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Volumn 179, Issue 16, 1997, Pages 5226-5231

Cloning and characterization of two catA genes in Acinetobacter lwoffii K24

Author keywords

[No Author keywords available]

Indexed keywords

ACINETOBACTER; AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME INDUCTION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; GENE LOCATION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL;

EID: 0001134355     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.16.5226-5231.1997     Document Type: Article
Times cited : (52)

References (35)
  • 1
    • 0023967997 scopus 로고
    • Transcriptionai regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida
    • Aldrich, T. L., and A. M. Chakrabarty. 1988. Transcriptionai regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida. J. Bacteriol. 170:1297-1304.
    • (1988) J. Bacteriol. , vol.170 , pp. 1297-1304
    • Aldrich, T.L.1    Chakrabarty, A.M.2
  • 2
    • 0023216678 scopus 로고
    • Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme
    • Aldrich, T. L., B. Frantz, J. F. Gill, J. J. Kilbane, and A. M. Chakrabarty. 1987. Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme. Gene 52:185-195.
    • (1987) Gene , vol.52 , pp. 185-195
    • Aldrich, T.L.1    Frantz, B.2    Gill, J.F.3    Kilbane, J.J.4    Chakrabarty, A.M.5
  • 3
    • 0000558072 scopus 로고
    • Purification and characterization of catechol 1,2-dioxygenase from aniline-assimilating Rhodococcus erythropolis AN-13
    • Aoki, K., T. Konohana, R. Shinke, and H. Nishira. 1984. Purification and characterization of catechol 1,2-dioxygenase from aniline-assimilating Rhodococcus erythropolis AN-13. Agric. Biol. Chem. 48:2087-2095.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2087-2095
    • Aoki, K.1    Konohana, T.2    Shinke, R.3    Nishira, H.4
  • 4
    • 0000751731 scopus 로고
    • Two catechol. 1,2-dioxygenases from an aniline-assimilating bacterium, Frateuria species ANA-18
    • Aoki, K., T. Konohana, R. Shinke, and H. Nishira. 1984. Two catechol. 1,2-dioxygenases from an aniline-assimilating bacterium, Frateuria species ANA-18. Agric. Biol. Chem. 47:2097-2104.
    • (1984) Agric. Biol. Chem. , vol.47 , pp. 2097-2104
    • Aoki, K.1    Konohana, T.2    Shinke, R.3    Nishira, H.4
  • 6
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantification of micrugram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. Rapid and sensitive method for the quantification of micrugram 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
  • 7
    • 0025827638 scopus 로고
    • Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance
    • Broderick, J. B., and T. V. O'Halloran. 1991. Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance. Biochemistry 30:7349-7358.
    • (1991) Biochemistry , vol.30 , pp. 7349-7358
    • Broderick, J.B.1    O'Halloran, T.V.2
  • 8
    • 0017895519 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds
    • Dorn, E., and H.-J. Knackmuss. 1978. Chemical structure and biodegradability of halogenated aromatic compounds. Biochem. J. 174:73-84.
    • (1978) Biochem. J. , vol.174 , pp. 73-84
    • Dorn, E.1    Knackmuss, H.-J.2
  • 9
    • 0027391396 scopus 로고
    • Cloning and characterization of a gene coding for the catechol 1,2-dioxygenase of Arthrobacter sp. mA3
    • Erk, R., and J. Belter. 1993. Cloning and characterization of a gene coding for the catechol 1,2-dioxygenase of Arthrobacter sp. mA3. Gene 123:87-92.
    • (1993) Gene , vol.123 , pp. 87-92
    • Erk, R.1    Belter, J.2
  • 10
    • 0023374169 scopus 로고
    • Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation
    • Frantz, B., and A. M. Chakrabarty. 1987. Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation. Proc. Natl. Acad. Sci. USA 84:4460-4464.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4460-4464
    • Frantz, B.1    Chakrabarty, A.M.2
  • 11
    • 0027508335 scopus 로고
    • Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes
    • Frazee, R. W., D. M. Livingston, D. C. Laporte, and J. D. Lipscomb. 1993. Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes. J. Bacteriol. 175:6194-6202.
    • (1993) J. Bacteriol. , vol.175 , pp. 6194-6202
    • Frazee, R.W.1    Livingston, D.M.2    Laporte, D.C.3    Lipscomb, J.D.4
  • 12
    • 0016806798 scopus 로고
    • Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechuase, from a Pseudomonad
    • Fujiwara, M., L. A. Golovieva, Y. Saeki, M. Nozaki, and O. Hayaishi. 1975. Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechuase, from a Pseudomonad. J. Biol. Chem. 250:4848-4855.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4848-4855
    • Fujiwara, M.1    Golovieva, L.A.2    Saeki, Y.3    Nozaki, M.4    Hayaishi, O.5
  • 13
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., and M. Kok. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2
  • 14
    • 0026705490 scopus 로고
    • Characterization of isofunctional ring-cleavage enzymes in aniline and 3-chloroamhne degradation by Pseudomonas acidovorans CA28
    • Hinteregger, C., M. Loidi, and F. Streichsbier. 1992. Characterization of isofunctional ring-cleavage enzymes in aniline and 3-chloroamhne degradation by Pseudomonas acidovorans CA28. FEMS Microbiol. Lett. 97:261-266.
    • (1992) FEMS Microbiol. Lett. , vol.97 , pp. 261-266
    • Hinteregger, C.1    Loidi, M.2    Streichsbier, F.3
  • 16
  • 18
    • 0025979874 scopus 로고
    • Sequence of the plasmid-encoded catechol 1,2-dioxygenase-expressing gene, pheB, of phenol-degrading Pseudomonas Sp. strain EST1001
    • Kivisaar, M., L. Kasak, and A. Murk. 1991. Sequence of the plasmid-encoded catechol 1,2-dioxygenase-expressing gene, pheB, of phenol-degrading Pseudomonas Sp. strain EST1001. Gene 98:15-20.
    • (1991) Gene , vol.98 , pp. 15-20
    • Kivisaar, M.1    Kasak, L.2    Murk, A.3
  • 20
    • 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
  • 22
    • 0029112780 scopus 로고
    • Cloning, DNA sequencing, and amino acid sequencing of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 and Pseudomonas arvilla C-1
    • Nakai, C., H. Uyeyama, H. Kagamiyama, T. Nakazawa, S. Inouye, F. Kishi, A. Nakazawa, and M. Nozaki. 1995. Cloning, DNA sequencing, and amino acid sequencing of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 and Pseudomonas arvilla C-1. Arch. Biochem. Biophys.
    • (1995) Arch. Biochem. Biophys.
    • Nakai, C.1    Uyeyama, H.2    Kagamiyama, H.3    Nakazawa, T.4    Inouye, S.5    Kishi, F.6    Nakazawa, A.7    Nozaki, M.8
  • 23
    • 0025159432 scopus 로고
    • Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, ββ, from Pseudomonas arvilla C-1
    • Nakai, C., K. Horiike, S. Kuramitsu, H. Kagamiyama, and M. Nozaki. 1990. Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, 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
  • 24
    • 0024258298 scopus 로고
    • Purification and properties ot 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 ot 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
  • 25
    • 0024094638 scopus 로고
    • DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: Evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions
    • Neidle, E. L., C. Hartnett, S. Bonitz, and L. N. Ornston. 1988. DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions. J. Bacteriol. 170:4874-4880
    • (1988) J. Bacteriol. , vol.170 , pp. 4874-4880
    • Neidle, E.L.1    Hartnett, C.2    Bonitz, S.3    Ornston, L.N.4
  • 26
    • 0024463460 scopus 로고
    • Characterization of Acinetobacter calcoaceticus catM, a repressor gene homologous in sequence to transcriptional activator genes
    • Neidle, E. L., C. Hartnett, and L. N. Ornston. 1989. Characterization of Acinetobacter calcoaceticus catM, a repressor gene homologous in sequence to transcriptional activator genes. J. Bacteriol. 171:5410-5421.
    • (1989) J. Bacteriol. , vol.171 , pp. 5410-5421
    • Neidle, E.L.1    Hartnett, C.2    Ornston, L.N.3
  • 27
    • 0023022814 scopus 로고
    • Cloning and expression of Acinetobacter calcoaceticus catechol 1,2-dioxygenase structural gene catA in Escherichia coli
    • Neidle, E. L., and L. N. Ornston. 1986. Cloning and expression of Acinetobacter calcoaceticus catechol 1,2-dioxygenase structural gene catA in Escherichia coli. J. Bacteriol. 168:815-820.
    • (1986) J. Bacteriol. , vol.168 , pp. 815-820
    • Neidle, E.L.1    Ornston, L.N.2
  • 28
    • 77956993726 scopus 로고
    • Metapyrocatechase (Pseudomonas)
    • Nozaki, M. 1970. Metapyrocatechase (Pseudomonas). Methods Enzymol. 17A:522-525.
    • (1970) Methods Enzymol. , vol.17 A , pp. 522-525
    • Nozaki, M.1
  • 29
    • 0014027888 scopus 로고
    • The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. I. Biochemistry
    • Ornston, L. N., and R. Y. Stanier. 1966. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. I. Biochemistry. J. Biol. Chem. 241:3776-3786.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3776-3786
    • Ornston, L.N.1    Stanier, R.Y.2
  • 30
    • 0026495342 scopus 로고
    • Roles of catR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida
    • Parsek, M. R., D. L. Shinabarger, R. K. Rothmel, and A. M. Chakrabarty. 1992. Roles of catR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida. J. Bacteriol. 174:7798-7806.
    • (1992) J. Bacteriol. , vol.174 , pp. 7798-7806
    • Parsek, M.R.1    Shinabarger, D.L.2    Rothmel, R.K.3    Chakrabarty, A.M.4
  • 31
    • 0017080224 scopus 로고
    • Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: Purification and properties
    • Patel, R. N., C. T. Hou, A. Felix, and M. O. Lillard. 1976. Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties. J. Bacteriol. 127:536-544.
    • (1976) J. Bacteriol. , vol.127 , pp. 536-544
    • Patel, R.N.1    Hou, C.T.2    Felix, A.3    Lillard, M.O.4
  • 32
    • 0025357079 scopus 로고
    • Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4
    • Perkins, E. J., M. P. Gordon, O. Caceres, and P. F. Lurquin. 1990. Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4. J. Bacteriol. 172:2351-2359.
    • (1990) J. Bacteriol. , vol.172 , pp. 2351-2359
    • Perkins, E.J.1    Gordon, M.P.2    Caceres, O.3    Lurquin, P.F.4
  • 34
    • 0022541362 scopus 로고
    • Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coll
    • Shanley, M. S., E. L. Neidle, R. E. Parales, and L. N. Ornston. 1986. Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coll. J. Bacteriol. 165:557-563.
    • (1986) J. Bacteriol. , vol.165 , pp. 557-563
    • Shanley, M.S.1    Neidle, E.L.2    Parales, R.E.3    Ornston, L.N.4
  • 35
    • 0025806414 scopus 로고
    • Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: Evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates
    • van der Meer, J. R., R. I. L. Eggen, A. J. B. Zehnder, and W. M. de Vos. 1991. Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates. J. Bacteriol. 173:2425-2434.
    • (1991) J. Bacteriol. , vol.173 , pp. 2425-2434
    • Van Der Meer, J.R.1    Eggen, R.I.L.2    Zehnder, A.J.B.3    De Vos, W.M.4


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