메뉴 건너뛰기




Volumn 67, Issue 1, 2003, Pages 36-45

Purification and Characterization of meta-Cleavage Compound Hydrolase from a Carbazole Degrader Pseudomonas resinovorans Strain CA10

Author keywords

Carbazole; Dibenzofuran; Meta cleavage compound hydrolase; Pseudomonas resinovorans strain CA10

Indexed keywords

2 HYDROXY 6 OXO 6 (2' AMINOPHENYL) HEXA 2,4 DIENOIC ACID HYDROLASE; 2-HYDROXY-6-OXO-6-(2'-AMINOPHENYL)-HEXA-2,4-DIENOIC ACID HYDROLASE; BACTERIAL DNA; CARBAZOLE DERIVATIVE; HYDROLASE;

EID: 0012484786     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.36     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 0020444957 scopus 로고
    • Carcinogenic effect of carbazole in the liver of (C57BL/6NxC3H/HeN)F1 mice
    • Tsuda, H., Hagiwara, A., Shibata, M., and Ito, N., Carcinogenic effect of carbazole in the liver of (C57BL/6NxC3H/HeN)F1 mice. J. Natl. Cancer Inst., 69, 1393-1398 (1982).
    • (1982) J. Natl. Cancer Inst. , vol.69 , pp. 1393-1398
    • Tsuda, H.1    Hagiwara, A.2    Shibata, M.3    Ito, N.4
  • 2
    • 0001878070 scopus 로고
    • Characterization of wood-preserving coal-tar creosote by gas-liquid chromatography
    • Nestler, F. H. M., Characterization of wood-preserving coal-tar creosote by gas-liquid chromatography. Anal. Chem., 46, 46-53 (1974).
    • (1974) Anal. Chem. , vol.46 , pp. 46-53
    • Nestler, F.H.M.1
  • 3
    • 0034084433 scopus 로고    scopus 로고
    • Bacterial metabolism of fluorene, dibenzofuran, diben-zothiophene, and carbazole
    • Bressler, D. C., and Fedorak, P. M., Bacterial metabolism of fluorene, dibenzofuran, diben-zothiophene, and carbazole. Can. J. Microbiol., 46, 397-409 (2000).
    • (2000) Can. J. Microbiol. , vol.46 , pp. 397-409
    • Bressler, D.C.1    Fedorak, P.M.2
  • 4
    • 0035729093 scopus 로고    scopus 로고
    • Bacterial degradation of aromatic compounds via angular dioxygenation
    • Nojiri, H., Habe, H., and Omori, T., Bacterial degradation of aromatic compounds via angular dioxygenation. J. Gen. Appl. Microbiol., 47, 279-305 (2001).
    • (2001) J. Gen. Appl. Microbiol. , vol.47 , pp. 279-305
    • Nojiri, H.1    Habe, H.2    Omori, T.3
  • 5
    • 0000843661 scopus 로고    scopus 로고
    • Molecular bases of aerobic bacterial degradation of dioxins: Involvement of angular dioxygenation
    • Nojiri, H., and Omori, T., Molecular bases of aerobic bacterial degradation of dioxins: involvement of angular dioxygenation. Biosci. Biotechnol. Biochem., 66, 2001-2016 (2002).
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2001-2016
    • Nojiri, H.1    Omori, T.2
  • 7
    • 0030744612 scopus 로고    scopus 로고
    • Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. Strain CA10
    • Sato, S., Nam, J.-W., Kasuga, K., Nojiri, H., Yamane, H., and Omori, T., Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J. Bac-teriol., 179, 4850-4858 (1997).
    • (1997) J. Bac-Teriol. , vol.179 , pp. 4850-4858
    • Sato, S.1    Nam, J.-W.2    Kasuga, K.3    Nojiri, H.4    Yamane, H.5    Omori, T.6
  • 8
    • 0030855128 scopus 로고    scopus 로고
    • Cloning of genes involved in carbazole degradation of Pseudomonas sp. Strain CA10: Nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase
    • Sato, S., Ouchiyama, N., Kimura, T., Nojiri, H., Yamane, H., and Omori, T., Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase. J. Bacteriol., 179, 4841-4849 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 4841-4849
    • Sato, S.1    Ouchiyama, N.2    Kimura, T.3    Nojiri, H.4    Yamane, H.5    Omori, T.6
  • 9
    • 0034981075 scopus 로고    scopus 로고
    • Genetic characterization and evolutionary implications of a car gene cluster in the carbazole-degrader, Pseudomonas sp. Strain CA10
    • Nojiri, H., Sekiguchi, H., Maeda, K., Urata, M., Nakai, S., Yoshida, T., Habe, H., and Omori, T., Genetic characterization and evolutionary implications of a car gene cluster in the carbazole-degrader, Pseudomonas sp. strain CA10. J. Bacteriol., 183, 3663-3679 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 3663-3679
    • Nojiri, H.1    Sekiguchi, H.2    Maeda, K.3    Urata, M.4    Nakai, S.5    Yoshida, T.6    Habe, H.7    Omori, T.8
  • 10
    • 0029045738 scopus 로고
    • 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudonomas putida 86
    • Rosche, B., Tshisuaka, B., Fetzner, S., and Lingens, F., 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudonomas putida 86. J. Biol. Chem., 270, 17836-17842 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17836-17842
    • Rosche, B.1    Tshisuaka, B.2    Fetzner, S.3    Lingens, F.4
  • 11
    • 0035257614 scopus 로고    scopus 로고
    • New classification system for oxygenase components involved in ring-hydroxylating oxygenations
    • Nam, J.-W., Nojiri, H., Yoshida, T., Habe, H., Yamane, H., and Omori, T., New classification system for oxygenase components involved in ring-hydroxylating oxygenations. Biosci. Biotechnol. Biochem., 65, 254-263 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 254-263
    • Nam, J.-W.1    Nojiri, H.2    Yoshida, T.3    Habe, H.4    Yamane, H.5    Omori, T.6
  • 12
    • 0031804925 scopus 로고    scopus 로고
    • Degradation of dioxin-like compounds by microorganisms
    • Wittich, R.-M., Degradation of dioxin-like compounds by microorganisms. Appl. Microbiol. Biotechnol., 49, 489-499 (1998).
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 489-499
    • Wittich, R.-M.1
  • 13
    • 0032940805 scopus 로고    scopus 로고
    • Diverse oxygenations catalyzed by carba-zole 1,9a-dioxygenase from Pseudomonas sp. Strain CA10
    • Nojiri, H., Nam, J.-W., Kosaka, M., Morii, K., Takemura, T., Furihata, K., Yamane, H., and Omori, T., Diverse oxygenations catalyzed by carba-zole 1,9a-dioxygenase from Pseudomonas sp. strain CA10. J. Bacteriol., 181, 3105-3113 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 3105-3113
    • Nojiri, H.1    Nam, J.-W.2    Kosaka, M.3    Morii, K.4    Takemura, T.5    Furihata, K.6    Yamane, H.7    Omori, T.8
  • 14
    • 0035432248 scopus 로고    scopus 로고
    • Degradation of chlorinated dibenzofurans and dibenzo-p-dioxins by two types of bacteria having angular dioxygenase with different features
    • Habe, H., Chung, J.-S., Lee, J.-H., Kasuga, K., Yoshida, T., Nojiri, H., and Omori, T., Degradation of chlorinated dibenzofurans and dibenzo-p-dioxins by two types of bacteria having angular dioxygenase with different features. Appl. Environ. Microbiol., 67, 3610-3617 (2001).
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3610-3617
    • Habe, H.1    Chung, J.-S.2    Lee, J.-H.3    Kasuga, K.4    Yoshida, T.5    Nojiri, H.6    Omori, T.7
  • 15
    • 0018306487 scopus 로고
    • Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls
    • Furukawa, K., Tomozuka, N., and Kamibayashi, A., Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls. Appl. Environ. Microbiol., 38, 301-310 (1979).
    • (1979) Appl. Environ. Microbiol. , vol.38 , pp. 301-310
    • Furukawa, K.1    Tomozuka, N.2    Kamibayashi, A.3
  • 16
    • 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., and Hayashida, S., Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bph operon) and toluene (tod operon). J. Bacteriol., 175, 5224-5232 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 5224-5232
    • Furukawa, K.1    Hirose, J.2    Suyama, A.3    Zaiki, T.4    Hayashida, S.5
  • 17
    • 0030000836 scopus 로고    scopus 로고
    • Analysis of cumene (Isopropylbenzene) degradation genes from Pseudomonas fluorescens IP01
    • Habe, H., Kasuga, K., Nojiri, H., Yamane, H., and Omori, T., Analysis of cumene (isopropylbenzene) degradation genes from Pseudomonas fluorescens IP01. Appl. Environ. Microbiol., 62, 4471-4477 (1996).
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4471-4477
    • Habe, H.1    Kasuga, K.2    Nojiri, H.3    Yamane, H.4    Omori, T.5
  • 18
    • 0032483324 scopus 로고    scopus 로고
    • Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls
    • Seah, S. Y. K., Terracina, G., Bolin, J. T., Riebel, P., Snieckus, V., and Eltis, L. D., Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls. J. Biol. Chem., 237, 22943-22949 (1998).
    • (1998) J. Biol. Chem. , vol.237 , pp. 22943-22949
    • Seah, S.Y.K.1    Terracina, G.2    Bolin, J.T.3    Riebel, P.4    Snieckus, V.5    Eltis, L.D.6
  • 19
    • 0034717267 scopus 로고    scopus 로고
    • Identification of a serine hydrolase as a key determinant in the microbial degradation of polychlorinated biphenyls
    • Seah, S. Y. K., Labbe, G., Nerdinger, S., Johnson, M. R., Snieckus, V., and Eltis, L. D., Identification of a serine hydrolase as a key determinant in the microbial degradation of polychlorinated biphenyls. J. Biol. Chem., 275, 15701-15708 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 15701-15708
    • Seah, S.Y.K.1    Labbe, G.2    Nerdinger, S.3    Johnson, M.R.4    Snieckus, V.5    Eltis, L.D.6
  • 20
    • 0034520920 scopus 로고    scopus 로고
    • Toluene degradation pathway from Pseudomonas putida F1: Substrate specificity and gene induction by 1-substituted benzenes
    • Cho, M. C., Kang, D. O., Yoon, B. D., and Lee, K., Toluene degradation pathway from Pseudomonas putida F1: substrate specificity and gene induction by 1-substituted benzenes. J. Ind. Microbiol. Biotechnol., 25, 163-170 (2000).
    • (2000) J. Ind. Microbiol. Biotechnol. , vol.25 , pp. 163-170
    • Cho, M.C.1    Kang, D.O.2    Yoon, B.D.3    Lee, K.4
  • 22
    • 0033807114 scopus 로고    scopus 로고
    • Identification of a serine hydrolase which cleaves the alicyclic ring of tetralin
    • Hernaez, M. J., Andujar, E., Rios, J. L., Kaschabek, S. R., Reinke, W., and Santero, E., Identification of a serine hydrolase which cleaves the alicyclic ring of tetralin. J. Bacteriol., 182, 5448-5453 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 5448-5453
    • Hernaez, M.J.1    Ujar, E.2    Rios, J.L.3    Kaschabek, S.R.4    Reinke, W.5    Santero, E.6
  • 23
    • 0036400672 scopus 로고    scopus 로고
    • Isolation and characterization of Sphingomonas sp. GTIN11 capable of carbazole metabolism in petroleum
    • Kilbane, J. J., Daram, A., Abbasian J., and Kayser, K. J., Isolation and characterization of Sphingomonas sp. GTIN11 capable of carbazole metabolism in petroleum. Biochem. Biophys. Res. Commun., 297, 242-248 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 242-248
    • Kilbane, J.J.1    Daram, A.2    Abbasian, J.3    Kayser, K.J.4
  • 24
    • 0027137639 scopus 로고
    • Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. Strain RW1
    • Bunz, P. V., Falchetto, R., and Cook, A. M., Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1. Biodegradation, 4, 171-178 (1993).
    • (1993) Biodegradation , vol.4 , pp. 171-178
    • Bunz, P.V.1    Falchetto, R.2    Cook, A.M.3
  • 25
    • 0031859323 scopus 로고    scopus 로고
    • Genetic analysis of dioxin dioxygenase of Sphingo-monas sp. Strain RW1: Catabolic genes dispersed on the genome
    • Armengaud, J., Happe, B., and Timmis, K. N., Genetic analysis of dioxin dioxygenase of Sphingo-monas sp. strain RW1: catabolic genes dispersed on the genome. J. Bacteriol., 180, 3954-3966 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 3954-3966
    • Armengaud, J.1    Happe, B.2    Timmis, K.N.3
  • 26
    • 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
  • 27
    • 0030000545 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and characterization of the genes encoding the enzymes involved in the degradation of cumene to 2-hydroxy-6-oxo-7-methylocta-2,4-dienoic acid in Pseudomonas fluorescens IP01
    • Aoki, H., Kimura, H., Habe, H., Yamane, H., Kodama, T., and Omori, T., Cloning, nucleotide sequence and characterization of the genes encoding the enzymes involved in the degradation of cumene to 2-hydroxy-6-oxo-7-methylocta-2,4-dienoic acid in Pseudomonas fluorescens IP01. J. Ferment. Bioeng., 81, 187-196 (1996).
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 187-196
    • Aoki, H.1    Kimura, H.2    Habe, H.3    Yamane, H.4    Kodama, T.5    Omori, T.6
  • 29
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res., 7, 1513-1523 (1979).
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 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., 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).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0023114367 scopus 로고
    • Purification and properties of 2,3-dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene
    • Furukawa, K., and Arimura, N., Purification and properties of 2,3-dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene. J. Bacteriol., 169, 924-927 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 924-927
    • Furukawa, K.1    Arimura, N.2
  • 33
    • 0027250341 scopus 로고
    • Three different 2,3-dihydroxybiphenyl-1,2-dioxygenase genes in the Gram-positive polychlorobiphenyl-degrading bacterium Rhodococcus globerulus P6
    • Astrias, J., 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
    • Astrias, J.1    Timmis, K.N.2
  • 34
    • 0015219756 scopus 로고
    • The meta cleavage of catechol by Azotobacter species: 4-ox-alocrotonate pathway
    • Sala-Trepat, J. M., and Evans, W. C., The meta cleavage of catechol by Azotobacter species: 4-ox-alocrotonate pathway. Eur. J. Biochem., 20, 400-413 (1971).
    • (1971) Eur. J. Biochem. , vol.20 , pp. 400-413
    • Sala-Trepat, J.M.1    Evans, W.C.2
  • 36
    • 85010517505 scopus 로고    scopus 로고
    • Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10
    • press
    • Iwata, K., Nojiri, H., Shimizu, K., Yoshida, T., Habe, H., and Omori, T., Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10. Biosci. Biotechnol. Biochem., in press.
    • Biosci. Biotechnol. Biochem
    • Iwata, K.1    Nojiri, H.2    Shimizu, K.3    Yoshida, T.4    Habe, H.5    Omori, T.6
  • 38
    • 84961980743 scopus 로고
    • Cosmo: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt, A., and Schuumann, G., Cosmo: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient. J. Chem. Soc. Perkin Transactions, 2, 799-805 (1993).
    • (1993) J. Chem. Soc. Perkin Transactions , vol.2 , pp. 799-805
    • Klamt, A.1    Schuumann, G.2
  • 39
    • 84988122931 scopus 로고
    • An algorithm for the location of transition states
    • Baker, J., An algorithm for the location of transition states. J. Comp. Chem., 7, 385 (1986).
    • (1986) J. Comp. Chem. , vol.7 , pp. 385
    • Baker, J.1
  • 40
    • 0027400542 scopus 로고
    • Metabolism of 2,2?-dihydroxybiphenyl by Pseudomonas sp. Strain HBP1: Production and consumption of 2,2',3-trihydroxybiphenyl
    • Kohler, H.-P. E., Schmid, A., and van der Maarel, M., Metabolism of 2,2?-dihydroxybiphenyl by Pseudomonas sp. Strain HBP1: production and consumption of 2,2',3-trihydroxybiphenyl. J. Bacteriol., 175, 1621-1628 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 1621-1628
    • Kohler, H.-P.E.1    Schmid, A.2    Van Der Maarel, M.3
  • 41
    • 0034673180 scopus 로고    scopus 로고
    • Catalytic mechanism of a C-C hydrolase enzyme: Evidence for a gem-diol intermediate, not an acyl enzyme
    • Fleming, S. M., Robertson, T. A., Langley, G. J., and Bugg, T. D. H., Catalytic mechanism of a C-C hydrolase enzyme: evidence for a gem-diol intermediate, not an acyl enzyme. Biochemistry, 39, 1522-1531 (2000).
    • (2000) Biochemistry , vol.39 , pp. 1522-1531
    • Fleming, S.M.1    Robertson, T.A.2    Langley, G.J.3    Bugg, T.D.H.4
  • 42
    • 0000641673 scopus 로고
    • Ordering of wave functions and eigenenergies to the individual electrons of an atom
    • Koopmans, T., Ordering of wave functions and eigenenergies to the individual electrons of an atom. Physica, 1, 104-113 (1933).
    • (1933) Physica , vol.1 , pp. 104-113
    • Koopmans, T.1
  • 43
    • 0346948866 scopus 로고
    • Role of frontier orbitals in chemical-reac-tion
    • Fukui, K., Role of frontier orbitals in chemical-reac-tion. Science, 218, 747-754 (1982).
    • (1982) Science , vol.218 , pp. 747-754
    • Fukui, K.1
  • 44
    • 0035933281 scopus 로고    scopus 로고
    • Crystal structure of 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (BphD enzyme) from the Rhodococcus sp. Strain RHA1 of the PCB degradation pathway
    • Nandhagopal, N., Yamada, A., Hatta, T., Masai, E., Fukuda, M., Mitsui, Y., and Senda, T., Crystal structure of 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (BphD enzyme) from the Rhodococcus sp. Strain RHA1 of the PCB degradation pathway. J. Mol. Biol., 309, 1139-1151 (2001).
    • (2001) J. Mol. Biol. , vol.309 , pp. 1139-1151
    • Nandhagopal, N.1    Yamada, A.2    Hatta, T.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6    Senda, T.7
  • 45
    • 0036308433 scopus 로고    scopus 로고
    • Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IP01
    • Saku, T., Fushinobu, S., Jun, S.-Y., Ikeda, N., Nojiri, H., Yamane, H., Omori, T., and Wakagi, T., Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IP01. J. Biosci. Bioeng., 93, 568-574 (2002).
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 568-574
    • Saku, T.1    Fushinobu, S.2    Jun, S.-Y.3    Ikeda, N.4    Nojiri, H.5    Yamane, H.6    Omori, T.7    Wakagi, T.8
  • 46
    • 0036708001 scopus 로고    scopus 로고
    • Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products
    • Fushinobu, S., Saku, T., Hidaka, M., Jun, S.-Y., Nojiri, H., Yamane, H., Shoun, H., Omori, T., and Wakagi, T., Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products. Protein Sci., 11, 2184-2195 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2184-2195
    • Fushinobu, S.1    Saku, T.2    Hidaka, M.3    Jun, S.-Y.4    Nojiri, H.5    Yamane, H.6    Shoun, H.7    Omori, T.8    Wakagi, T.9
  • 47
    • 84998386234 scopus 로고
    • Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOP-DA) reducing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl
    • Omori, T., Sugimura, K., Ishigooka, H., and Minoda, Y., Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOP-DA) reducing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl. Agric. Biol. Chem., 50, 931-937 (1986).
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 931-937
    • Omori, T.1    Sugimura, K.2    Ishigooka, H.3    Minoda, Y.4
  • 48
    • 0017807931 scopus 로고
    • Purification and properties of 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase from two strains of Pseudomonas putida
    • Bayly, R. C., and Berardino, D. D., Purification and properties of 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase from two strains of Pseudomonas putida. J. Bacteriol., 134, 30-37 (1978).
    • (1978) J. Bacteriol. , vol.134 , pp. 30-37
    • Bayly, R.C.1    Berardino, D.D.2
  • 49
    • 0022507290 scopus 로고
    • Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydroalse) encoded by the TOL plasmid pWW0 from Pseudomonasputida mt-2
    • Duggleby, C. J., and Williams, P. A., Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydroalse) encoded by the TOL plasmid pWW0 from Pseudomonasputida mt-2. J. Gen. Microbiol., 132, 717-726 (1986).
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 717-726
    • Duggleby, C.J.1    Williams, P.A.2
  • 50
    • 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 Bugg, T. D. H., 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).
    • (1997) Biochemistry , vol.36 , pp. 12242-12251
    • Lam, W.W.Y.1    Bugg, T.D.H.2
  • 51
    • 0031284266 scopus 로고    scopus 로고
    • Cloning and characterization of the genes involved in the degradation of dibenzofuran by Terrabacter sp. Strain DBF63
    • Kasuga, K., Nojiri, H., Yamane, H., Kodama, T., and Omori, T., Cloning and characterization of the genes involved in the degradation of dibenzofuran by Terrabacter sp. Strain DBF63. J. Ferment. Bioeng., 84, 387-399 (1997).
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 387-399
    • Kasuga, K.1    Nojiri, H.2    Yamane, H.3    Kodama, T.4    Omori, T.5
  • 52
    • 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., and Timmis, K. N., 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).
    • (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
  • 53
    • 0026082007 scopus 로고
    • 3-(2-Hydroxyphenyl)catechol as substrate for proximal meta ring cleavage in diben-zofuran degradation by Brevibacterium sp. Strain DPO 1361
    • Strubel, V., Engesser, K. H., Fischer, P., and Knackmuss, H.-J., 3-(2-Hydroxyphenyl)catechol as substrate for proximal meta ring cleavage in diben-zofuran degradation by Brevibacterium sp. Strain DPO 1361. J. Bacteriol., 173, 1932-1937 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 1932-1937
    • Strubel, V.1    Engesser, K.H.2    Fischer, P.3    Knackmuss, H.-J.4
  • 54
    • 0030053413 scopus 로고    scopus 로고
    • Carba-zole degradation by Pseudomonas sp. LD2: Metabolic characteristics and the identification of some metabolites
    • Gieg, L. M., Otter, A., and Fedorak, P. M., Carba-zole degradation by Pseudomonas sp. LD2: metabolic characteristics and the identification of some metabolites. Environ. Sci. Technol., 30, 575-585 (1996).
    • (1996) Environ. Sci. Technol. , vol.30 , pp. 575-585
    • Gieg, L.M.1    Otter, A.2    Fedorak, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.