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Volumn 51, Issue 5, 1999, Pages 592-597

Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2- dioxygenase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BIPHENYL DERIVATIVE; NAPHTHALENE DERIVATIVE; OXYGENASE;

EID: 0033024795     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530051437     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 0032873363 scopus 로고    scopus 로고
    • Catalytic activity of Pseudomonas putida strain G7 naphthalene 1,2-dioxygenase on biphenyl
    • in press
    • Barriault D, Sylvestre M (1999) Catalytic activity of Pseudomonas putida strain G7 naphthalene 1,2-dioxygenase on biphenyl. Int Biodeterior Biodegrad (in press)
    • (1999) Int Biodeterior Biodegrad
    • Barriault, D.1    Sylvestre, M.2
  • 3
    • 0002557598 scopus 로고
    • Phthallate dioxygenase reductase and related flavin-iron-sulphur containing electron transferase
    • Müller F (ed) CRC, Boca Raton, Fla, pp
    • Batie CJ, Ballou DP, Correll CJ (1991) Phthallate dioxygenase reductase and related flavin-iron-sulphur containing electron transferase. In: Müller F (ed) Chemistry and biochemistry of flavoenzymes. CRC, Boca Raton, Fla, pp 544-554
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 544-554
    • Batie, C.J.1    Ballou, D.P.2    Correll, C.J.3
  • 4
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri A, Bermudez E, Raillard S, Stemmer WPC (1998) DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391: 288-291
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Bermudez, E.2    Raillard, S.3    Stemmer, W.P.C.4
  • 5
    • 0015781618 scopus 로고
    • Transmissible plasmids coding early enzymes of naphthalene oxidation in Pseudomonas putida
    • Dunn N, Gunsalus IC (1973) Transmissible plasmids coding early enzymes of naphthalene oxidation in Pseudomonas putida. J Bacteriol 144: 974-979
    • (1973) J Bacteriol , vol.144 , pp. 974-979
    • Dunn, N.1    Gunsalus, I.C.2
  • 6
    • 0020806085 scopus 로고
    • Naphthalene dioxygenase: Purification and properties of a terminal oxygenase component
    • Ensley BD, Gibson DT (1983) Naphthalene dioxygenase: purification and properties of a terminal oxygenase component. J Bacteriol 155: 505-511
    • (1983) J Bacteriol , vol.155 , pp. 505-511
    • Ensley, B.D.1    Gibson, D.T.2
  • 7
    • 0027223958 scopus 로고
    • Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bph operon) and toluene (tod operon)
    • Furukawa K, Hirose J, Suyama A, Zaiki T, Hayashida S (1993) Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (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
  • 8
    • 0028804381 scopus 로고
    • Dihydroxylation and dechlorination of chlorinated biphenyls by purified biphenyl 2,3-dioxygenase from Pseudomonas sp. Strain LB400
    • Haddock JD, Horton JR, Gibson DT (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
  • 9
    • 0025192274 scopus 로고
    • NAP, a component of naphthalene dioxygenase from Pseudomonas sp. Strain NCIB 9816
    • NAP, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J Bacteriol 172: 465-468
    • (1990) J Bacteriol , vol.172 , pp. 465-468
    • Haigler, B.E.1    Gibson, D.T.2
  • 10
    • 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.E.1    Gibson, D.T.2
  • 11
    • 0031959875 scopus 로고    scopus 로고
    • Biphenyl-associated meta-cleavage dioxygenases from Comamonas testosteroni strain B-356 involved in benzoate degradation
    • Hein P, Powlowski J, Barriault D, Hurtubise Y, Ahmad D, Sylvestre M (1998) Biphenyl-associated meta-cleavage dioxygenases from Comamonas testosteroni strain B-356 involved in benzoate degradation. Can J Microbiol 44: 42-49
    • (1998) Can J Microbiol , vol.44 , pp. 42-49
    • Hein, P.1    Powlowski, J.2    Barriault, D.3    Hurtubise, Y.4    Ahmad, D.5    Sylvestre, M.6
  • 12
    • 0028865344 scopus 로고
    • Purification and characterisation of the Comamonas testosteroni B-356 biphenyl dioxygenase components
    • Hurtubise Y, Barriault D, Powlowski J, Sylvestre M (1995) Purification and characterisation 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
  • 13
    • 0029877462 scopus 로고    scopus 로고
    • Characterisation of active recombinant His-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase
    • Hurtubise Y, Barriault D, Sylvestre M (1996) Characterisation 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
  • 14
    • 0031733410 scopus 로고    scopus 로고
    • Involvement of the terminal oxygenase β subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls
    • Hurtubise Y, Barriault D, Sylvestre M (1998) Involvement of the terminal oxygenase β subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls. J Bacteriol 180: 5828-5835
    • (1998) J Bacteriol , vol.180 , pp. 5828-5835
    • Hurtubise, Y.1    Barriault, D.2    Sylvestre, M.3
  • 16
    • 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, Torigoe S, Kaida N, Asaki T, Iida T, Hayashi H, Takizawa N (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
  • 17
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason JR, Cammack R (1992) The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu Rev Microbiol 46: 277-305
    • (1992) Annu Rev Microbiol , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 18
    • 0024429076 scopus 로고
    • Characterization of new bacterial transformation products of 1,1,1-trichloro-2,2,-bis-(4-chlorobiphenyl) ethane (DDT) by gas chromatography/mass spectrometry
    • Massé R, Lalanne D, Messier F, Sylvestre M (1989) Characterization of new bacterial transformation products of 1,1,1-trichloro-2,2,-bis-(4-chlorobiphenyl) ethane (DDT) by gas chromatography/mass spectrometry. Biomed Environ Mass Spectrom 18: 741-752
    • (1989) Biomed Environ Mass Spectrom , vol.18 , pp. 741-752
    • Massé, R.1    Lalanne, D.2    Messier, F.3    Sylvestre, M.4
  • 19
    • 0027164003 scopus 로고
    • NAH plasmid-mediated catabolism of anthracene and phenanthrene to naphthoic acids
    • Menn FM, Applegate BM, Sayler GS (1993) NAH plasmid-mediated catabolism of anthracene and phenanthrene to naphthoic acids. Appl Environ Microbiol 59: 1938-194
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1938-2194
    • Menn, F.M.1    Applegate, B.M.2    Sayler, G.S.3
  • 22
    • 0026134328 scopus 로고
    • Metabolism of hydroxybiphenyl and chloro-hydroxybiphenyl by biphenyl/ chlorobiphenyl degrading Pseudomonas testosteroni, strain B-356
    • Sondossi M, Sylvestre M, Ahmad D, Massé R (1991) Metabolism of hydroxybiphenyl and chloro-hydroxybiphenyl by biphenyl/ chlorobiphenyl degrading Pseudomonas testosteroni, strain B-356. J Ind Microbiol 7: 77-88
    • (1991) J Ind Microbiol , vol.7 , pp. 77-88
    • Sondossi, M.1    Sylvestre, M.2    Ahmad, D.3    Massé, R.4
  • 23
    • 0028110130 scopus 로고
    • DNA shaming by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer WPC (1994) DNA shaming by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc Natl Acad Sci USA 91: 10747-10751
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 24
    • 0019429534 scopus 로고
    • Purification and properties of NADH-ferredoxinTOL reductase. A component of toluene dioxygenase from Pseudomonas putida
    • Subramanian V, Liu TN, Yeh WK, Narro M, Gibson DT (1981) Purification and properties of NADH-ferredoxinTOL reductase. A component of toluene dioxygenase from Pseudomonas putida. J Biol Chem 256: 2723-2730
    • (1981) J Biol Chem , vol.256 , pp. 2723-2730
    • Subramanian, V.1    Liu, T.N.2    Yeh, W.K.3    Narro, M.4    Gibson, D.T.5
  • 25
    • 0029785073 scopus 로고    scopus 로고
    • Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding bphB gene
    • Sylvestre M, Hurtubise Y, Barriault D, Bergeron J, Ahmad D (1996a) Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding bphB gene. 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
  • 26
    • 0029845403 scopus 로고    scopus 로고
    • Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: Evolutionary relationships among gram-negative biphenyl dioxygenases
    • Sylvestre M, Sirois M, Hurtubise Y, Bergeron J, Ahmad D, Shareck F, Larose A, Barriault D, Guillemette I, Juteau JM (1996b) Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships among gram-negative biphenyl dioxygenases. Gene 174: 195-202
    • (1996) Gene , vol.174 , pp. 195-202
    • Sylvestre, M.1    Sirois, M.2    Hurtubise, Y.3    Bergeron, J.4    Ahmad, D.5    Shareck, F.6    Larose, A.7    Barriault, D.8    Guillemette, I.9    Juteau, J.M.10
  • 27
    • 0029920974 scopus 로고    scopus 로고
    • The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudomonas sp strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation
    • Werlen C, Kohler HPE, Meer JR van der (1996) The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudomonas sp strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation. J Biol Chem 271: 4009-4016
    • (1996) J Biol Chem , vol.271 , pp. 4009-4016
    • Werlen, C.1    Kohler, H.P.E.2    Van Der Meer, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.