H., Yamamoto, T., Kimbara, T., Fukuda, M., Sato, M., Yano, K. & Mitsui, Y. (1996). Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J Mol Biol 255, 735-752.
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, T.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 26
    • 0029038688 scopus 로고
    • X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism
    • Shu, L., Chiou, Y. M., Orville, A. M., Miller, M. A., Lipscomb, J. D. & Que, L. Jr (1995). X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry 24, 6649-6659.
    • (1995) Biochemistry , vol.24 , pp. 6649-6659
    • Shu, L.1    Chiou, Y.M.2    Orville, A.M.3    Miller, M.A.4    Lipscomb, J.D.5    Que L., Jr.6
  • 27
    • 0000208617 scopus 로고    scopus 로고
    • Geometric and electronic structure/function correlations in nonheme iron enzymes
    • & 7 other authors
    • Solomon, E. I., Brunold, T. C., Davis, M. I. & 7 other authors (2000). Geometric and electronic structure/function correlations in nonheme iron enzymes. Chem Rev 100, 235-350.
    • (2000) Chem. Rev. , vol.100 , pp. 235-350
    • Solomon, E.I.1    Brunold, T.C.2    Davis, M.I.3
  • 28
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
    • Sugimoto, K., Senda, T., Aoshima, H., Masai, E., Fukuda, M. & Mitsui, Y. (1999). Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure Fold Des 7, 953-965.
    • (1999) Structure Fold Des. , vol.7 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 29
    • 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. (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
  • 30
    • 0035114170 scopus 로고    scopus 로고
    • Crystal structure of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase
    • Uragami, Y., Senda, T., Sugimoto, K., Sato, N., Nagarajan, V., Masai, E., Fukuda, M. & Mitsui, Y. (2001). Crystal structure of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J Inorg Biochem 83, 269-279.
    • (2001) J. Inorg. Biochem. , vol.83 , pp. 269-279
    • Uragami, Y.1    Senda, T.2    Sugimoto, K.3    Sato, N.4    Nagarajan, V.5    Masai, E.6    Fukuda, M.7    Mitsui, Y.8
  • 31
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol
    • Vaillancourt, F. H., Han, S., Fortin, P. D., Bolin, J. T. & Eltis, L. D. (1998). Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. J Biol Chem 273, 34887-34895.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5
  • 32
    • 0037139492 scopus 로고    scopus 로고
    • Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography
    • Vaillancourt, F. H., Barbosa, C. J., Spiro, T. G., Bolin, J. T., Blades, M. W., Turner, R. F. & Eltis, L. D. (2002). Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography. J Am Chem Soc 124, 2485-2496.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2485-2496
    • Vaillancourt, F.H.1    Barbosa, C.J.2    Spiro, T.G.3    Bolin, J.T.4    Blades, M.W.5    Turner, R.F.6    Eltis, L.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.