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Volumn 191, Issue 15, 2009, Pages 4905-4915

Characterization of a gene cluster involved in 4-chlorocatechol degradation by Pseudomonas reinekei MT1

Author keywords

[No Author keywords available]

Indexed keywords

3 CHLOROMUCONIC ACID; 3 OXOADIPATE; 4 CHLOROCATECHOL; 5 CHLOROSALICYLATE; ADIPIC ACID DERIVATIVE; CARBOXYMETHYLENEBUTENOLIDASE; CATECHOL 1,2 DIOXYGENASE; CATECHOL DERIVATIVE; DIENELACTONE; HYDROLASE; ISOMERASE; LACTONE DERIVATIVE; MALEYLACETATE REDUCTASE; MUCONATE CYCLOISOMERASE; MUCONIC ACID; PROTOANEMONIN; SALICYLIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 67749088148     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00331-09     Document Type: Article
Times cited : (17)

References (65)
  • 1
    • 0033040221 scopus 로고    scopus 로고
    • A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1
    • Armengaud, J., K. N. Timmis, and R. M. Wittich. 1999. A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. J. Bacteriol. 181:3452-3461.
    • (1999) J. Bacteriol , vol.181 , pp. 3452-3461
    • Armengaud, J.1    Timmis, K.N.2    Wittich, R.M.3
  • 2
    • 0034977060 scopus 로고    scopus 로고
    • Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358
    • Bertani, I., M. Kojic, and V. Venturi. 2001. Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. Microbiology 147:1611-1620.
    • (2001) Microbiology , vol.147 , pp. 1611-1620
    • Bertani, I.1    Kojic, M.2    Venturi, V.3
  • 3
    • 0027329037 scopus 로고
    • Purification of 3,5-dichlorocatechol 1,2-dioxygenase, a nonheme iron dioxygenase and a key enzyme in the biodegradation of a herbicide, 2,4-dichlorophenoxyacetic acid (2,4-D), from Pseudomonas cepacia CSV90
    • Bhat, M. A., T. Ishida, K. Horiike, C. S. Vaidyanathan, and M. Nozaki. 1993. Purification of 3,5-dichlorocatechol 1,2-dioxygenase, a nonheme iron dioxygenase and a key enzyme in the biodegradation of a herbicide, 2,4-dichlorophenoxyacetic acid (2,4-D), from Pseudomonas cepacia CSV90. Arch. Biochem. Biophys. 300:738-746.
    • (1993) Arch. Biochem. Biophys , vol.300 , pp. 738-746
    • Bhat, M.A.1    Ishida, T.2    Horiike, K.3    Vaidyanathan, C.S.4    Nozaki, M.5
  • 4
    • 0028784952 scopus 로고
    • From xenobiotic to antibiotic. Formation of protoanemonin from 4-chlorocatechol by enzymes of the 3-oxoadipate pathway
    • Blasco, R., R.-M. Wittich, M. Mallavarapu, K. N. Timmis, and D. H. Pieper. 1995. From xenobiotic to antibiotic. Formation of protoanemonin from 4-chlorocatechol by enzymes of the 3-oxoadipate pathway. J. Biol. Chem. 270:29229-29235.
    • (1995) J. Biol. Chem , vol.270 , pp. 29229-29235
    • Blasco, R.1    Wittich, R.-M.2    Mallavarapu, M.3    Timmis, K.N.4    Pieper, D.H.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0030809197 scopus 로고    scopus 로고
    • Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens
    • Briganti, F., E. Pessione, C. Giunta, and A. Scozzafava. 1997. Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens. FEBS Lett. 416: 61-64.
    • (1997) FEBS Lett , vol.416 , pp. 61-64
    • Briganti, F.1    Pessione, E.2    Giunta, C.3    Scozzafava, A.4
  • 7
    • 33947402733 scopus 로고    scopus 로고
    • A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate
    • Cámara, B., P. Bielecki, F. Kaminski, V. M. dos Santos, I. Plumeier, P. Nikodem, and D. H. Pieper. 2007. A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate. J. Bacteriol. 189:1664-1674.
    • (2007) J. Bacteriol , vol.189 , pp. 1664-1674
    • Cámara, B.1    Bielecki, P.2    Kaminski, F.3    dos Santos, V.M.4    Plumeier, I.5    Nikodem, P.6    Pieper, D.H.7
  • 9
    • 0017251574 scopus 로고
    • Metabolism of resorcinylic compounds by bacteria: Alternative pathways for resorcinol catabolism in Pseudomonas putida
    • Chapman, P. J., and D. W. Ribbons. 1976. Metabolism of resorcinylic compounds by bacteria: alternative pathways for resorcinol catabolism in Pseudomonas putida. J. Bacteriol. 125:985-998.
    • (1976) J. Bacteriol , vol.125 , pp. 985-998
    • Chapman, P.J.1    Ribbons, D.W.2
  • 10
    • 0027168789 scopus 로고
    • Substrate-induced activation of dienelactone hydrolase: An enzyme with a naturally occuring Cys-His-Asp triad
    • Cheah, E., C. Austin, G. W. Ashley, and D. Ollis. 1993. Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occuring Cys-His-Asp triad. Protein Eng. 6:575-583.
    • (1993) Protein Eng , vol.6 , pp. 575-583
    • Cheah, E.1    Austin, C.2    Ashley, G.W.3    Ollis, D.4
  • 11
    • 0017814391 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol
    • Dorn, E., and H.-J. Knackmuss. 1978. Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol. Biochem. J. 174:85-94.
    • (1978) Biochem. J , vol.174 , pp. 85-94
    • Dorn, E.1    Knackmuss, H.-J.2
  • 12
    • 0017895519 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad
    • Dorn, E., and H.-J. Knackmuss. 1978. Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad. Biochem. J. 174:73-84.
    • (1978) Biochem. J , vol.174 , pp. 73-84
    • Dorn, E.1    Knackmuss, H.-J.2
  • 13
    • 33644862846 scopus 로고    scopus 로고
    • Analysis of antibiotic resistance gene expression in Pseudomonas aeruginosa by quantitative real-time-PCR
    • Dumas, J., C. van Delden, K. Perron, and T. Koehler. 2006. Analysis of antibiotic resistance gene expression in Pseudomonas aeruginosa by quantitative real-time-PCR. FEMS Microbiol. Lett. 254:217-225.
    • (2006) FEMS Microbiol. Lett , vol.254 , pp. 217-225
    • Dumas, J.1    van Delden, C.2    Perron, K.3    Koehler, T.4
  • 14
    • 0031909725 scopus 로고    scopus 로고
    • Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: Evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
    • Eulberg, D., S. Lakner, L. A. Golovleva, and M. Schlömann. 1998. Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J. Bacteriol. 180:1072-1081.
    • (1998) J. Bacteriol , vol.180 , pp. 1072-1081
    • Eulberg, D.1    Lakner, S.2    Golovleva, L.A.3    Schlömann, M.4
  • 15
    • 0032460513 scopus 로고    scopus 로고
    • The putative regulator of catechol catabolism in Rhodococcus opacus 1CP - an IclR-type, not a LysR-type transcriptional regulator
    • Eulberg, D., and M. Schlömann. 1998. The putative regulator of catechol catabolism in Rhodococcus opacus 1CP - an IclR-type, not a LysR-type transcriptional regulator. Antonie van Leeuwenhoek 74:71-82.
    • (1998) Antonie van Leeuwenhoek , vol.74 , pp. 71-82
    • Eulberg, D.1    Schlömann, M.2
  • 16
    • 0027511734 scopus 로고
    • Syntrophic interactions during degradation of 4-aminobenzenesulfonic acid by a two species bacterial culture
    • Feigel, B. J., and H.-J. Knackmuss. 1993. Syntrophic interactions during degradation of 4-aminobenzenesulfonic acid by a two species bacterial culture. Arch. Microbiol. 159:124-130.
    • (1993) Arch. Microbiol , vol.159 , pp. 124-130
    • Feigel, B.J.1    Knackmuss, H.-J.2
  • 17
    • 20444401188 scopus 로고    scopus 로고
    • Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation
    • Ferraroni, M., J. Seifert, V. M. Travkin, M. Thiel, S. Kaschabek, A. Scozzafava, L. Golovleva, M. Schlömann, and F. Briganti. 2005. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280:21144-21154.
    • (2005) J. Biol. Chem , vol.280 , pp. 21144-21154
    • Ferraroni, M.1    Seifert, J.2    Travkin, V.M.3    Thiel, M.4    Kaschabek, S.5    Scozzafava, A.6    Golovleva, L.7    Schlömann, M.8    Briganti, F.9
  • 18
    • 0031938056 scopus 로고    scopus 로고
    • PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter
    • Gerischer, U., A. Segura, and L. N. Ornston. 1998. PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter. J. Bacteriol. 180:1512-1524.
    • (1998) J. Bacteriol , vol.180 , pp. 1512-1524
    • Gerischer, U.1    Segura, A.2    Ornston, L.N.3
  • 19
    • 1842800737 scopus 로고
    • Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions
    • Gerlt, J. A., and P. G. Gassmann. 1992. Understanding enzyme-catalyzed proton abstraction from carbon acids: details of stepwise mechanisms for β-elimination reactions. J. Am. Chem. Soc. 114:5928-5934.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 5928-5934
    • Gerlt, J.A.1    Gassmann, P.G.2
  • 20
    • 0026760856 scopus 로고
    • Microbial breakdown of halogenated aromatics pesticides and related compounds
    • Häggblom, M. M. 1992. Microbial breakdown of halogenated aromatics pesticides and related compounds. FEMS Microbiol. Rev. 103:29-72.
    • (1992) FEMS Microbiol. Rev , vol.103 , pp. 29-72
    • Häggblom, M.M.1
  • 21
    • 33750960096 scopus 로고    scopus 로고
    • Characterization of the genes encoding the 3-carboxy-cis,cis-muconate- lactonizing enzymes from the 4-sulfocatechol degradative pathways of Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2
    • Halak, S., T. Basta, S. Burger, M. Contzen, and A. Stolz. 2006. Characterization of the genes encoding the 3-carboxy-cis,cis-muconate- lactonizing enzymes from the 4-sulfocatechol degradative pathways of Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2. Microbiology 152:3207-3216.
    • (2006) Microbiology , vol.152 , pp. 3207-3216
    • Halak, S.1    Basta, T.2    Burger, S.3    Contzen, M.4    Stolz, A.5
  • 22
    • 0029200309 scopus 로고
    • The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 Å resolution
    • Helin, S., P. C. Kahn, B. L. Guha, D. G. Mallows, and A. Goldman. 1995. The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 Å resolution. J. Mol. Biol. 254:918-941.
    • (1995) J. Mol. Biol , vol.254 , pp. 918-941
    • Helin, S.1    Kahn, P.C.2    Guha, B.L.3    Mallows, D.G.4    Goldman, A.5
  • 24
    • 33751016057 scopus 로고    scopus 로고
    • Genetic characterization of the resorcinol catabolic pathway in Corynebacterium glutamicum
    • Huang, Y., K. X. Zhao, X. H. Shen, M. T. Chaudhry, C. Y. Jiang, and S. J. Liu. 2006. Genetic characterization of the resorcinol catabolic pathway in Corynebacterium glutamicum. Appl. Environ. Microbiol. 72:7238-7245.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 7238-7245
    • Huang, Y.1    Zhao, K.X.2    Shen, X.H.3    Chaudhry, M.T.4    Jiang, C.Y.5    Liu, S.J.6
  • 25
    • 0031745320 scopus 로고    scopus 로고
    • Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in Burkholderia cepacia AC1100: Characterization of the tftC and tftD genes and locations of the tft operons on multiple replicons
    • Hübner, A., C. E. Danganan, L. Y. Xun, A. M. Chakrabarty, and W. Hendrickson. 1998. Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in Burkholderia cepacia AC1100: characterization of the tftC and tftD genes and locations of the tft operons on multiple replicons. Appl. Environ. Microbiol. 64:2086-2093.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 2086-2093
    • Hübner, A.1    Danganan, C.E.2    Xun, L.Y.3    Chakrabarty, A.M.4    Hendrickson, W.5
  • 26
    • 1142281826 scopus 로고    scopus 로고
    • Functional gene diversity analysis in BTEX contaminated soils by means of PCR-SSCP DNA fingerprinting: Comparative diversity assessment against bacterial isolates and PCR-DNA clone libraries
    • Junca, H., and D. H. Pieper. 2004. Functional gene diversity analysis in BTEX contaminated soils by means of PCR-SSCP DNA fingerprinting: comparative diversity assessment against bacterial isolates and PCR-DNA clone libraries. Environ. Microbiol. 6:95-110.
    • (2004) Environ. Microbiol , vol.6 , pp. 95-110
    • Junca, H.1    Pieper, D.H.2
  • 27
    • 0027380662 scopus 로고
    • Degradation of chloroaromatics: Purification and characterization of maleylacetate reductase from Pseudomonas sp. strain B13
    • Kaschabek, S. R., and W. Reineke. 1993. Degradation of chloroaromatics: purification and characterization of maleylacetate reductase from Pseudomonas sp. strain B13. J. Bacteriol. 175:6075-6081.
    • (1993) J. Bacteriol , vol.175 , pp. 6075-6081
    • Kaschabek, S.R.1    Reineke, W.2
  • 28
    • 0026475123 scopus 로고
    • Maleylacetate reductase of Pseudomonas sp. strain B13: Dechlorination of chloromaleylacetates, metabolites in the degradation of chloroaromatic compounds
    • Kaschabek, S. R., and W. Reineke. 1992. Maleylacetate reductase of Pseudomonas sp. strain B13: dechlorination of chloromaleylacetates, metabolites in the degradation of chloroaromatic compounds. Arch. Microbiol. 158:412-417.
    • (1992) Arch. Microbiol , vol.158 , pp. 412-417
    • Kaschabek, S.R.1    Reineke, W.2
  • 29
    • 0034945353 scopus 로고    scopus 로고
    • Mechanism of chloride elimination from 3-chloro- and 2,4-dichloro- cis,cis-muconate: New insight obtained from analysis of muconate cycloisomerase variant CatBK169A
    • Kaulmann, U., S. R. Kaschabek, and M. Schlömann. 2001. Mechanism of chloride elimination from 3-chloro- and 2,4-dichloro- cis,cis-muconate: new insight obtained from analysis of muconate cycloisomerase variant CatBK169A. J. Bacteriol. 183:4551-4561.
    • (2001) J. Bacteriol , vol.183 , pp. 4551-4561
    • Kaulmann, U.1    Kaschabek, S.R.2    Schlömann, M.3
  • 31
    • 0025273166 scopus 로고
    • Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus
    • Kuhm, A. E., M. Schlömann, H.-J. Knackmuss, and D. H. Pieper. 1990. Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus JMP134. Biochem. J. 266:877-883.
    • (1990) JMP134. Biochem. J , vol.266 , pp. 877-883
    • Kuhm, A.E.1    Schlömann, M.2    Knackmuss, H.-J.3    Pieper, D.H.4
  • 32
    • 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 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 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. van Agteren, D. B. Janssen, and W. Reineke. 1997. Microbial degradation of chloroaromatics: use of the meta-cleavage pathway for mineralization of chlorobenzene. J. Bacteriol. 179:4530-4537.
    • (1997) J. Bacteriol , vol.179 , pp. 4530-4537
    • Mars, A.E.1    Kasberg, T.2    Kaschabek, S.R.3    van Agteren, M.H.4    Janssen, D.B.5    Reineke, W.6
  • 34
    • 2142689713 scopus 로고    scopus 로고
    • Efficient degradation of 2,4,6-trichlorophenol requires a set of catabolic genes related to tcp genes from Ralstonia eutropha JMP134 (pJP4)
    • Matus, V., M. A. Sánchez, M. Martínez, and B. González. 2003. Efficient degradation of 2,4,6-trichlorophenol requires a set of catabolic genes related to tcp genes from Ralstonia eutropha JMP134 (pJP4). Appl. Environ. Microbiol. 69:7108-7115.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 7108-7115
    • Matus, V.1    Sánchez, M.A.2    Martínez, M.3    González, B.4
  • 35
    • 0036777640 scopus 로고    scopus 로고
    • A new modified ortho cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: Genetic and biochemical evidence
    • Moiseeva, O. V., I. P. Solyanikova, S. R. Kaschabek, J. Groning, M. Thiel, L. A. Golovleva, and M. Schlömann. 2002. A new modified ortho cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidence. J. Bacteriol. 184:5282-5292.
    • (2002) J. Bacteriol , vol.184 , pp. 5282-5292
    • Moiseeva, O.V.1    Solyanikova, I.P.2    Kaschabek, S.R.3    Groning, J.4    Thiel, M.5    Golovleva, L.A.6    Schlömann, M.7
  • 36
    • 0029671186 scopus 로고    scopus 로고
    • Maleylacetate reductases in chloroaromatic-degrading bacteria using the modified ortho pathway: Comparison of catalytic properties
    • Müller, D., M. Schlömann, and W. Reineke. 1996. Maleylacetate reductases in chloroaromatic-degrading bacteria using the modified ortho pathway: comparison of catalytic properties. J. Bacteriol. 178:298-300.
    • (1996) J. Bacteriol , vol.178 , pp. 298-300
    • Müller, D.1    Schlömann, M.2    Reineke, W.3
  • 37
    • 0025159432 scopus 로고
    • Three isoenzymes of catechol 1,2-dioxygenase (Pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1
    • Nakai, C., K. Horiike, S. Kuramitsu, H. Kagamiyama, and M. Nozaki. 1990. Three isoenzymes of catechol 1,2-dioxygenase (Pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1. J. Biol. Chem. 265:660-665.
    • (1990) J. Biol. Chem , vol.265 , pp. 660-665
    • Nakai, C.1    Horiike, K.2    Kuramitsu, S.3    Kagamiyama, H.4    Nozaki, M.5
  • 38
    • 0024258298 scopus 로고
    • Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1
    • Nakai, C., T. Nakazawa, and M. Nozaki. 1988. Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1. Arch. Biochem. Biophys. 267:701-713.
    • (1988) Arch. Biochem. Biophys , vol.267 , pp. 701-713
    • Nakai, C.1    Nakazawa, T.2    Nozaki, M.3
  • 39
    • 0344825087 scopus 로고    scopus 로고
    • New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1
    • Nikodem, P., V. Hecht, M. Schlömann, and D. H. Pieper. 2003. New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1. J. Bacteriol. 185:6790-6800.
    • (2003) J. Bacteriol , vol.185 , pp. 6790-6800
    • Nikodem, P.1    Hecht, V.2    Schlömann, M.3    Pieper, D.H.4
  • 40
    • 0029035387 scopus 로고
    • Supraoperonic clustering of pca genes for catabolism of the phenolic compound protocatechuate in Agrobacterium tumefaciens
    • Parke, D. 1995. Supraoperonic clustering of pca genes for catabolism of the phenolic compound protocatechuate in Agrobacterium tumefaciens. J. Bacteriol. 177:3808-3817.
    • (1995) J. Bacteriol , vol.177 , pp. 3808-3817
    • Parke, D.1
  • 41
    • 48749084090 scopus 로고    scopus 로고
    • Community-based degradation of 4-chlorosalicylate tracked on the single cell level
    • Pawelczyk, S., W. R. Abraham, H. Harms, and S. Müller. 2008. Community-based degradation of 4-chlorosalicylate tracked on the single cell level. J. Microbiol. Methods 75:117-126.
    • (2008) J. Microbiol. Methods , vol.75 , pp. 117-126
    • Pawelczyk, S.1    Abraham, W.R.2    Harms, H.3    Müller, S.4
  • 42
    • 0033108071 scopus 로고    scopus 로고
    • Towards elucidation of microbial community metabolic pathways: Unravelling the network of carbon sharing in a pollutant-degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry
    • Pelz, O., M. Tesar, R. M. Wittich, E. R. B. Moore, K. N. Timmis, and W. R. Abraham. 1999. Towards elucidation of microbial community metabolic pathways: unravelling the network of carbon sharing in a pollutant-degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry. Environ. Microbiol. 1:167-174.
    • (1999) Environ. Microbiol , vol.1 , pp. 167-174
    • Pelz, O.1    Tesar, M.2    Wittich, R.M.3    Moore, E.R.B.4    Timmis, K.N.5    Abraham, W.R.6
  • 43
    • 0037371162 scopus 로고    scopus 로고
    • Efficient turnover of chlorocatechols is essential for growth of Ralstonia eutropha JMP134(pJP4) in 3-chlorobenzoic acid
    • Perez-Pantoja, D., T. Ledger, D. H. Pieper, and B. Gonzalez. 2003. Efficient turnover of chlorocatechols is essential for growth of Ralstonia eutropha JMP134(pJP4) in 3-chlorobenzoic acid. J. Bacteriol. 185:1534-1542.
    • (2003) J. Bacteriol , vol.185 , pp. 1534-1542
    • Perez-Pantoja, D.1    Ledger, T.2    Pieper, D.H.3    Gonzalez, B.4
  • 44
    • 17844397226 scopus 로고    scopus 로고
    • Aerobic degradation of polychlorinated biphenyls
    • Pieper, D. H. 2005. Aerobic degradation of polychlorinated biphenyls. Appl. Microbiol. Biotechnol. 67:170-191.
    • (2005) Appl. Microbiol. Biotechnol , vol.67 , pp. 170-191
    • Pieper, D.H.1
  • 45
    • 0035148730 scopus 로고    scopus 로고
    • Chlorocatechols at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase Pseudomonas chlororaphis RW71
    • Potrawfke, T., J. Armengaud, and R. M. Wittich. 2001. Chlorocatechols at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase Pseudomonas chlororaphis RW71. J. Bacteriol. 183:997-1011.
    • (2001) J. Bacteriol , vol.183 , pp. 997-1011
    • Potrawfke, T.1    Armengaud, J.2    Wittich, R.M.3
  • 46
    • 0029928157 scopus 로고    scopus 로고
    • Metabolism of 5-chlorosubstituted muconolactones
    • Prucha, M., V. Wray, and D. H. Pieper. 1996. Metabolism of 5-chlorosubstituted muconolactones. Eur. J. Biochem. 237:357-366.
    • (1996) Eur. J. Biochem , vol.237 , pp. 357-366
    • Prucha, M.1    Wray, V.2    Pieper, D.H.3
  • 47
    • 0024148746 scopus 로고
    • Microbial degradation of haloaromatics
    • Reineke, W., and H.-J. Knackmuss. 1988. Microbial degradation of haloaromatics. Annu. Rev. Microbiol. 42:263-287.
    • (1988) Annu. Rev. Microbiol , vol.42 , pp. 263-287
    • Reineke, W.1    Knackmuss, H.-J.2
  • 48
    • 0021329184 scopus 로고
    • Microbial metabolism of haloaromatics: Isolation and properties of a chlorobenzene-degrading bacterium
    • Reineke, W., and H.-J. Knackmuss. 1984. Microbial metabolism of haloaromatics: isolation and properties of a chlorobenzene-degrading bacterium. Appl. Environ. Microbiol. 47:395-402.
    • (1984) Appl. Environ. Microbiol , vol.47 , pp. 395-402
    • Reineke, W.1    Knackmuss, H.-J.2
  • 49
    • 0032190167 scopus 로고    scopus 로고
    • Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1
    • Ridder, L., F. Briganti, M. Boersma, S. Boeren, E. Vis, A. Scozzafava, C. Veeger, and I. Rietjens. 1998. Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1. Eur. J. Biochem. 257:92-100.
    • (1998) Eur. J. Biochem , vol.257 , pp. 92-100
    • Ridder, L.1    Briganti, F.2    Boersma, M.3    Boeren, S.4    Vis, E.5    Scozzafava, A.6    Veeger, C.7    Rietjens, I.8
  • 50
    • 0027937565 scopus 로고
    • Characterization of the pcaR regulatory gene from Pseudomonas putida, which is required for the complete degradation of p-hydroxybenzoate
    • Romero-Steiner, S., R. E. Parales, C. S. Harwood, and J. E. Houghton. 1994. Characterization of the pcaR regulatory gene from Pseudomonas putida, which is required for the complete degradation of p-hydroxybenzoate. J. Bacteriol. 176:5771-5779.
    • (1994) J. Bacteriol , vol.176 , pp. 5771-5779
    • Romero-Steiner, S.1    Parales, R.E.2    Harwood, C.S.3    Houghton, J.E.4
  • 51
    • 0029742386 scopus 로고    scopus 로고
    • Characterisation of a chromosomally encoded catechol 1,2-dioxygenase (EC 1.13.11.1) from Alcaligenes eutrophus CH34
    • Sauret-Ignazi, G., J. Gagnon, C. Beguin, M. Barrelle, Y. Markowicz, J. Pelmont, and A. Toussaint. 1996. Characterisation of a chromosomally encoded catechol 1,2-dioxygenase (EC 1.13.11.1) from Alcaligenes eutrophus CH34. Arch. Microbiol. 166:42-50.
    • (1996) Arch. Microbiol , vol.166 , pp. 42-50
    • Sauret-Ignazi, G.1    Gagnon, J.2    Beguin, C.3    Barrelle, M.4    Markowicz, Y.5    Pelmont, J.6    Toussaint, A.7
  • 52
    • 0032964802 scopus 로고    scopus 로고
    • Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates
    • Schell, U., S. Helin, T. Kajander, M. Schlömann, and A. Goldman. 1999. Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates. Proteins 34:125-136.
    • (1999) Proteins , vol.34 , pp. 125-136
    • Schell, U.1    Helin, S.2    Kajander, T.3    Schlömann, M.4    Goldman, A.5
  • 53
    • 0028708533 scopus 로고
    • Evolution of chlorocatechol catabolic pathways. Conclusions to be drawn from comparisons of lactone hydrolases
    • Schlömann, M. 1994. Evolution of chlorocatechol catabolic pathways. Conclusions to be drawn from comparisons of lactone hydrolases. Biodegradation 5:301-321.
    • (1994) Biodegradation , vol.5 , pp. 301-321
    • Schlömann, M.1
  • 54
    • 0019162442 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid
    • Schmidt, E., and H.-J. Knackmuss. 1980. Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid. Biochem. J. 192:339-347.
    • (1980) Biochem. J , vol.192 , pp. 339-347
    • Schmidt, E.1    Knackmuss, H.-J.2
  • 55
    • 0035211211 scopus 로고    scopus 로고
    • Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals
    • Schweigert, N., A. J. B. Zehnder, and R. I. L. Eggen. 2001. Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals. Environ. Microbiol. 3:81-91.
    • (2001) Environ. Microbiol , vol.3 , pp. 81-91
    • Schweigert, N.1    Zehnder, A.J.B.2    Eggen, R.I.L.3
  • 56
    • 0032457281 scopus 로고    scopus 로고
    • Characterization of the maleylacetate reductase MacA of Rhodococcus opacus 1CP and evidence for the presence of an isofunctional enzyme
    • Seibert, V., E. M. Kourbatova, L. A. Golovleva, and M. Schlomann. 1998. Characterization of the maleylacetate reductase MacA of Rhodococcus opacus 1CP and evidence for the presence of an isofunctional enzyme. J. Bacteriol. 180:3503-3508.
    • (1998) J. Bacteriol , vol.180 , pp. 3503-3508
    • Seibert, V.1    Kourbatova, E.M.2    Golovleva, L.A.3    Schlomann, M.4
  • 57
    • 0027522089 scopus 로고
    • Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)
    • Seibert, V., K. Stadler-Fritzsche, and M. Schlömann. 1993. Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4). J. Bacteriol. 175:6745-6754.
    • (1993) J. Bacteriol , vol.175 , pp. 6745-6754
    • Seibert, V.1    Stadler-Fritzsche, K.2    Schlömann, M.3
  • 58
    • 0029014004 scopus 로고
    • Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: Indications for functionally convergent evolution among bacterial cycloisomerases
    • Solyanikova, I. P., O. V. Malteva, M. D. Vollmer, L. A. Golovleva, and M. Schlömann. 1995. Characterization of muconate and chloromuconate cycloisomerase from Rhodococcus erythropolis 1CP: indications for functionally convergent evolution among bacterial cycloisomerases. J. Bacteriol. 177: 2821-2826.
    • (1995) J. Bacteriol , vol.177 , pp. 2821-2826
    • Solyanikova, I.P.1    Malteva, O.V.2    Vollmer, M.D.3    Golovleva, L.A.4    Schlömann, M.5
  • 59
    • 34547781750 scopus 로고    scopus 로고
    • Tamura, K, J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: molecular evolutionary genetic analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: molecular evolutionary genetic analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
  • 60
    • 13844253486 scopus 로고    scopus 로고
    • Two unusual chlorocatechol catabolic gene clusters in Sphingomonas sp. TFD44
    • Thiel, M., S. Kaschabek, J. Gröning, M. Mau, and M. Schlömann. 2005. Two unusual chlorocatechol catabolic gene clusters in Sphingomonas sp. TFD44. Arch. Microbiol. 183:80-94.
    • (2005) Arch. Microbiol , vol.183 , pp. 80-94
    • Thiel, M.1    Kaschabek, S.2    Gröning, J.3    Mau, M.4    Schlömann, M.5
  • 61
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 62
    • 4544275675 scopus 로고    scopus 로고
    • Bacterial transcriptional regulators for degradation pathways of aromatic compounds
    • Tropel, D., and J. R. van der Meer. 2004. Bacterial transcriptional regulators for degradation pathways of aromatic compounds. Microbiol. Mol. Biol. Rev. 68:474-500.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 474-500
    • Tropel, D.1    van der Meer, J.R.2
  • 63
    • 0031684925 scopus 로고    scopus 로고
    • Substrate specificity of and product formation by muconate cycloisomerases: An analysis of wild-type enzymes and engineered variants
    • Vollmer, M. D., H. Hoier, H. J. Hecht, U. Schell, J. Groning, A. Goldman, and M. Schlömann. 1998. Substrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants. Appl. Environ. Microbiol. 64:3290-3299.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 3290-3299
    • Vollmer, M.D.1    Hoier, H.2    Hecht, H.J.3    Schell, U.4    Groning, J.5    Goldman, A.6    Schlömann, M.7
  • 64
    • 0033061607 scopus 로고    scopus 로고
    • Substrate specificities of the chloromuconate cycloisomerases from Pseudomonas sp. B13, Ralstonia eutropha JMP134 and Pseudomonas sp. P51
    • Vollmer, M. D., U. Schell, V. Seibert, S. Lakner, and M. Schlömann. 1999. Substrate specificities of the chloromuconate cycloisomerases from Pseudomonas sp. B13, Ralstonia eutropha JMP134 and Pseudomonas sp. P51. Appl. Microbiol. Biotechnol. 51:598-605.
    • (1999) Appl. Microbiol. Biotechnol , vol.51 , pp. 598-605
    • Vollmer, M.D.1    Schell, U.2    Seibert, V.3    Lakner, S.4    Schlömann, M.5
  • 65
    • 0029077739 scopus 로고
    • Conversion of 2-chloro-cis,cis-muconate and its matabolites 2-chloro- and 5-chloromuconolactone by chloromuconate cycloisomerases of pJP4 and pAC27
    • Vollmer, M. K., and M. Schlömann. 1995. Conversion of 2-chloro-cis,cis-muconate and its matabolites 2-chloro- and 5-chloromuconolactone by chloromuconate cycloisomerases of pJP4 and pAC27. J. Bacteriol. 177:2938-2941.
    • (1995) J. Bacteriol , vol.177 , pp. 2938-2941
    • Vollmer, M.K.1    Schlömann, M.2


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