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Volumn 64, Issue 12, 1998, Pages 4637-4642

Degradation of polychlorinated biphenyl metabolites by naphthalene- catabolizing enzymes

Author keywords

[No Author keywords available]

Indexed keywords

1,2 DIHYDRO 1,2 DIHYDROXYNAPHTHALENE DEHYDROGENASE; 2,3 DIHYDRO 2,3 DIHYDROXYBIPHENYL; 2,3 DIHYDROXYBIPHENYL; 3,4 BIPHENYLDIOL; 3,4 DIHYDRO 3,4 DIHYDROXY 2,2',5,5' TETRACHLOROBIPHENYL; 3,4 DIHYDRO 3,4 DIHYDROXYBIPHENYL; 3,4 DIHYDROXY 2,2',5,5' TETRACHLOROBIPHENYL; BACTERIAL ENZYME; NAPHTHALENE DERIVATIVE; OXIDOREDUCTASE; OXYGENASE; POLYCHLORINATED BIPHENYL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0031767768     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.12.4637-4642.1998     Document Type: Article
Times cited : (31)

References (33)
  • 1
    • 0021330498 scopus 로고
    • Suicide inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-halocatechols
    • Bartels, I., H.-J. Knackmuss, and W. Reineke. 1984. Suicide inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-halocatechols. Appl. Environ. Microbiol. 47:500-505.
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 500-505
    • Bartels, I.1    Knackmuss, H.-J.2    Reineke, W.3
  • 2
    • 0022522353 scopus 로고
    • Bacterial formation of humus-like materials from polychlorinated biphenyls (PCBs)
    • Baxter, R. M. 1986. Bacterial formation of humus-like materials from polychlorinated biphenyls (PCBs). Water Pollut. Res. Can. 21:1-7.
    • (1986) Water Pollut. Res. Can. , vol.21 , pp. 1-7
    • Baxter, R.M.1
  • 3
    • 0022621961 scopus 로고
    • Rapid assay for screening and characterizing microorganisms for the ability to degrade polychorinated biphenlys
    • Bedard, D. L., R. Unterman, L. H. Bopp, M. J. Brennan, M. L. Haberl, and C. Johnson. 1986. Rapid assay for screening and characterizing microorganisms for the ability to degrade polychorinated biphenlys. Appl. Environ. Microbiol. 51:761-768.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 761-768
    • Bedard, D.L.1    Unterman, R.2    Bopp, L.H.3    Brennan, M.J.4    Haberl, M.L.5    Johnson, C.6
  • 4
    • 0027386075 scopus 로고
    • Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: Complete DNA sequence of an upper naphthalene catabolic pathway
    • Denome, S. A., D. C. Stanley, E. S. Olson, and K. D. Young. 1993. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol. 175:6890-6901.
    • (1993) J. Bacteriol. , vol.175 , pp. 6890-6901
    • Denome, S.A.1    Stanley, D.C.2    Olson, E.S.3    Young, K.D.4
  • 5
    • 0015781618 scopus 로고
    • Transmissible plasmids coding early enzymes of naphthalene oxidation in Pseudomonas putida
    • Dunn, N. W., and I. C. Gunsalus. 1973. Transmissible plasmids coding early enzymes of naphthalene oxidation in Pseudomonas putida. J. Bacteriol. 114: 974-979.
    • (1973) J. Bacteriol. , vol.114 , pp. 974-979
    • Dunn, N.W.1    Gunsalus, I.C.2
  • 6
    • 0027509616 scopus 로고
    • Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase
    • Eltis, L. D., B. Hofmann, H. J. Hecht, H. Lunsdorf, and K. N. Timmis. 1993. Purification and crystallization 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
  • 7
    • 0027368828 scopus 로고
    • Enhanced biodegradation of polychlorinated biphenyl after site-directed mutagenesis of a biphenyl dioxygenase gene
    • Erickson, B. D., and F. J. Mondello. 1993. Enhanced biodegradation of polychlorinated biphenyl after site-directed mutagenesis of a biphenyl dioxygenase gene. Appl. Environ. Microbiol. 59:3858-3862.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3858-3862
    • Erickson, B.D.1    Mondello, F.J.2
  • 8
    • 0027223958 scopus 로고
    • Gene components responsible for discrete substrate specificity in the metabolism of biphenly (bph operon) and toluene (tod operon)
    • Furukawa, K., J. Hirose, A. Suyama, T. Zaiki, and S. Hayashida. 1993. Gene components responsible for discrete substrate specificity in the metabolism of biphenly (bph operon) and toluene (tod operon). J. Bacteriol. 175:5224-5232.
    • (1993) J. Bacteriol. , vol.175 , pp. 5224-5232
    • Furukawa, K.1    Hirose, J.2    Suyama, A.3    Zaiki, T.4    Hayashida, S.5
  • 9
    • 0017879297 scopus 로고
    • Effect of chlorine substitution on the biodegradability of polychlorinated biphenyls
    • Furukawa, K., K. Tonomura, and A. Kamibayashi. 1978. Effect of chlorine substitution on the biodegradability of polychlorinated biphenyls. Appl. Environ. Microbiol. 35:223-227.
    • (1978) Appl. Environ. Microbiol. , vol.35 , pp. 223-227
    • Furukawa, K.1    Tonomura, K.2    Kamibayashi, A.3
  • 10
    • 0028804381 scopus 로고
    • Dihydroxylation and dechlorination of chlorinated biphenyls by purified biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
    • Haddock, J. D., J. R. Horton, and D. T. Gibson. 1995. Dihydroxylation and dechlorination of chlorinated biphenyls by purified biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. J. Bacteriol. 177:20-26.
    • (1995) J. Bacteriol. , vol.177 , pp. 20-26
    • Haddock, J.D.1    Horton, J.R.2    Gibson, D.T.3
  • 11
    • 0025055440 scopus 로고
    • NAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • NAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Bacteriol. 172:457-464.
    • (1990) J. Bacteriol. , vol.172 , pp. 457-464
    • Haigler, B.1    Gibson, D.T.2
  • 12
    • 0024451702 scopus 로고
    • Bacterial aromatic ring-cleavage enzymes are classified into two different gene families
    • Harayama, S., and M. Rekik. 1989. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 264: 15238-15333.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15238-15333
    • Harayama, S.1    Rekik, M.2
  • 14
    • 0030870888 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase: Kinetic evidence for enol/keto tautomerization
    • Henderson, I. M. J., and T. D. H. Bugg. 1997. Pre-steady-state kinetic analysis of 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase: kinetic evidence for enol/keto tautomerization. Biochemistry 36:12252-12258.
    • (1997) Biochemistry , vol.36 , pp. 12252-12258
    • Henderson, I.M.J.1    Bugg, T.D.H.2
  • 15
    • 0029877462 scopus 로고    scopus 로고
    • Characterization of active recombinant His-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase
    • Hurtubise, Y., D. Barriault, and M. Sylvestre. 1996. Characterization of active recombinant His-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase. J. Biol. Chem. 271:8152-8156.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8152-8156
    • Hurtubise, Y.1    Barriault, D.2    Sylvestre, M.3
  • 16
    • 0028865344 scopus 로고
    • Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components
    • Hurtubise, Y., D. Barriault, J. Powlowski, and M. Sylvestre. 1995. Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components. J. Bacteriol. 177:6610-6618.
    • (1995) J. Bacteriol. , vol.177 , pp. 6610-6618
    • Hurtubise, Y.1    Barriault, D.2    Powlowski, J.3    Sylvestre, M.4
  • 17
    • 0030998438 scopus 로고    scopus 로고
    • Functional analysis of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally
    • Kimura, N., A. Nishi, M. Goto, and K. Furukawa. 1997. Functional analysis of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally. J. Bacteriol. 179:3936-3943.
    • (1997) J. Bacteriol. , vol.179 , pp. 3936-3943
    • Kimura, N.1    Nishi, A.2    Goto, M.3    Furukawa, K.4
  • 18
    • 0028327636 scopus 로고
    • Cloning and characterization of a chromosomal gene cluster, pah, that encodes the upper pathway for phenanthrene and naphthalene utilization by Pseudomonas putida OUS82
    • Kiyohara, H., S. Torigoe, N. Kaida, T. Asaki, T. Iida, H. Hayashi, and N. Takizawa. 1994. Cloning and characterization of a chromosomal gene cluster, pah, that encodes the upper pathway for phenanthrene and naphthalene utilization by Pseudomonas putida OUS82. J. Bacteriol. 176:2439-2443.
    • (1994) J. Bacteriol. , vol.176 , pp. 2439-2443
    • Kiyohara, H.1    Torigoe, S.2    Kaida, N.3    Asaki, T.4    Iida, T.5    Hayashi, H.6    Takizawa, N.7
  • 19
    • 0019457548 scopus 로고
    • Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
    • Klecka, G. M., and D. T. Gibson. 1981. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol. Appl. Environ. Microbiol. 41:1159-1165.
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 1159-1165
    • Klecka, G.M.1    Gibson, D.T.2
  • 20
    • 0025773011 scopus 로고
    • Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids
    • Kuhm, A. E., A. Stolz, K. L. Ngai, and H. J. Knackmuss. 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.L.3    Knackmuss, H.J.4
  • 21
    • 0024262983 scopus 로고
    • Cloning, nucleotide sequence and characterization of genes encoding naphthalene dioxygenase of Pseudomonas putida strain NCIB9816
    • Kurkela, S., H. Lehvaslaiho, E. T. Palva, and T. H. Teeri. 1988. Cloning, nucleotide sequence and characterization of genes encoding naphthalene dioxygenase of Pseudomonas putida strain NCIB9816. Gene 73:355-362.
    • (1988) Gene , vol.73 , pp. 355-362
    • Kurkela, S.1    Lehvaslaiho, H.2    Palva, E.T.3    Teeri, T.H.4
  • 22
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0030776495 scopus 로고    scopus 로고
    • Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase
    • Lam, W. W. Y., and T. D. H. Bugg. 1997. Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase. Biochemistry 36:12242-12251.
    • (1997) Biochemistry , vol.36 , pp. 12242-12251
    • Lam, W.W.Y.1    Bugg, T.D.H.2
  • 25
    • 0030743522 scopus 로고    scopus 로고
    • Microbial degradation of chloroaromatics: Use of the meta-cleavage pathway for mineralization of chlorobenzene
    • Mars, A. E., T. Kasberg, S. R. Kaschabek, M. H. Vanagteren, D. B. Janssen, and W. Reineke. 1997. Microbial degradation of chloroaromatics: use of the meta-cleavage pathway for mineralization of chlorobenzene. J. Bacteriol. 179:45311-1537.
    • (1997) J. Bacteriol. , vol.179 , pp. 45311-51537
    • Mars, A.E.1    Kasberg, T.2    Kaschabek, S.R.3    Vanagteren, M.H.4    Janssen, D.B.5    Reineke, W.6
  • 26
    • 0024495459 scopus 로고
    • A comprehensive chromatographic/mass spectrometric analysis of 4-chlorobiphenyl bacterial degradation products
    • Massé, R., F. Messier, C. Ayotte, M.-F. Lévesque, and M. Sylvestre. 1989. A comprehensive chromatographic/mass spectrometric analysis of 4-chlorobiphenyl bacterial degradation products. Biomed. Environ. Mass Spectr. 18: 27-47.
    • (1989) Biomed. Environ. Mass Spectr. , vol.18 , pp. 27-47
    • Massé, R.1    Messier, F.2    Ayotte, C.3    Lévesque, M.-F.4    Sylvestre, M.5
  • 27
    • 0030752851 scopus 로고    scopus 로고
    • Identification and modification of biphenyl dioxygenase sequences that determine the specificity of polychlorinated hiphenyl degradation
    • Mondello, F. J., M. P. Turcich, J. H. Lobos, and B. D. Erickson. 1997. Identification and modification of biphenyl dioxygenase sequences that determine the specificity of polychlorinated hiphenyl degradation. Appl. Environ. Microbiol. 63:3096-3103.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3096-3103
    • Mondello, F.J.1    Turcich, M.P.2    Lobos, J.H.3    Erickson, B.D.4
  • 29
    • 0017107475 scopus 로고
    • Bacterial cis-dihydrodiol dehydrogenases: Comparison of physicochemical and immunological properties
    • Patel, T. R., and D. T. Gibson. 1976. Bacterial cis-dihydrodiol dehydrogenases: comparison of physicochemical and immunological properties. J. Bacteriol. 128:842-850.
    • (1976) J. Bacteriol. , vol.128 , pp. 842-850
    • Patel, T.R.1    Gibson, D.T.2
  • 30
    • 0016140273 scopus 로고
    • Purification and properties of (+)-cis-naphthalene dihydrodiol dehydrogenase of Pseudomonas putida
    • Patel, T. R., and D. T. Gibson. 1974. Purification and properties of (+)-cis-naphthalene dihydrodiol dehydrogenase of Pseudomonas putida. J. Bacteriol. 119:879-888.
    • (1974) J. Bacteriol. , vol.119 , pp. 879-888
    • Patel, T.R.1    Gibson, D.T.2
  • 32
    • 0029785073 scopus 로고    scopus 로고
    • Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 sequence of the encoding gene (bphB)
    • Sylvestre, M., Y. Hurtubise, D. Barriault, J. Bergeron, and D. Ahmad. 1996. Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 sequence of the encoding gene (bphB). Appl. Environ. Microbiol. 62:2710-2715.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2710-2715
    • Sylvestre, M.1    Hurtubise, Y.2    Barriault, D.3    Bergeron, J.4    Ahmad, D.5
  • 33
    • 0024300820 scopus 로고
    • Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1
    • Taira, K., N. Hayase, N. Arimura, S. Yamashita, T. Miyazaki, and K. Furukawa. 1988. Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1. Biochemistry 27:3990-3996.
    • (1988) Biochemistry , vol.27 , pp. 3990-3996
    • Taira, K.1    Hayase, N.2    Arimura, N.3    Yamashita, S.4    Miyazaki, T.5    Furukawa, K.6


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