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Volumn 181, Issue 16, 1999, Pages 4812-4817

Catalytic properties of the 3-chlorocatechol-oxidizing 2,3- dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIHYDROXYBIPHENYL 1,2 DIOXYGENASE; 3 CHLOROCATECHOL; BACTERIAL ENZYME; CATECHOL DERIVATIVE; OXYGENASE; UNCLASSIFIED DRUG;

EID: 0032838290     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.16.4812-4817.1999     Document Type: Article
Times cited : (18)

References (30)
  • 1
    • 0026558894 scopus 로고
    • Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating
    • Adams, R. H., C.-M. Huang, F. K. Higson, V. Brenner, and D. D. Focht. 1992. Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating. Appl. Environ. Microbiol. 58:647-652.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 647-652
    • Adams, R.H.1    Huang, C.-M.2    Higson, F.K.3    Brenner, V.4    Focht, D.D.5
  • 2
    • 0028276797 scopus 로고
    • Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in R. globerulus P6
    • Asturias, J. A., L. D. Eltis, M. Prucha, and K. N. Timmis. 1994. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in R. globerulus P6. J. Biol. Chem. 269:7807-7815.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7807-7815
    • Asturias, J.A.1    Eltis, L.D.2    Prucha, M.3    Timmis, K.N.4
  • 3
    • 0027250341 scopus 로고
    • Three different 2,3-dihydroxybiphenyl 1,2-dioxygenase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rhodococcus globenilus P6
    • Asturias, J. A., and K. N. Timmis. 1993. Three different 2,3-dihydroxybiphenyl 1,2-dioxygenase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rhodococcus globenilus P6. J. Bacteriol. 175:4631-4640.
    • (1993) J. Bacteriol. , vol.175 , pp. 4631-4640
    • Asturias, J.A.1    Timmis, K.N.2
  • 4
    • 0021330498 scopus 로고
    • Suicide inactivation of catechol 2,3-dioxygenase from P. putida mt-2 by 3-halocatechols
    • Bartels, I., H.-J. Knackmuss, and W. Reineke. 1984. Suicide inactivation of catechol 2,3-dioxygenase from P. putida mt-2 by 3-halocatechols. Appl. Environ. Microbiol. 47:500-505.
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 500-505
    • Bartels, I.1    Knackmuss, H.-J.2    Reineke, W.3
  • 5
    • 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., A. Wasserfallen, M. Rekik, K. N. Timmis, and S. Harayama. 1994. Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth. J. Bacteriol. 176:6074-6081.
    • (1994) J. Bacteriol. , vol.176 , pp. 6074-6081
    • Cerdan, P.1    Wasserfallen, A.2    Rekik, M.3    Timmis, K.N.4    Harayama, S.5
  • 6
    • 0028948295 scopus 로고
    • Substrate specificity differences between two catechol 2,3-dioxygenases encoded by the TOL and NAH plasmids from Pseudomonas putida
    • Cerdan, P., M. Rekik, and S. Harayama. 1995. Substrate specificity differences between two catechol 2,3-dioxygenases encoded by the TOL and NAH plasmids from Pseudomonas putida. Eur. J. Biochem. 229:113-118.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 113-118
    • Cerdan, P.1    Rekik, M.2    Harayama, S.3
  • 7
    • 0025274612 scopus 로고
    • Streptomyces promoter-probe plasmids that utilise the xylE gene of Pseudomonas putida
    • Clayton, T. M., and M. J. Bibb. 1990. Streptomyces promoter-probe plasmids that utilise the xylE gene of Pseudomonas putida. Nucleic Acids Res. 18:1077.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1077
    • Clayton, T.M.1    Bibb, M.J.2
  • 8
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis, L. D., and J. T. Bolin. 1996. Evolutionary relationships among extradiol dioxygenases. J. Bacteriol. 178:5930-5937.
    • (1996) J. Bacteriol. , vol.178 , pp. 5930-5937
    • Eltis, L.D.1    Bolin, J.T.2
  • 10
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., L. D. Eltis, K. N. Timmis, S. W. Muchmore, and J. T. Bolin. 1995. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270:976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 11
    • 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., L. D. Eltis, H. Poth, R. Hedderich, and K. N. Timmis. 1993. 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) J. Bacteriol. , vol.175 , pp. 7313-7320
    • Happe, B.1    Eltis, L.D.2    Poth, H.3    Hedderich, R.4    Timmis, K.N.5
  • 12
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., M. Kok, and E. L. Neidle. 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    Neidle, E.L.3
  • 13
    • 0024451702 scopus 로고
    • Bacterial aromatic ring-cleavage enzymes are classified into two different gene families
    • Harayama, S., and M. Rekik. 1989. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 264: 15328-15333.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15328-15333
    • Harayama, S.1    Rekik, M.2
  • 14
    • 1842328640 scopus 로고    scopus 로고
    • Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad
    • Heiss, G., C. Müller, J. Altenbuchner, and A. Stolz. 1997. Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad. Microbiology 143:1691-1699.
    • (1997) Microbiology , vol.143 , pp. 1691-1699
    • Heiss, G.1    Müller, C.2    Altenbuchner, J.3    Stolz, A.4
  • 15
    • 0028840818 scopus 로고
    • Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalenesulfonate-degrading bacterium strain BN6
    • Heiss, G., A. Stolz, A. E. Kuhm, C. Müller, J. Klein, J. Altenbuchner, and H.-J. Knackmuss. 1995. Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalenesulfonate-degrading bacterium strain BN6. J. Bacteriol. 177:5865-5871.
    • (1995) J. Bacteriol. , vol.177 , pp. 5865-5871
    • Heiss, G.1    Stolz, A.2    Kuhm, A.E.3    Müller, C.4    Klein, J.5    Altenbuchner, J.6    Knackmuss, H.-J.7
  • 16
    • 0031936515 scopus 로고    scopus 로고
    • Degradation of chloroaromatics: Purification and characterization of a novel type of chlorocatechol 2,3-dioxygenase of Pseudomonas putida GJ31
    • Kaschabek, S. R., T. Kasberg, D. Müller, A. E. Mars, D. B. Janssen, and W. Reineke. 1998. Degradation of chloroaromatics: purification and characterization of a novel type of chlorocatechol 2,3-dioxygenase of Pseudomonas putida GJ31. J. Bacteriol. 180:296-302.
    • (1998) J. Bacteriol. , vol.180 , pp. 296-302
    • Kaschabek, S.R.1    Kasberg, T.2    Müller, D.3    Mars, A.E.4    Janssen, D.B.5    Reineke, W.6
  • 18
    • 0019457548 scopus 로고
    • Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-chlorocatechol
    • Klecks, G. M., and D. T. Gibson. 1981. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-chlorocatechol. Appl. Environ. Microbiol. 41:1159-1165.
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 1159-1165
    • Klecks, G.M.1    Gibson, D.T.2
  • 19
    • 0025773011 scopus 로고
    • Purification and characterization of a 1,2-dihydroxynaptithalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids
    • Kuhm, A. E., A. Stolz, K.-L. Ngai, and H.-J. Knackmuss. 1991. Purification and characterization of a 1,2-dihydroxynaptithalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J. Bacteriol. 173:3795-3802.
    • (1991) J. Bacteriol. , vol.173 , pp. 3795-3802
    • Kuhm, A.E.1    Stolz, A.2    Ngai, K.-L.3    Knackmuss, H.-J.4
  • 20
    • 0030743522 scopus 로고    scopus 로고
    • Microbial degradation of chloroaromatics: Use of the mew-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 mew-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
  • 21
    • 0023667753 scopus 로고
    • Redesigning metabolic routes: Manipulation of TOL plasmid pathway for catabolism of alkylbenzoates
    • Ramos, J. L., A. Wasserfallen, K. Rose, and K. N. Timmis. 1987. Redesigning metabolic routes: Manipulation of TOL plasmid pathway for catabolism of alkylbenzoates. Science 235:593-596.
    • (1987) Science , vol.235 , pp. 593-596
    • Ramos, J.L.1    Wasserfallen, A.2    Rose, K.3    Timmis, K.N.4
  • 22
    • 0032461201 scopus 로고    scopus 로고
    • Distal cleavage of 3-chlorocatechol to 3-chloro-2-hydroxymuconic semialdehyde by an extradiol dioxygenase
    • Riegert, U., G. Heiss, P. Fischer, and A. Stolz. 1998. Distal cleavage of 3-chlorocatechol to 3-chloro-2-hydroxymuconic semialdehyde by an extradiol dioxygenase. J. Bacteriol. 180:2849-2853.
    • (1998) J. Bacteriol. , vol.180 , pp. 2849-2853
    • Riegert, U.1    Heiss, G.2    Fischer, P.3    Stolz, A.4
  • 23
    • 0023644204 scopus 로고
    • Assemblage of ortho cleavage route for simultaneous degradation of chloro- and methylaromatics
    • Rojo, F., D. H. Pieper, K.-H. Engesser, H.-J. Knackmuss, and K. N. Timmis. 1987. Assemblage of ortho cleavage route for simultaneous degradation of chloro- and methylaromatics. Science 238:1395-1398.
    • (1987) Science , vol.238 , pp. 1395-1398
    • Rojo, F.1    Pieper, D.H.2    Engesser, K.-H.3    Knackmuss, H.-J.4    Timmis, K.N.5
  • 24
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. Strain KKS102
    • Senda, T., K. Sugiyama, H. Narita, T. Yamamoto, K. Kimbara, M. Fukuda, M. Sato, K. Yano, and Y. Mitsui. 1996. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J. Mol. Biol. 255:735-752.
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 25
    • 0029038688 scopus 로고
    • X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism
    • Shu, L., Y.-M. Chiou, A. M. Orville, M. A. Miller, J. D. Lipscomb, and L. Que, Jr. 1995. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry 34:6649-6659.
    • (1995) Biochemistry , vol.34 , pp. 6649-6659
    • Shu, L.1    Chiou, Y.-M.2    Orville, A.M.3    Miller, M.A.4    Lipscomb, J.D.5    Que L., Jr.6
  • 26
    • 0029789393 scopus 로고    scopus 로고
    • Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (Mpcl): Sequence analysis and biochemical properties of a third family of extradiol dioxygenases
    • Spence, E. L., M. Kawamukai, J. Sanvolsin, H. Braven, and T. D. H. Bugg. 1996. Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (Mpcl): sequence analysis and biochemical properties of a third family of extradiol dioxygenases. J. Bacteriol. 178:5249-5256.
    • (1996) J. Bacteriol. , vol.178 , pp. 5249-5256
    • Spence, E.L.1    Kawamukai, M.2    Sanvolsin, J.3    Braven, H.4    Bugg, T.D.H.5
  • 27
    • 0000441068 scopus 로고
    • Biodegradability of mixtures of chloro-and methylsubstituted aromatics: Simultaneous degradation of 3-chlorobenzoate and 3-methylbenzoate
    • Taeger, K., H.-J. Knackmuss, and E. Schmidt. 1988. Biodegradability of mixtures of chloro-and methylsubstituted aromatics: simultaneous degradation of 3-chlorobenzoate and 3-methylbenzoate. Appl. Microbiol. Biotechnol. 28:603-608.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 603-608
    • Taeger, K.1    Knackmuss, H.-J.2    Schmidt, E.3
  • 28
    • 0001311360 scopus 로고
    • Principles of enzyme assays and kinetic studies
    • R. Eisenthal and M. J. Danson (ed.), IRL Press, New York, N.Y.
    • Tipton, K. F. 1992. Principles of enzyme assays and kinetic studies, p. 1-24. In R. Eisenthal and M. J. Danson (ed.), Enzyme assays. A practical approach. IRL Press, New York, N.Y.
    • (1992) Enzyme Assays. A Practical Approach , pp. 1-24
    • Tipton, K.F.1
  • 29
    • 0018993834 scopus 로고
    • Kinetics of suicide substrates
    • Waley, S. G. 1980. Kinetics of suicide substrates. Biochem. J. 185:771-773.
    • (1980) Biochem. J. , vol.185 , pp. 771-773
    • Waley, S.G.1
  • 30
    • 14744273210 scopus 로고
    • A Pseudomonas putida strain able to degrade m-toluate in the presence of 3-chlorocatechol
    • Wasserfallen, A., M. Rekik, and S. Harayama. 1991. A Pseudomonas putida strain able to degrade m-toluate in the presence of 3-chlorocatechol. Bio/Technology 9:296-298.
    • (1991) Bio/Technology , vol.9 , pp. 296-298
    • Wasserfallen, A.1    Rekik, M.2    Harayama, S.3


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