메뉴 건너뛰기




Volumn 131, Issue , 2013, Pages 420-428

Catabolism of 4-alkylphenols by Acinetobacter sp. OP5: Genetic organization of the oph gene cluster and characterization of alkylcatechol 2, 3-dioxygenase

Author keywords

Alkylcatechol 2, 3 dioxygenase; Alkylphenol; Phenol hydroxygenase

Indexed keywords

CLONING; PHENOLS;

EID: 84873194766     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2012.12.086     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0031733597 scopus 로고    scopus 로고
    • Adaptation of Comamonas testosteroni TA441 to utilize phenol: organization and regulation of the genes involved in phenol degradation
    • Arai H., Akahira S., Ohishi T., Maeda M., Kudo T. Adaptation of Comamonas testosteroni TA441 to utilize phenol: organization and regulation of the genes involved in phenol degradation. Microbiology 1998, 144(Pt 10):2895-2903.
    • (1998) Microbiology , vol.144 , Issue.PART 10 , pp. 2895-2903
    • Arai, H.1    Akahira, S.2    Ohishi, T.3    Maeda, M.4    Kudo, T.5
  • 3
    • 0028033313 scopus 로고
    • Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth
    • Cerdan P., Wasserfallen A., Rekik M., Timmis K.N., Harayama S. Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth. J. Bacteriol. 1994, 176(19):6074-6081.
    • (1994) J. Bacteriol. , vol.176 , Issue.19 , pp. 6074-6081
    • Cerdan, P.1    Wasserfallen, A.2    Rekik, M.3    Timmis, K.N.4    Harayama, S.5
  • 4
    • 71749087321 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the extradiol dioxygenase LapB from a long-chain alkylphenol degradation pathway in Pseudomonas
    • Cho J.H., Jung D.K., Lee K., Rhee S. Crystal structure and functional analysis of the extradiol dioxygenase LapB from a long-chain alkylphenol degradation pathway in Pseudomonas. J. Biol. Chem. 2009, 284(49):34321-34330.
    • (2009) J. Biol. Chem. , vol.284 , Issue.49 , pp. 34321-34330
    • Cho, J.H.1    Jung, D.K.2    Lee, K.3    Rhee, S.4
  • 5
    • 0022507290 scopus 로고
    • Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoa te hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonus putida mt-2
    • Duggleby C.J., William P.A. Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoa te hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonus putida mt-2. J. Gen. Microbiol. 1986, 132:717-726.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 717-726
    • Duggleby, C.J.1    William, P.A.2
  • 6
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis L.D., Bolin J.T. Evolutionary relationships among extradiol dioxygenases. J. Bacteriol. 1996, 178(20):5930-5937.
    • (1996) J. Bacteriol. , vol.178 , Issue.20 , pp. 5930-5937
    • Eltis, L.D.1    Bolin, J.T.2
  • 7
    • 0020612907 scopus 로고
    • Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo
    • Ensley B.D., Ratzkin B.J., Osslund T.D., Simon M.J., Wackett L.P., Gibson D.T. Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo. Science 1983, 222(4620):167-169.
    • (1983) Science , vol.222 , Issue.4620 , pp. 167-169
    • Ensley, B.D.1    Ratzkin, B.J.2    Osslund, T.D.3    Simon, M.J.4    Wackett, L.P.5    Gibson, D.T.6
  • 8
    • 0035417245 scopus 로고    scopus 로고
    • Alkylphenolic compounds in edible molluscs of the Adriatic Sea (Italy)
    • Ferrara F., Fabietti F., Delise M., Bocca A.P., Funari E. Alkylphenolic compounds in edible molluscs of the Adriatic Sea (Italy). Environ. Sci. Technol. 2001, 35(15):3109-3112.
    • (2001) Environ. Sci. Technol. , vol.35 , Issue.15 , pp. 3109-3112
    • Ferrara, F.1    Fabietti, F.2    Delise, M.3    Bocca, A.P.4    Funari, E.5
  • 9
    • 0035073290 scopus 로고    scopus 로고
    • Sphingomonas cloacae sp. nov., a nonylphenol-degrading bacterium isolated from wastewater of a sewage-treatment plant in Tokyo
    • Fujii K., Urano N., Ushio H., Satomi M., Kimura S. Sphingomonas cloacae sp. nov., a nonylphenol-degrading bacterium isolated from wastewater of a sewage-treatment plant in Tokyo. Int. J. Syst. Evol. Microbiol. 2001, 51(Pt 2):603-610.
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , Issue.PART 2 , pp. 603-610
    • Fujii, K.1    Urano, N.2    Ushio, H.3    Satomi, M.4    Kimura, S.5
  • 10
    • 15444369429 scopus 로고    scopus 로고
    • Differential degradation of nonylphenol isomers by Sphingomonas xenophaga Bayram
    • Gabriel F.L., Giger W., Guenther K., Kohler H.P. Differential degradation of nonylphenol isomers by Sphingomonas xenophaga Bayram. Appl. Environ. Microbiol. 2005, 71(3):1123-1129.
    • (2005) Appl. Environ. Microbiol. , vol.71 , Issue.3 , pp. 1123-1129
    • Gabriel, F.L.1    Giger, W.2    Guenther, K.3    Kohler, H.P.4
  • 11
    • 0344875042 scopus 로고    scopus 로고
    • 3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenase
    • Jeong J.J., Kim J.H., Kim C.K., Hwang I., Lee K. 3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenase. Microbiology 2003, 149(Pt 11):3265-3277.
    • (2003) Microbiology , vol.149 , Issue.PART 11 , pp. 3265-3277
    • Jeong, J.J.1    Kim, J.H.2    Kim, C.K.3    Hwang, I.4    Lee, K.5
  • 12
    • 0000225313 scopus 로고
    • Similarity Analyses of rRNAs
    • American Society for Microbiology, Washington, DC, R.G.E. Murray, W.A. Wood, N.R. Krieg, P. Gerhardt (Eds.)
    • Johnson J. Similarity Analyses of rRNAs. Methods for General and Molecular Bacteriology 1994, 683-700. American Society for Microbiology, Washington, DC. R.G.E. Murray, W.A. Wood, N.R. Krieg, P. Gerhardt (Eds.).
    • (1994) Methods for General and Molecular Bacteriology , pp. 683-700
    • Johnson, J.1
  • 13
    • 58549086167 scopus 로고    scopus 로고
    • Acetylation of fluoroquinolone antimicrobial agents by an Escherichia coli strain isolated from a municipal wastewater treatment plant
    • Jung C.M., Heinze T.M., Strakosha R., Elkins C.A., Sutherland J.B. Acetylation of fluoroquinolone antimicrobial agents by an Escherichia coli strain isolated from a municipal wastewater treatment plant. J. Appl. Microbiol. 2009, 106(2):564-571.
    • (2009) J. Appl. Microbiol. , vol.106 , Issue.2 , pp. 564-571
    • Jung, C.M.1    Heinze, T.M.2    Strakosha, R.3    Elkins, C.A.4    Sutherland, J.B.5
  • 14
    • 10644234814 scopus 로고    scopus 로고
    • Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17
    • Kim D., Chae J.C., Jang J.Y., Zylstra G.J., Kim Y.M., Kang B.S., Kim E. Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17. Biochem. Biophys. Res. Commun. 2005, 326(4):880-886.
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , Issue.4 , pp. 880-886
    • Kim, D.1    Chae, J.C.2    Jang, J.Y.3    Zylstra, G.J.4    Kim, Y.M.5    Kang, B.S.6    Kim, E.7
  • 15
    • 3042988645 scopus 로고    scopus 로고
    • Characteristics of catechol 2,3-dioxygenase produced by 4-chlorobenzoate-degrading Pseudomonas sp.S-47
    • Kim K.P., Seo D.I., Min K.H., Ka J.O., Park Y.K., Kim C.K. Characteristics of catechol 2,3-dioxygenase produced by 4-chlorobenzoate-degrading Pseudomonas sp.S-47. J. Microbiol. 1997, 35:295-299.
    • (1997) J. Microbiol. , vol.35 , pp. 295-299
    • Kim, K.P.1    Seo, D.I.2    Min, K.H.3    Ka, J.O.4    Park, Y.K.5    Kim, C.K.6
  • 16
    • 0030012764 scopus 로고    scopus 로고
    • Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments
    • Kukor J.J., Olsen R.H. Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments. Appl. Environ. Microbiol. 1996, 62(5):1728-1740.
    • (1996) Appl. Environ. Microbiol. , vol.62 , Issue.5 , pp. 1728-1740
    • Kukor, J.J.1    Olsen, R.H.2
  • 17
    • 74149094016 scopus 로고    scopus 로고
    • Growth of Pseudomonas sp. TX1 on a wide range of octylphenol polyethoxylate concentrations and the formation of dicarboxylated metabolites
    • Lin Y.W., Guo G.L., Hsieh H.C., Huang S.L. Growth of Pseudomonas sp. TX1 on a wide range of octylphenol polyethoxylate concentrations and the formation of dicarboxylated metabolites. Bioresour. Technol. 2010, 101(8):2853-2859.
    • (2010) Bioresour. Technol. , vol.101 , Issue.8 , pp. 2853-2859
    • Lin, Y.W.1    Guo, G.L.2    Hsieh, H.C.3    Huang, S.L.4
  • 18
    • 27544450953 scopus 로고    scopus 로고
    • Assessing the detoxication efficiencies of wastewater treatment processes using a battery of bioassays/biomarkers
    • Mei Ma., Li Jian., Zijian Wang. Assessing the detoxication efficiencies of wastewater treatment processes using a battery of bioassays/biomarkers. Arch. Environ. Contam. Toxicol. 2005, 49:480-487.
    • (2005) Arch. Environ. Contam. Toxicol. , vol.49 , pp. 480-487
    • Mei, M.1    Li, J.2    Zijian, W.3
  • 19
    • 0033064439 scopus 로고    scopus 로고
    • Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31
    • Mars A.E., Kingma J., Kaschabek S.R., Reineke W., Janssen D.B. Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31. J. Bacteriol. 1999, 181(4):1309-1318.
    • (1999) J. Bacteriol. , vol.181 , Issue.4 , pp. 1309-1318
    • Mars, A.E.1    Kingma, J.2    Kaschabek, S.R.3    Reineke, W.4    Janssen, D.B.5
  • 20
    • 70349652810 scopus 로고    scopus 로고
    • Sustainable risk management of emerging contaminants in municipal wastewaters
    • Martin O.V., Voulvoulis N. Sustainable risk management of emerging contaminants in municipal wastewaters. Philos. Transact. A Math. Phys. Eng. Sci. 2009, 367(1904):3895-3922.
    • (2009) Philos. Transact. A Math. Phys. Eng. Sci. , vol.367 , Issue.1904 , pp. 3895-3922
    • Martin, O.V.1    Voulvoulis, N.2
  • 21
    • 0029874406 scopus 로고    scopus 로고
    • Carbon catabolite repression of phenol degradation in Pseudomonas putida is mediated by the inhibition of the activator protein PhlR
    • Muller C., Petruschka L., Cuypers H., Burchhardt G., Herrmann H. Carbon catabolite repression of phenol degradation in Pseudomonas putida is mediated by the inhibition of the activator protein PhlR. J. Bacteriol. 1996, 178(7):2030-2036.
    • (1996) J. Bacteriol. , vol.178 , Issue.7 , pp. 2030-2036
    • Muller, C.1    Petruschka, L.2    Cuypers, H.3    Burchhardt, G.4    Herrmann, H.5
  • 22
    • 0032037223 scopus 로고    scopus 로고
    • Purification, characterization, and gene analysis of catechol 2,3-dioxygenase from the aniline-assimilating bacterium Pseudomonas species AW-2
    • Murakami S., Nakanishi Y., Kodama N., Takenaka S., Shinke R., Aoki K. Purification, characterization, and gene analysis of catechol 2,3-dioxygenase from the aniline-assimilating bacterium Pseudomonas species AW-2. Biosci. Biotechnol. Biochem. 1998, 62(4):747-752.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , Issue.4 , pp. 747-752
    • Murakami, S.1    Nakanishi, Y.2    Kodama, N.3    Takenaka, S.4    Shinke, R.5    Aoki, K.6
  • 23
    • 0028944411 scopus 로고
    • Aromatic effector activation of the NtrC-like transcriptional regulator PhhR limits the catabolic potential of the (methyl)phenol degradative pathway it controls
    • Ng L.C., Poh C.L., Shingler V. Aromatic effector activation of the NtrC-like transcriptional regulator PhhR limits the catabolic potential of the (methyl)phenol degradative pathway it controls. J. Bacteriol. 1995, 177(6):1485-1490.
    • (1995) J. Bacteriol. , vol.177 , Issue.6 , pp. 1485-1490
    • Ng, L.C.1    Poh, C.L.2    Shingler, V.3
  • 24
    • 36649023102 scopus 로고    scopus 로고
    • Identification of opdA, a gene involved in biodegradation of the endocrine disrupter octylphenol
    • Porter A.W., Hay A.G. Identification of opdA, a gene involved in biodegradation of the endocrine disrupter octylphenol. Appl. Environ. Microbiol. 2007, 73(22):7373-7379.
    • (2007) Appl. Environ. Microbiol. , vol.73 , Issue.22 , pp. 7373-7379
    • Porter, A.W.1    Hay, A.G.2
  • 25
    • 0028672047 scopus 로고
    • Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600
    • Powlowski J., Shingler V. Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600. Biodegradation 1994, 5(3-4):219-236.
    • (1994) Biodegradation , vol.5 , Issue.3-4 , pp. 219-236
    • Powlowski, J.1    Shingler, V.2
  • 26
    • 0030066424 scopus 로고    scopus 로고
    • Estrogenic activity of surfactants and some of their degradation products assessed using a recombinant yeast screen
    • Routledge E.J., Sumpter J.P. Estrogenic activity of surfactants and some of their degradation products assessed using a recombinant yeast screen. Environ. Toxicol. Chem. 1996, 15:241-248.
    • (1996) Environ. Toxicol. Chem. , vol.15 , pp. 241-248
    • Routledge, E.J.1    Sumpter, J.P.2
  • 28
    • 0037820589 scopus 로고    scopus 로고
    • Biodegradation of nonylphenol in a continuous packed-bed bioreactor
    • Soares A., Guieysse B., Mattiasson B. Biodegradation of nonylphenol in a continuous packed-bed bioreactor. Biotechnol. Lett. 2003, 25(12):927-933.
    • (2003) Biotechnol. Lett. , vol.25 , Issue.12 , pp. 927-933
    • Soares, A.1    Guieysse, B.2    Mattiasson, B.3
  • 29
    • 36048942986 scopus 로고    scopus 로고
    • Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4
    • Takeo M., Nishimura M., Takahashi H., Kitamura C., Kato D., Negoro S. Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4. J. Biosci. Bioeng. 2007, 104(4):309-314.
    • (2007) J. Biosci. Bioeng. , vol.104 , Issue.4 , pp. 309-314
    • Takeo, M.1    Nishimura, M.2    Takahashi, H.3    Kitamura, C.4    Kato, D.5    Negoro, S.6
  • 30
    • 77958565468 scopus 로고    scopus 로고
    • Isolation and characterization of 4-tert-butylphenol-utilizing Sphingobium fuliginis strains from Phragmites australis rhizosphere sediment
    • Toyama T., Momotani N., Ogata Y., Miyamori Y., Inoue D., Sei K., Mori K., Kikuchi S., Ike M. Isolation and characterization of 4-tert-butylphenol-utilizing Sphingobium fuliginis strains from Phragmites australis rhizosphere sediment. Appl. Environ. Microbiol. 2010, 76(20):6733-6740.
    • (2010) Appl. Environ. Microbiol. , vol.76 , Issue.20 , pp. 6733-6740
    • Toyama, T.1    Momotani, N.2    Ogata, Y.3    Miyamori, Y.4    Inoue, D.5    Sei, K.6    Mori, K.7    Kikuchi, S.8    Ike, M.9
  • 31
    • 79151472956 scopus 로고    scopus 로고
    • Analysis of bacterial degradation pathways for long-chain alkylphenols involving phenol hydroxylase, alkylphenol monooxygenase and catechol dioxygenase genes
    • Tuan N.N., Hsieh H.C., Lin Y.W., Huang S.L. Analysis of bacterial degradation pathways for long-chain alkylphenols involving phenol hydroxylase, alkylphenol monooxygenase and catechol dioxygenase genes. Bioresour. Technol. 2011, 102(5):4232-4240.
    • (2011) Bioresour. Technol. , vol.102 , Issue.5 , pp. 4232-4240
    • Tuan, N.N.1    Hsieh, H.C.2    Lin, Y.W.3    Huang, S.L.4
  • 32
    • 10344235266 scopus 로고    scopus 로고
    • The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1
    • Viggiani A., Siani L., Notomista E., Birolo L., Pucci P., Di Donato A. The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1. J. Biol. Chem. 2004, 279(47):48630-48639.
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 48630-48639
    • Viggiani, A.1    Siani, L.2    Notomista, E.3    Birolo, L.4    Pucci, P.5    Di Donato, A.6
  • 33
    • 0036635428 scopus 로고    scopus 로고
    • Environmental fate of alkylphenols and alkylphenol ethoxylates-a review
    • Ying G.G., Williams B., Kookana R. Environmental fate of alkylphenols and alkylphenol ethoxylates-a review. Environ. Int. 2002, 28(3):215-226.
    • (2002) Environ. Int. , vol.28 , Issue.3 , pp. 215-226
    • Ying, G.G.1    Williams, B.2    Kookana, R.3
  • 34
    • 48349088742 scopus 로고    scopus 로고
    • Molecular cloning genetic organization of gene cluster encoding phenol hydroxylase and catechol 2,3-dioxygenase in Alcaligenes faecalis IS-46
    • Zhu C., Zhang L., Zhao L. Molecular cloning genetic organization of gene cluster encoding phenol hydroxylase and catechol 2,3-dioxygenase in Alcaligenes faecalis IS-46. World Journal of Microbiology and Biotechnology 2008, 24:1687-1695.
    • (2008) World Journal of Microbiology and Biotechnology , vol.24 , pp. 1687-1695
    • Zhu, C.1    Zhang, L.2    Zhao, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.