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Volumn 34, Issue , 1999, Pages 173-189

Catechol dioxygenases

Author keywords

[No Author keywords available]

Indexed keywords

BENZOIC ACID DERIVATIVE; CATECHOL DERIVATIVE; OXYGENASE;

EID: 0033289158     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/bse0340173     Document Type: Article
Times cited : (92)

References (41)
  • 1
    • 0001615959 scopus 로고
    • Mechanistic aspects of dihydroxybenzoate dioxygenases
    • Lipscomb, J.D. & Orville, A.M. (1992) Mechanistic aspects of dihydroxybenzoate dioxygenases. Met Ions Biol. Syst. 28, 243-298
    • (1992) Met Ions Biol. Syst. , vol.28 , pp. 243-298
    • Lipscomb, J.D.1    Orville, A.M.2
  • 2
    • 0002253441 scopus 로고
    • Oxygen activation at nonheme iron centres
    • Reedijk, J., ed., Marcel Dekker, New York
    • Que, Jr., L. (1989) Oxygen activation at nonheme iron centres. In Bioinorgonic Catalysis (Reedijk, J., ed.), pp. 347-393, Marcel Dekker, New York
    • (1989) Bioinorgonic Catalysis , pp. 347-393
    • Que Jr., L.1
  • 3
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que, Jr., L. & Ho, R.Y.N. (1996) Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem. Rev. 96, 2607-2624
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que Jr., L.1    Ho, R.Y.N.2
  • 4
    • 0014605052 scopus 로고
    • Regulation of the meta cleavage pathway for benzoate oxidation by Pseudomonas putida
    • Feist, C.F. & Hegeman, G.D. (1969) Regulation of the meta cleavage pathway for benzoate oxidation by Pseudomonas putida. J. Bacteriol. 100, 1121-1123
    • (1969) J. Bacteriol. , vol.100 , pp. 1121-1123
    • Feist, C.F.1    Hegeman, G.D.2
  • 5
    • 0014027888 scopus 로고
    • The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida
    • Ornston, L.N. & Stanier, R.Y. (1966) The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. J. Biol. Chem. 241, 3776-3786
    • (1966) J. Biol. Chem. , vol.241 , pp. 3776-3786
    • Ornston, L.N.1    Stanier, R.Y.2
  • 6
    • 0021099237 scopus 로고
    • Purification, subunit structure, and partial amino acid sequence of metapyrocatechase
    • Nakai, C., Hori, K., Kagamiyama, H., Nakazawa, T. & Nozaki, M. (1983) Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem. 258, 2916-2922
    • (1983) J. Biol. Chem. , vol.258 , pp. 2916-2922
    • Nakai, C.1    Hori, K.2    Kagamiyama, H.3    Nakazawa, T.4    Nozaki, M.5
  • 7
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the tol plasmid of Pseudomonas putida mt-2
    • Nakai, C., Kagamiyama, H., Nozaki, M., Nakazawa, T., Inouye, S., Evina, Y. & Nakazawa, A. (1983) Complete nucleotide sequence of the metapyrocatechase gene on the tol plasmid of Pseudomonas putida mt-2. J. Biol. Chem. 258, 2923-2928
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Evina, Y.6    Nakazawa, A.7
  • 8
    • 0021112843 scopus 로고
    • EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase: Characterization of a new Fe(II) environment
    • Arciero, D.M., Lipscomb, J.D., Huynh, B.H., Kent, T.A. & Münck, E. (1983) EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase: characterization of a new Fe(II) environment. J. Biol. Chem. 258, 14981-14991
    • (1983) J. Biol. Chem. , vol.258 , pp. 14981-14991
    • Arciero, D.M.1    Lipscomb, J.D.2    Huynh, B.H.3    Kent, T.A.4    Münck, E.5
  • 10
  • 11
    • 0023823389 scopus 로고
    • Reductive dechlorination of polychlorinated biphenyls by anaerobic microorganisms from sediments
    • Quensen, III, J.F., Tiedje, J.M. & Boyd, S.A. (1988) Reductive dechlorination of polychlorinated biphenyls by anaerobic microorganisms from sediments. Science 242, 752-754
    • (1988) Science , vol.242 , pp. 752-754
    • Quensen III, J.F.1    Tiedje, J.M.2    Boyd, S.A.3
  • 12
    • 0019481141 scopus 로고
    • Plasmid specifying total degradation of 3-chlorobenzoate by a modified ortho pathway
    • Chatterjee, D.K., Kellogg, S.T., Hamada, S. & Chakrabarty, A.M. (1981) Plasmid specifying total degradation of 3-chlorobenzoate by a modified ortho pathway. J. Bacteriol. 146, 639-646
    • (1981) J. Bacteriol. , vol.146 , pp. 639-646
    • Chatterjee, D.K.1    Kellogg, S.T.2    Hamada, S.3    Chakrabarty, A.M.4
  • 13
    • 0025827638 scopus 로고
    • Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance
    • Broderick, J. & O'Halloran, T.V. (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.1    O'Halloran, T.V.2
  • 14
    • 0007683197 scopus 로고
    • Resonance Raman spectra of protocatechuate 3,4-dioxygenase. Evidence for coordination of tyrosine residue to ferric iron
    • Tatsuno, Y. & Saeki, Y. (1978) Resonance Raman spectra of protocatechuate 3,4-dioxygenase. Evidence for coordination of tyrosine residue to ferric iron. J. Am. Chem. Soc. 100, 4614-4615
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 4614-4615
    • Tatsuno, Y.1    Saeki, Y.2
  • 15
    • 0019321240 scopus 로고
    • Resonance Raman studies of pyrocatechase-inhibitor complexes
    • Que, Jr., L., Heistand, R.H. II, Mayer, R., & Roe, A.L. (1980) Resonance Raman studies of pyrocatechase-inhibitor complexes. Biochemistry 19, 2588-2593
    • (1980) Biochemistry , vol.19 , pp. 2588-2593
    • Que Jr., L.1    Heistand II, R.H.2    Mayer, R.3    Roe, A.L.4
  • 16
    • 0019890089 scopus 로고
    • Resonance Raman studies on protocatechuate 3,4-dioxygenase-inhibitor complexes
    • Que, Jr., L. & Epstein, R.M. (1981) Resonance Raman studies on protocatechuate 3,4-dioxygenase-inhibitor complexes. Biochemistry 20, 2545-2549
    • (1981) Biochemistry , vol.20 , pp. 2545-2549
    • Que Jr., L.1    Epstein, R.M.2
  • 17
    • 0007653243 scopus 로고
    • EXAFS and Raman evidence for histidine binding at the active site of protocatechuate 3,4-dioxygenase
    • Felton, R.H., Barrow, W.L., May, S.W., Sowell, A.L., Goel, S., Bunker, G. & Stern, E.A. (1982) EXAFS and Raman evidence for histidine binding at the active site of protocatechuate 3,4-dioxygenase. J. Am. Chem. Soc. 104, 6132-6134
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6132-6134
    • Felton, R.H.1    Barrow, W.L.2    May, S.W.3    Sowell, A.L.4    Goel, S.5    Bunker, G.6    Stern, E.A.7
  • 18
    • 0023221645 scopus 로고
    • Elucidation of the coordination chemistry of the enzyme-substrate complex of catechol 1,2-dioxygenase by NMR spectroscopy
    • Que, Jr., L., Lauffer, R.B., Lynch, J.B., Murch, B.P. & Pyrz, J.W. (1987) Elucidation of the coordination chemistry of the enzyme-substrate complex of catechol 1,2-dioxygenase by NMR spectroscopy. J. Am. Chem. Soc. 109, 5381-5385
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5381-5385
    • Que Jr., L.1    Lauffer, R.B.2    Lynch, J.B.3    Murch, B.P.4    Pyrz, J.W.5
  • 19
    • 0007186793 scopus 로고
    • Resonance Raman studies on pyrocatechase
    • Que, Jr., L. & Heistand, II, R.H. (1979) Resonance Raman studies on pyrocatechase. J. Am. Chem. Soc. 101, 2219-2221
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 2219-2221
    • Que Jr., L.1    Heistand II, R.H.2
  • 20
    • 0024328715 scopus 로고
    • Binding of isotopically labelled substrates, inhibitors, and cyanide by protocatechuate 3,4-dioxygenase
    • Orville, A.M. & Lipscomb, J.D. (1989) Binding of isotopically labelled substrates, inhibitors, and cyanide by protocatechuate 3,4-dioxygenase. J. Biol. Chem. 264, 8791-8801
    • (1989) J. Biol. Chem. , vol.264 , pp. 8791-8801
    • Orville, A.M.1    Lipscomb, J.D.2
  • 21
    • 0021288266 scopus 로고
    • 17O-Water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase: Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs
    • 17O-Water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase: evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs. J. Biol. Chem. 259, 4487-4495
    • (1984) J. Biol. Chem. , vol.259 , pp. 4487-4495
    • Whittaker, J.W.1    Lipscomb, J.D.2
  • 22
    • 0025633650 scopus 로고
    • An EXAFS study of the interaction of substrate with the ferric active site of protocatechuate 3,4-dioxygenase
    • True, A.E., Orville, A.M., Pearce, LL, Lipscomb, J.D. & Que, Jr., L. (1990) An EXAFS study of the interaction of substrate with the ferric active site of protocatechuate 3,4-dioxygenase. Biochemistry 29, 10847-10854
    • (1990) Biochemistry , vol.29 , pp. 10847-10854
    • True, A.E.1    Orville, A.M.2    Pearce, L.L.3    Lipscomb, J.D.4    Que Jr., L.5
  • 23
    • 0021275478 scopus 로고
    • Brevibacterium fuscum protocatechuate 3,4-dioxygenase: Purification, crystallization, and characterization
    • Whittaker, J.W., Lipscomb, J.D., Kent, T.A. & Münck, E. (1984) Brevibacterium fuscum protocatechuate 3,4-dioxygenase: purification, crystallization, and characterization. J. Biol. Chem. 259, 4466-4475
    • (1984) J. Biol. Chem. , vol.259 , pp. 4466-4475
    • Whittaker, J.W.1    Lipscomb, J.D.2    Kent, T.A.3    Münck, E.4
  • 24
    • 33845281032 scopus 로고
    • Mössbauer and EPR spectroscopy of catechol 1,2-dioxygenase
    • Kent, T.A., Münck, E., Pyrz, J.W. & Que, Jr., L. (1987) Mössbauer and EPR spectroscopy of catechol 1,2-dioxygenase. Inorg. Chem. 26, 1402-1408
    • (1987) Inorg. Chem. , vol.26 , pp. 1402-1408
    • Kent, T.A.1    Münck, E.2    Pyrz, J.W.3    Que Jr., L.4
  • 25
    • 0347030825 scopus 로고
    • Ph.D. dissertation. Northwestern University
    • Broderick, J.B. (1992) Ph.D. dissertation. Northwestern University
    • (1992)
    • Broderick, J.B.1
  • 26
    • 0019772728 scopus 로고
    • The reaction of oxygen with protocatechuate 3,4-dioxygenase from Pseudomonas putida
    • Bull, C., Ballou, D.P. & Otsuka, S. (1981) The reaction of oxygen with protocatechuate 3,4-dioxygenase from Pseudomonas putida. J. Biol. Chem. 256, 12681-12686
    • (1981) J. Biol. Chem. , vol.256 , pp. 12681-12686
    • Bull, C.1    Ballou, D.P.2    Otsuka, S.3
  • 27
    • 0021100507 scopus 로고
    • Rapid reaction studies on the oxygenation reactions of catechol dioxygenase
    • Walsh, T.A., Ballou, D.P., Mayer, R. & Que, Jr., L. (1983) Rapid reaction studies on the oxygenation reactions of catechol dioxygenase. J. Biol. Chem. 258, 14422-14427
    • (1983) J. Biol. Chem. , vol.258 , pp. 14422-14427
    • Walsh, T.A.1    Ballou, D.P.2    Mayer, R.3    Que Jr., L.4
  • 28
    • 0024296029 scopus 로고
    • Structure and assembly of protocatechuate 3,4-dioxygenase
    • Ohlendorf, D.H., Lipscomb, J.D. & Weber, P.C. (1988) Structure and assembly of protocatechuate 3,4-dioxygenase. Nature (London) 336, 403-405
    • (1988) Nature (London) , vol.336 , pp. 403-405
    • Ohlendorf, D.H.1    Lipscomb, J.D.2    Weber, P.C.3
  • 29
    • 0030874393 scopus 로고    scopus 로고
    • Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: Multiple exogenous ligand binding orientations within the active site
    • Orville, A.M., Elango, N., Lipscomb, J.D. & Ohlendorf, D.H. (1997) Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site. Biochemistry 36, 10039-10051
    • (1997) Biochemistry , vol.36 , pp. 10039-10051
    • Orville, A.M.1    Elango, N.2    Lipscomb, J.D.3    Ohlendorf, D.H.4
  • 31
    • 0000006176 scopus 로고
    • Variable-temperature variable-field magnetic circular dichroism studies of the Fe(II) active site in metapyrocatechase: Implications for the molecular mechanism of extradiol dioxygenases
    • Mabrouk, P.A., Orville, A.M., Lipscomb, J.D. & Solomon, E.I. (1991) Variable-temperature variable-field magnetic circular dichroism studies of the Fe(II) active site in metapyrocatechase: implications for the molecular mechanism of extradiol dioxygenases. J. Am. Chem. Soc. 113, 4053-4061
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4053-4061
    • Mabrouk, P.A.1    Orville, A.M.2    Lipscomb, J.D.3    Solomon, E.I.4
  • 32
    • 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., Chiou, Y.-M., Orville, A.M., Miller, M.A., Lipscomb, J.D. & Que, Jr., L. (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 Jr., L.6
  • 33
    • 0028838765 scopus 로고
    • Evidence of histidine coordination to the catalytic ferrous ion in the ring-cleaving 2,2′,3-trihydroxybiphenyl dioxygenase from the dibenzofuran-degrading bacterium Sphingomonas sp. strain RWI
    • Bertini, I., Capozzi, F., Dikiy, A., Happe, B., Luchinat, C. & Timmis, K.M. (1995) Evidence of histidine coordination to the catalytic ferrous ion in the ring-cleaving 2,2′,3-trihydroxybiphenyl dioxygenase from the dibenzofuran-degrading bacterium Sphingomonas sp. strain RWI. Biochem. Biophys. Res. Commun. 215, 855-860
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 855-860
    • Bertini, I.1    Capozzi, F.2    Dikiy, A.3    Happe, B.4    Luchinat, C.5    Timmis, K.M.6
  • 34
    • 0022270779 scopus 로고
    • 17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase: Evidence for binding of exogenous ligands to the active site Fe(II) of extradiol dioxygenases
    • 17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase: evidence for binding of exogenous ligands to the active site Fe(II) of extradiol dioxygenases. J. Biol. Chem. 260, 14035-14044
    • (1985) J. Biol. Chem. , vol.260 , pp. 14035-14044
    • Arciero, D.M.1    Orville, A.M.2    Lipscomb, J.D.3
  • 35
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., Eltis, L.D., Timmis, K.N., Muchmore, S.W. & Bolin, J.T. (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
  • 36
    • 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., Sugiyama, K., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Sato, M., Yano, K. & Mitsui, Y. (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
  • 37
    • 0024258298 scopus 로고
    • Purification and preperties of catechol 1,2-dioxygenase from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1
    • Nakai, C.T., Nakazawa, T. & Nozaki, M. (1988) Purification and preperties of catechol 1,2-dioxygenase 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.T.1    Nakazawa, T.2    Nozaki, M.3
  • 38
    • 0014429697 scopus 로고
    • Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization
    • Fujisawa, H. & Hayaishi, O. (1968) Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization. J. Biol. Chem. 243, 2673-2681
    • (1968) J. Biol. Chem. , vol.243 , pp. 2673-2681
    • Fujisawa, H.1    Hayaishi, O.2
  • 39
    • 0016806798 scopus 로고
    • Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase from a pseudomonad
    • Fujiwara, M., Golovleva, L.A., Saeki, Y., Nozaki, M. & Hayaishi, O. (1975) Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase from a pseudomonad. J. Biol. Chem. 250, 4848-4855
    • (1975) J. Biol. Chem. , vol.250 , pp. 4848-4855
    • Fujiwara, M.1    Golovleva, L.A.2    Saeki, Y.3    Nozaki, M.4    Hayaishi, O.5
  • 40
    • 0017814391 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds: Substituent effects on 1,2-dioxygenation of catechol
    • Dorn, E. & Knackmuss, H.-J. (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
  • 41
    • 0001853051 scopus 로고
    • Metabolism of 2,4-dichlorophenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP134
    • Pieper, D.H., Rieneke, W., Engesser, K.-H. & Knackmuss, H.-J. (1988) Metabolism of 2,4-dichlorophenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP134. Arch. Microbiol. 150, 95-102
    • (1988) Arch. Microbiol. , vol.150 , pp. 95-102
    • Pieper, D.H.1    Rieneke, W.2    Engesser, K.-H.3    Knackmuss, H.-J.4


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