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Volumn 179, Issue 1, 1997, Pages 202-208

Purification and characterization of 2,4,6-trichlorophenol-4- monooxygenase, a dehalogenating enzyme from Azotobacter sp. strain GP1

Author keywords

[No Author keywords available]

Indexed keywords

2,4,6 TRICHLOROPHENOL; UNSPECIFIC MONOOXYGENASE;

EID: 0031019867     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.1.202-208.1997     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 84985268933 scopus 로고
    • Characterization of the Rhodococcus sp. BPG-8 resoreinol hydroxylase
    • Armstrong, S. M., and T. R. Patel. 1993. Characterization of the Rhodococcus sp. BPG-8 resoreinol hydroxylase. J. Basic Microbiol. 33:75-81.
    • (1993) J. Basic Microbiol. , vol.33 , pp. 75-81
    • Armstrong, S.M.1    Patel, T.R.2
  • 2
    • 0027065530 scopus 로고
    • P-Hydroxyphenylacetate-3-hydroxylase, a two-protein component enzyme
    • Arunachalam, U., V. Massey, and C. S. Vaidyanathan. 1992. p-Hydroxyphenylacetate-3-hydroxylase, a two-protein component enzyme. J. Biol. Chem. 267:25848-25855.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25848-25855
    • Arunachalam, U.1    Massey, V.2    Vaidyanathan, C.S.3
  • 3
    • 0019994544 scopus 로고
    • The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species
    • Beadle, C. A., and R. W. Smith. 1982. The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species. Eur. J. Biochem. 123:323-332.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 323-332
    • Beadle, C.A.1    Smith, R.W.2
  • 4
    • 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. 1976. 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) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028100163 scopus 로고
    • Bacterial dehalogenases: Biochemistry, genetics and biotechnological applications
    • Fetzner, S., and F. Lingens. 1994. Bacterial dehalogenases: biochemistry, genetics and biotechnological applications. Microbiol. Rev. 38:641-685.
    • (1994) Microbiol. Rev. , vol.38 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 6
    • 0000477640 scopus 로고
    • Spectrophotometric determination of chloride at the parts-per-billion level by the mercury (II) thiocyanate method
    • Florence, T. M., Y. J. Farrar, and L. Hights. 1971. Spectrophotometric determination of chloride at the parts-per-billion level by the mercury (II) thiocyanate method. Anal. Chim. Acta 54:373-377.
    • (1971) Anal. Chim. Acta , vol.54 , pp. 373-377
    • Florence, T.M.1    Farrar, Y.J.2    Hights, L.3
  • 8
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450
    • Gorsky, L. D., D. R. Kopp, and M. J. Coon. 1984. On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. J. Biol. Chem. 259:6812-6817.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6812-6817
    • Gorsky, L.D.1    Kopp, D.R.2    Coon, M.J.3
  • 9
    • 0025367352 scopus 로고
    • Mechanisms of bacterial degradation and transformation of chlorinated monoaromatic compounds
    • Hägghlom, M. 1990. Mechanisms of bacterial degradation and transformation of chlorinated monoaromatic compounds. J. Basic Microbiol. 30:115-141.
    • (1990) J. Basic Microbiol. , vol.30 , pp. 115-141
    • Hägghlom, M.1
  • 10
    • 0026760856 scopus 로고
    • Microbial breakdown of halogenated aromatic pesticides and related compounds
    • Häggblom, M. 1992b Microbial breakdown of halogenated aromatic pesticides and related compounds. FEMS Microbiol. Rev. 103:29-72.
    • (1992) FEMS Microbiol. Rev. , vol.103 , pp. 29-72
    • Häggblom, M.1
  • 11
    • 0028384706 scopus 로고
    • Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Pyl
    • Hormann, K., and J. R. Andreesen. 1994. Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Pyl. Biol. Chem. Hoppe-Seyler 375:211-218.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 211-218
    • Hormann, K.1    Andreesen, J.R.2
  • 12
    • 0026591315 scopus 로고
    • Isolation of Pseudomans picketti strains that degrade 2,4.6 trichlorophenol and their dechlorination of chlorophenols
    • Kiyohara, H., T. Hatta, Y. Ogama, T. Kakuda, H. Yokojamn, and N. Takizawa. 1992. Isolation of Pseudomans picketti strains that degrade 2,4.6 trichlorophenol and their dechlorination of chlorophenols. Appl. Environ Microbiol. 58:1276-1283.
    • (1992) Appl. Environ Microbiol. , vol.58 , pp. 1276-1283
    • Kiyohara, H.1    Hatta, T.2    Ogama, Y.3    Kakuda, T.4    Yokojamn, H.5    Takizawa, N.6
  • 13
    • 0029032304 scopus 로고
    • Purification and characterization of hydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1
    • Latus, M., H.-J. Seitz, J. Eberspächer, and F. Lingens. 1995. Purification and characterization of hydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1. Appl. Environ. Microbiol. 61:2453-2460.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2453-2460
    • Latus, M.1    Seitz, H.-J.2    Eberspächer, J.3    Lingens, F.4
  • 15
    • 85063518034 scopus 로고
    • Phenol hydroxylase
    • F. Müller (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Neujahr, H. Y. 1991. Phenol hydroxylase. p. 65-85. In F. Müller (ed.), Chemistry and biochemistry of flavoenzymes, vol. II. CRC Press, Inc., Boca Raton, Fla.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.2 , pp. 65-85
    • Neujahr, H.Y.1
  • 16
    • 0027476196 scopus 로고
    • Cloning, sequence analysis, and expression of Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli
    • Orser, C. S., C. C. Lange, L. Xun, T. C. Zahrt, and B. J. Schneider. 1993. Cloning, sequence analysis, and expression of Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli. J. Bacteriol. 175:411-416.
    • (1993) J. Bacteriol. , vol.175 , pp. 411-416
    • Orser, C.S.1    Lange, C.C.2    Xun, L.3    Zahrt, T.C.4    Schneider, B.J.5
  • 17
    • 0028672052 scopus 로고
    • Molecular analysis of pentachlorophenol degradation
    • Orser, C. S., and C. C. Lange. 1994. Molecular analysis of pentachlorophenol degradation. Biodegradation 5:277-288.
    • (1994) Biodegradation , vol.5 , pp. 277-288
    • Orser, C.S.1    Lange, C.C.2
  • 18
    • 0028093362 scopus 로고
    • Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylaxe of Escherichia coli
    • Prieto, M. A., and J. L. Garcia. 1994. Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylaxe of Escherichia coli. J. Biol. Chem. 269:22823-22829.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22823-22829
    • Prieto, M.A.1    Garcia, J.L.2
  • 19
    • 0025851175 scopus 로고
    • Affinity purification and characterization of 2,4-dichlorophenol hydroxylase from Psedomonas cepacia
    • Radjendirane, V., M. A. Bhat, and C. S. Vaidyanathan. 1991. Affinity purification and characterization of 2,4-dichlorophenol hydroxylase from Psedomonas cepacia. Arch. Biochem. Biophys. 288:169-176.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 169-176
    • Radjendirane, V.1    Bhat, M.A.2    Vaidyanathan, C.S.3
  • 20
    • 0025319217 scopus 로고
    • Substrate-mediated purification and characterization of a 3-hydroxybenzoicacae id-6-hydroxylase from Micrococcus
    • Rajasekharan, S., R. Rajasekharan, and C. S. Vaidyanathan. 1990. Substrate-mediated purification and characterization of a 3-hydroxybenzoicacae id-6-hydroxylase from Micrococcus. Arch. Biochem. Biophys. 278:21-25.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 21-25
    • Rajasekharan, S.1    Rajasekharan, R.2    Vaidyanathan, C.S.3
  • 21
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 23
    • 0024442956 scopus 로고
    • Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter up. strain ATCC 33790
    • Schenk, T., R. Müller, F. Mörsberger, M. K. Otto, and F. Lingens. 1989. Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter up. strain ATCC 33790. J. Bacteriol. 171:5487-5491.
    • (1989) J. Bacteriol. , vol.171 , pp. 5487-5491
    • Schenk, T.1    Müller, R.2    Mörsberger, F.3    Otto, M.K.4    Lingens, F.5
  • 24
    • 0028793586 scopus 로고
    • A locus of Pseudomonas pickettii DTP0602, had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity, and hydroxylation of various chlorophenols by the enzyme
    • Takizawa, N., H. Yokoyama, K. Yanagihara, T. Hatta, and H. Kiyohara. 1995. A locus of Pseudomonas pickettii DTP0602, had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity, and hydroxylation of various chlorophenols by the enzyme. J. Ferment. Bioeng. 80:318-326.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 318-326
    • Takizawa, N.1    Yokoyama, H.2    Yanagihara, K.3    Hatta, T.4    Kiyohara, H.5
  • 25
    • 0028813521 scopus 로고
    • Metabolism of polychlorinated phenols by Pseudomonas cepacia AC11OO: Determiniuion of the first two steps and specific inhibitory effect of methimazole
    • Tomasi, I., I. Artaud, Y. Bertheau, and D. Mansuy. 1995. Metabolism of polychlorinated phenols by Pseudomonas cepacia AC11OO: determiniuion of the first two steps and specific inhibitory effect of methimazole. J. Bacteriol. 177:307-311.
    • (1995) J. Bacteriol. , vol.177 , pp. 307-311
    • Tomasi, I.1    Artaud, I.2    Bertheau, Y.3    Mansuy, D.4
  • 26
    • 0026303461 scopus 로고
    • Dechlorination of pentachlorophenol by membrane bound enzymes of Rhodococcus chlorophenolicus PCP-I
    • Uotila, J. S., M. S. Salkinoja-Salonen, and J. H. A. Apajahihti. 1991. Dechlorination of pentachlorophenol by membrane bound enzymes of Rhodococcus chlorophenolicus PCP-I. Biodegradation 2:25-31.
    • (1991) Biodegradation , vol.2 , pp. 25-31
    • Uotila, J.S.1    Salkinoja-Salonen, M.S.2    Apajahihti, J.H.A.3
  • 29
    • 0025925008 scopus 로고
    • Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: A novel FAD-dependent monooxygenase from a Flavobacterium species
    • van Berkei, W. J. H., and W. J. J. van den Tweel. 1991. Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium species. Eur. J. Biochem. 201:585-592.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 585-592
    • Van Berkei, W.J.H.1    Van den Tweel, W.J.J.2
  • 30
    • 85035186351 scopus 로고    scopus 로고
    • 1992. Recommendations of the Nomenclature Committee of the International Union of Biochemistry on the nomenclature of enzyme-catalyzed reactions. Academic Press. Inc., Orlando, Fla.
    • Webb, E. C. 1992. Recommendations of the Nomenclature Committee of the International Union of Biochemistry on the nomenclature of enzyme-catalyzed reactions. Academic Press. Inc., Orlando, Fla.
    • Webb, E.C.1
  • 31
    • 0015522985 scopus 로고
    • Studies of a flavoprotein. salicylate hydroxylase
    • White-Stevens, R. H., and H. Kamin. 1972. Studies of a flavoprotein. salicylate hydroxylase. J. Biol. Chem. 247:2358-2370.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2358-2370
    • White-Stevens, R.H.1    Kamin, H.2
  • 32
    • 0027954492 scopus 로고
    • Metabolism of 4-chlorophenol by Azotobacter sp. GP1: Structure of the meta cleavage product of 4-chlorocatechol
    • Wieser, M., J. Eberspächer, B. Vogler, and F. Língens. 1994. Metabolism of 4-chlorophenol by Azotobacter sp. GP1: structure of the meta cleavage product of 4-chlorocatechol. FEMS Microbiol. Lett. 116:73-78.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 73-78
    • Wieser, M.1    Eberspächer, J.2    Vogler, B.3    Língens, F.4
  • 33
    • 0029924178 scopus 로고    scopus 로고
    • Purification and characterization of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100
    • Xun, L. 1996. Purification and characterization of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100. J. Bacteriol. 178:2645-2649.
    • (1996) J. Bacteriol. , vol.178 , pp. 2645-2649
    • Xun, L.1
  • 34
    • 0025733737 scopus 로고
    • Purification and properties of pentachlorophenol hydroxylase. a flavoprotein from Flavobacterium sp. strain ATCC 39723
    • Xun, L., and C. S. Orser. 1991. Purification and properties of pentachlorophenol hydroxylase. a flavoprotein from Flavobacterium sp. strain ATCC 39723. J. Bacteriol. 173:4447-4453.
    • (1991) J. Bacteriol. , vol.173 , pp. 4447-4453
    • Xun, L.1    Orser, C.S.2
  • 35
    • 0026770524 scopus 로고
    • Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries
    • Xun, L., E. Topp, and C. S. Orser. 1992. Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries. J. Bacteriol. 174:2898-2902.
    • (1992) J. Bacteriol. , vol.174 , pp. 2898-2902
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 36
    • 0028869982 scopus 로고
    • Purification and characterization of 6-chlorohydroxyquinol 1.2-dioxygenase from Streptomyces rochei 303: Comparison with an analogous enzyme from Azoiobacter sp. strain GP1
    • Zaborina, O., M. Latus, J. Eberspächer, L. A. Golovleva, and K. Lingens. 1995. Purification and characterization of 6-chlorohydroxyquinol 1.2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azoiobacter sp. strain GP1. J. Bacteriol. 177:229-234.
    • (1995) J. Bacteriol. , vol.177 , pp. 229-234
    • Zaborina, O.1    Latus, M.2    Eberspächer, J.3    Golovleva, L.A.4    Lingens, K.5


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