메뉴 건너뛰기




Volumn 82, Issue 3, 1996, Pages 217-223

Cloning and characterization of extradiol aromatic ring-cleavage dioxygenases of Pseudomonas aeruginosa JI104

Author keywords

2,3 dihydroxy biphenyl; catechol; meta cleavage dioxygenase; substrate specificity

Indexed keywords

BACTERIAL ENZYME;

EID: 10244225248     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0922-338X(96)88811-8     Document Type: Article
Times cited : (26)

References (30)
  • 1
    • 0000976639 scopus 로고
    • Biochemistry of aromatic hydrocarbon degradation in Pseudomonas
    • Gunsalus, I. C., Sokatch, J. R., and Ornston, L. N. (ed.), Academic Press, New York
    • Dagley, S.: Biochemistry of aromatic hydrocarbon degradation in Pseudomonas, p. 527-556. In Gunsalus, I. C., Sokatch, J. R., and Ornston, L. N. (ed.), The bacteria, vol. 10. Academic Press, New York (1986).
    • (1986) The Bacteria , vol.10 , pp. 527-556
    • Dagley, S.1
  • 2
    • 0001792389 scopus 로고
    • Aerobic biodegradation of aromatic hydrocarbons by bacteria
    • Sigel, H. and Sigel, A. (ed.), Marcel Dekker Inc., New York
    • Harayama, S. and Timmis, K. N.: Aerobic biodegradation of aromatic hydrocarbons by bacteria, p. 99-156. In Sigel, H. and Sigel, A. (ed.), Metal ions in biological systems. Marcel Dekker Inc., New York (1992).
    • (1992) Metal Ions in Biological Systems , pp. 99-156
    • Harayama, S.1    Timmis, K.N.2
  • 3
    • 0024451702 scopus 로고
    • Bacterial aromatic ring-cleavage enzymes are classified into two different gene families
    • Harayama, S. and Rekik, M.: Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem., 264, 15328-15333 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 15328-15333
    • Harayama, S.1    Rekik, M.2
  • 4
    • 78651128288 scopus 로고
    • Metapyrocatechase: A new catechol-cleaving enzyme
    • Kojima, Y., Itada, N., and Hayaishi, O.: Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem., 236, 2223-2226 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 2223-2226
    • Kojima, Y.1    Itada, N.2    Hayaishi, O.3
  • 5
    • 0024806267 scopus 로고
    • Nucleotide sequence and expression of the catechol 2,3-dioxygenase-encoding gene of phenol-catabolizing Pseudomonas CF600
    • Bartilaon, M. and Shingler V.: Nucleotide sequence and expression of the catechol 2,3-dioxygenase-encoding gene of phenol-catabolizing Pseudomonas CF600. Gene, 85, 233-238 (1989).
    • (1989) Gene , vol.85 , pp. 233-238
    • Bartilaon, M.1    Shingler, V.2
  • 6
    • 0022617112 scopus 로고
    • Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes
    • Furukawa, K. and Miyazaki, T.: Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes. J. Bacteriol., 166, 392-398 (1986).
    • (1986) J. Bacteriol. , vol.166 , pp. 392-398
    • Furukawa, K.1    Miyazaki, T.2
  • 7
    • 0019456994 scopus 로고
    • Molecular cloning of TOL genes xylB and xylE in Escherichia coli
    • Inouye, S., Nakazawa, A., and Nakazawa, T.: Molecular cloning of TOL genes xylB and xylE in Escherichia coli. J. Bacteriol., 145, 1137-1143 (1981).
    • (1981) J. Bacteriol. , vol.145 , pp. 1137-1143
    • Inouye, S.1    Nakazawa, A.2    Nakazawa, T.3
  • 8
    • 0024427069 scopus 로고
    • Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli
    • Zylstra, G. J. and Gibson, D. T.: Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli. J. Biol. Chem., 264, 14940-14946 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 14940-14946
    • Zylstra, G.J.1    Gibson, D.T.2
  • 9
    • 0028329094 scopus 로고
    • Cloning of cmpE, a plasmid-borne catechol 2,3-dioxygenase-encoding gene from the aromatic- And chloroaromatic-degrading Pseudomonas sp. HV3
    • Yrjala, K., Paulin, L., Kilpi, S., and Romantschuk, M.: Cloning of cmpE, a plasmid-borne catechol 2,3-dioxygenase-encoding gene from the aromatic- and chloroaromatic-degrading Pseudomonas sp. HV3. Gene, 138, 119-121 (1994).
    • (1994) Gene , vol.138 , pp. 119-121
    • Yrjala, K.1    Paulin, L.2    Kilpi, S.3    Romantschuk, M.4
  • 11
    • 0024274467 scopus 로고
    • Isolation and characterization of a mixed culture that degrades polychlorinated biphenyls
    • Kimbara, K., Hashimoto, T., Fukuda, M., Koana, T., Takagi, M., Oishi, M., and Yano, K.: Isolation and characterization of a mixed culture that degrades polychlorinated biphenyls. Agric. Biol. Chem., 52, 2885-2891 (1988).
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 2885-2891
    • Kimbara, K.1    Hashimoto, T.2    Fukuda, M.3    Koana, T.4    Takagi, M.5    Oishi, M.6    Yano, K.7
  • 13
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J.: Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene, 33, 103-119 (1985).
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 14
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P. and Vogelstein, B.: A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem., 132, 6-13 (1983).
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 15
    • 0028270983 scopus 로고
    • Functional and structural relationship of various extradiol aromatic ring-cleavage dioxygenases of Pseudomonas origin
    • Hirose, J., Kimura, N., Suyama, A., Kobayashi, A., Hayashida, S., and Furukawa, K.: Functional and structural relationship of various extradiol aromatic ring-cleavage dioxygenases of Pseudomonas origin. FEMS Microbiol. Lett., 118, 273-277 (1994).
    • (1994) FEMS Microbiol. Lett. , vol.118 , pp. 273-277
    • Hirose, J.1    Kimura, N.2    Suyama, A.3    Kobayashi, A.4    Hayashida, S.5    Furukawa, K.6
  • 16
    • 0019769456 scopus 로고
    • Determination of nucleotide sequences in DNA
    • Sanger, F.: Determination of nucleotide sequences in DNA. Science, 214, 1205-1210 (1981).
    • (1981) Science , vol.214 , pp. 1205-1210
    • Sanger, F.1
  • 17
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing, J.: New M13 vectors for cloning. Methods Enzymol, 101, 20-78 (1983).
    • (1983) Methods Enzymol , vol.101 , pp. 20-78
    • Messing, J.1
  • 18
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-num-ber plasmid vectors for lacZ
    • Takeshita, S., Sato, M., Toba, M., Masahashi, W., and Hashimoto-Gotoh, T.: High-copy-number and low-copy-num- ber plasmid vectors for lacZ. Gene, 61, 63-74 (1987).
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 19
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2
    • Nakai, C., Kagamiyama, H., Nozaki, M., Nakazawa, T., Inouye, S., Ebina, Y., and Nakazawa, A.: Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2. J. Biol. Chem., 258, 2923-2928 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Ebina, Y.6    Nakazawa, A.7
  • 20
    • 0023120324 scopus 로고
    • Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes
    • Furukawa, K., Arimura, N., and Miyazaki, T.: Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes. J. Bacteriol., 169, 427-429 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 427-429
    • Furukawa, K.1    Arimura, N.2    Miyazaki, T.3
  • 21
    • 0024468821 scopus 로고
    • Molecular relationship of chromosomal genes encoding biphenyl/polychlorinated biphenyl catabolism: Some soil bacteria possess a highly conserved bph operon
    • Furukawa, K., Hayase, N., Taira, K., and Tomizuka, N.: Molecular relationship of chromosomal genes encoding biphenyl/polychlorinated biphenyl catabolism: some soil bacteria possess a highly conserved bph operon. J. Bacteriol., 171, 5467-5472 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 5467-5472
    • Furukawa, K.1    Hayase, N.2    Taira, K.3    Tomizuka, N.4
  • 22
    • 0025216788 scopus 로고
    • Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans
    • Harpel, M. R. and Lipscomb, J. D.: Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. J. Biol. Chem., 265, 6301-6311 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 6301-6311
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 23
    • 0022974415 scopus 로고
    • Naturally occurring TOL plasmids in Pseudomonas strains carry either two homologous or two nonhomologous catechol 2,3-oxygenase genes
    • Chatfield, L. K. and Williams, P. A.: Naturally occurring TOL plasmids in Pseudomonas strains carry either two homologous or two nonhomologous catechol 2,3-oxygenase genes. J. Bacteriol., 168, 878-885 (1986).
    • (1986) J. Bacteriol. , vol.168 , pp. 878-885
    • Chatfield, L.K.1    Williams, P.A.2
  • 24
    • 0021813884 scopus 로고
    • TOL plasmid pWW15 contains two nonhomologous, independently regulated catechol 2,3-oxygenase genes
    • Keil, H., Lebens, M. R., and Williams, P. A.: TOL plasmid pWW15 contains two nonhomologous, independently regulated catechol 2,3-oxygenase genes. J. Bacteriol., 163, 248-255 (1985).
    • (1985) J. Bacteriol. , vol.163 , pp. 248-255
    • Keil, H.1    Lebens, M.R.2    Williams, P.A.3
  • 25
    • 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. and Timmis, K. N.: 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).
    • (1993) J. Bacteriol. , vol.175 , pp. 4631-4640
    • Asturias, J.A.1    Timmis, K.N.2
  • 26
    • 0028797047 scopus 로고
    • Multiple genes encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase in the gram-positive polychlorinated biphenyl-degrading bacterium Rhodococcus erythropolis TA421, isolated from a termite ecosystem
    • Maeda, M., Chung, S. Y., Song, E., and Kudo, T.: Multiple genes encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase in the gram-positive polychlorinated biphenyl-degrading bacterium Rhodococcus erythropolis TA421, isolated from a termite ecosystem. Appl. Environ. Microbiol., 61, 549-555 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 549-555
    • Maeda, M.1    Chung, S.Y.2    Song, E.3    Kudo, T.4
  • 27
    • 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. KKS102
    • Senda, T., Sugiyama, K., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Sato, M., Yano, K., and Mitsui, Y.: Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. KKS102. J. Mol. Biol., 255, 735-752 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 28
    • 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., and Bolin, J. T.: Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science, 270, 976-980 (1995).
    • (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
  • 29
    • 0028672045 scopus 로고
    • The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas
    • Williams, P. A. and Sayers, J. R.: The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas. Biodegradation, 5, 195-217 (1994).
    • (1994) Biodegradation , vol.5 , pp. 195-217
    • Williams, P.A.1    Sayers, J.R.2
  • 30
    • 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.: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res., 22, 4673-4680 (1994).
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.