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Volumn 52, Issue 38, 2013, Pages 6724-6736

Characterizing the promiscuity of LigAB, a lignin catabolite degrading extradiol dioxygenase from Sphingomonas paucimobilis SYK-6

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYME INHIBITION; LIGNIN;

EID: 84884828733     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400665t     Document Type: Article
Times cited : (53)

References (81)
  • 1
    • 4644249418 scopus 로고    scopus 로고
    • Co-ordination network for lignin - Standardisation, production and applications adapted to market requirements (EUROLIGNIN)
    • Gosselink, R. J. A., de Jong, E., Guran, B., and Abächerli, A. (2004) Co-ordination network for lignin-standardisation, production and applications adapted to market requirements (EUROLIGNIN) Ind. Crops Prod. 20, 121-129
    • (2004) Ind. Crops Prod. , vol.20 , pp. 121-129
    • Gosselink, R.J.A.1    De Jong, E.2    Guran, B.3    Abächerli, A.4
  • 2
    • 0024110310 scopus 로고
    • Bacterial degradation of lignin
    • Vicuña, R. (1988) Bacterial degradation of lignin Enzyme Microb. Technol. 10, 646-655
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 646-655
    • Vicuña, R.1
  • 3
    • 79955761627 scopus 로고    scopus 로고
    • The emerging role for bacteria in lignin degradation and bio-product formation
    • Bugg, T. D. H., Ahmad, M., Hardiman, E. M., and Singh, R. (2010) The emerging role for bacteria in lignin degradation and bio-product formation Curr. Opin. Biotechnol. 22, 1-7
    • (2010) Curr. Opin. Biotechnol. , vol.22 , pp. 1-7
    • Bugg, T.D.H.1    Ahmad, M.2    Hardiman, E.M.3    Singh, R.4
  • 4
    • 0007628347 scopus 로고
    • The metabolism of biphenyl structures in lignin by the soil bacterium (Pseudomonas paucimobilis SYK-6)
    • Katayama, Y., Nishikawa, S., Murayama, A., Yamasaki, M., Morohoshi, N., and Haraguchi, T. (1988) The metabolism of biphenyl structures in lignin by the soil bacterium (Pseudomonas paucimobilis SYK-6) FEBS Lett. 233, 129-133
    • (1988) FEBS Lett. , vol.233 , pp. 129-133
    • Katayama, Y.1    Nishikawa, S.2    Murayama, A.3    Yamasaki, M.4    Morohoshi, N.5    Haraguchi, T.6
  • 5
    • 80054757502 scopus 로고    scopus 로고
    • Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase
    • Machonkin, T. E. and Doerner, A. E. (2011) Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase Biochemistry 50, 8899-8913
    • (2011) Biochemistry , vol.50 , pp. 8899-8913
    • Machonkin, T.E.1    Doerner, A.E.2
  • 8
    • 33745216477 scopus 로고    scopus 로고
    • The role of residue Thr249 in modulating the catalytic efficiency and substrate specificity of catechol-2,3-dioxygenase from Pseudomonas stutzeri OX1
    • Siani, L., Viggiani, A., Notomista, E., Pezzella, A., and Di Donato, A. (2006) The role of residue Thr249 in modulating the catalytic efficiency and substrate specificity of catechol-2,3-dioxygenase from Pseudomonas stutzeri OX1 FEBS J. 273, 2963-2976
    • (2006) FEBS J. , vol.273 , pp. 2963-2976
    • Siani, L.1    Viggiani, A.2    Notomista, E.3    Pezzella, A.4    Di Donato, A.5
  • 9
    • 34247534094 scopus 로고    scopus 로고
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates Science 316, 453-457
    • (2007) Science , vol.316 , pp. 453-457
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 11
    • 31044441352 scopus 로고    scopus 로고
    • Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis
    • Schaab, M. R., Barney, B. M., and Francisco, W. A. (2006) Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis Biochemistry 45, 1009-1016
    • (2006) Biochemistry , vol.45 , pp. 1009-1016
    • Schaab, M.R.1    Barney, B.M.2    Francisco, W.A.3
  • 13
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis, L. D. and Bolin, J. T. (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
  • 14
    • 0029789393 scopus 로고    scopus 로고
    • Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): Sequence analysis and biochemical properties of a third family of extradiol dioxygenases
    • Spence, E. L., Kawamukai, M., Sanvoisin, J., Braven, H., and Bugg, T. D. H. (1996) Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): 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    Sanvoisin, J.3    Braven, H.4    Bugg, T.D.H.5
  • 15
    • 0025296680 scopus 로고
    • Nucleotide sequence of metapyrocatechase i (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222
    • Kabisch, M. and Fortnagel, P. (1990) Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222 Nucleic Acids Res. 18, 3405-3405
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3405-3405
    • Kabisch, M.1    Fortnagel, P.2
  • 16
    • 0025051371 scopus 로고
    • Protocatechuate 4,5-dioxygenase from Pseudomonas testosteroni
    • Arciero, D. M., Orville, A. M., and Lipscomb, J. D. (1990) Protocatechuate 4,5-dioxygenase from Pseudomonas testosteroni Methods Enzymol. 188, 89-95
    • (1990) Methods Enzymol. , vol.188 , pp. 89-95
    • Arciero, D.M.1    Orville, A.M.2    Lipscomb, J.D.3
  • 17
    • 13844289384 scopus 로고    scopus 로고
    • Protocatechuate 4,5-dioxygenase from Comamonas testosteroni T-2: Biochemical and molecular properties of a new subgroup within class III of extradiol dioxygenases
    • Mampel, J., Providenti, M. A., and Cook, A. M. (2005) Protocatechuate 4,5-dioxygenase from Comamonas testosteroni T-2: biochemical and molecular properties of a new subgroup within class III of extradiol dioxygenases Arch. Microbiol. 183, 130-139
    • (2005) Arch. Microbiol. , vol.183 , pp. 130-139
    • Mampel, J.1    Providenti, M.A.2    Cook, A.M.3
  • 18
    • 0027293730 scopus 로고
    • Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: A new extradiol catecholic dioxygenase
    • Wolgel, S. A., Dege, J. E., Perkins-Olson, P. E., Juarez-Garcia, C. H., Crawford, R. L., Munck, E., and Lipscomb, J. D. (1993) Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: A new extradiol catecholic dioxygenase J. Bacteriol. 175, 4414-4426
    • (1993) J. Bacteriol. , vol.175 , pp. 4414-4426
    • Wolgel, S.A.1    Dege, J.E.2    Perkins-Olson, P.E.3    Juarez-Garcia, C.H.4    Crawford, R.L.5    Munck, E.6    Lipscomb, J.D.7
  • 20
    • 0029858048 scopus 로고    scopus 로고
    • 2-Aminophenol 1,6-dioxygenase: A novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45
    • Lendenmann, U. and Spain, J. C. (1996) 2-Aminophenol 1,6-dioxygenase: A novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45 J. Bacteriol. 178, 6227-6232
    • (1996) J. Bacteriol. , vol.178 , pp. 6227-6232
    • Lendenmann, U.1    Spain, J.C.2
  • 21
    • 0032721192 scopus 로고    scopus 로고
    • Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: Divergent evolution of 2-aminophenol meta-cleavage pathway
    • Davis, J. K., He, Z. Q., Somerville, C. C., and Spain, J. C. (1999) Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: divergent evolution of 2-aminophenol meta-cleavage pathway Arch. Microbiol. 172, 330-339
    • (1999) Arch. Microbiol. , vol.172 , pp. 330-339
    • Davis, J.K.1    He, Z.Q.2    Somerville, C.C.3    Spain, J.C.4
  • 22
    • 0030855128 scopus 로고    scopus 로고
    • Cloning of genes involved in carbazole degradation of Pseudomonas sp strain CA10: Nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase
    • Sato, S., Ouchiyama, N., Kimura, T., Nojiri, H., Yamane, H., and Omori, T. (1997) Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: Nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase J. Bacteriol. 179, 4841-4849
    • (1997) J. Bacteriol. , vol.179 , pp. 4841-4849
    • Sato, S.1    Ouchiyama, N.2    Kimura, T.3    Nojiri, H.4    Yamane, H.5    Omori, T.6
  • 23
    • 33646870781 scopus 로고    scopus 로고
    • Expression and homology modelling of 2 ′-aminobiphenyl-2,3-diol-1, 2-dioxygenase from Pseudomonas stutzeri carbazole degradation pathway
    • Larentis, A. L., Almeida, R. V., Rossle, S. C., Cardoso, A. M., Almeida, W. I., Bisch, P. M., Alves, T. L. M., and Martins, O. B. (2006) Expression and homology modelling of 2 ′-aminobiphenyl-2,3-diol-1,2-dioxygenase from Pseudomonas stutzeri carbazole degradation pathway Cell Biochem. Biophys. 44, 530-538
    • (2006) Cell Biochem. Biophys. , vol.44 , pp. 530-538
    • Larentis, A.L.1    Almeida, R.V.2    Rossle, S.C.3    Cardoso, A.M.4    Almeida, W.I.5    Bisch, P.M.6    Alves, T.L.M.7    Martins, O.B.8
  • 24
    • 0032900505 scopus 로고    scopus 로고
    • The phn genes of Burkholderia sp strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism
    • Laurie, A. D. and Lloyd-Jones, G. (1999) The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism J. Bacteriol. 181, 531-540
    • (1999) J. Bacteriol. , vol.181 , pp. 531-540
    • Laurie, A.D.1    Lloyd-Jones, G.2
  • 25
    • 27444438472 scopus 로고    scopus 로고
    • Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440 - The prototype of a new subgroup of extradiol dioxygenases
    • Nogales, J., Canales, A., Jimenez-Barbero, J., Garcia, J. L., and Diaz, E. (2005) Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440-The prototype of a new subgroup of extradiol dioxygenases J. Biol. Chem. 280, 35382-35390
    • (2005) J. Biol. Chem. , vol.280 , pp. 35382-35390
    • Nogales, J.1    Canales, A.2    Jimenez-Barbero, J.3    Garcia, J.L.4    Diaz, E.5
  • 26
    • 0025115933 scopus 로고
    • Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C
    • Roper, D. I. and Cooper, R. A. (1990) Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C FEBS Lett. 275, 53-57
    • (1990) FEBS Lett. , vol.275 , pp. 53-57
    • Roper, D.I.1    Cooper, R.A.2
  • 27
    • 0030882765 scopus 로고    scopus 로고
    • A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: Cloning and characterization of the hpp operon
    • Barnes, M. R., Duetz, W. A., and Williams, P. A. (1997) A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: Cloning and characterization of the hpp operon J. Bacteriol. 179, 6145-6153
    • (1997) J. Bacteriol. , vol.179 , pp. 6145-6153
    • Barnes, M.R.1    Duetz, W.A.2    Williams, P.A.3
  • 28
    • 0031977177 scopus 로고    scopus 로고
    • Cloning of new Rhodococcus extradiol dioxygenase genes and study of their distribution in different Rhodococcus strains
    • Kulakov, L. A., Delcroix, V. A., Larkin, M. J., Ksenzenko, V. N., and Kulakova, A. N. (1998) Cloning of new Rhodococcus extradiol dioxygenase genes and study of their distribution in different Rhodococcus strains Microbiology (Reading, U.K.) 144, 955-963
    • (1998) Microbiology (Reading, U.K.) , vol.144 , pp. 955-963
    • Kulakov, L.A.1    Delcroix, V.A.2    Larkin, M.J.3    Ksenzenko, V.N.4    Kulakova, A.N.5
  • 29
    • 11244352142 scopus 로고    scopus 로고
    • Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1
    • Maruyama, K., Shibayama, T., Ichikawa, A., Sakou, Y., Yamada, S., and Sugisaki, H. (2004) Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1 Biosci., Biotechnol., Biochem. 68, 1434-1441
    • (2004) Biosci., Biotechnol., Biochem. , vol.68 , pp. 1434-1441
    • Maruyama, K.1    Shibayama, T.2    Ichikawa, A.3    Sakou, Y.4    Yamada, S.5    Sugisaki, H.6
  • 30
    • 0034991776 scopus 로고    scopus 로고
    • Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B
    • Eaton, R. W. (2001) Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B J. Bacteriol. 183, 3689-3703
    • (2001) J. Bacteriol. , vol.183 , pp. 3689-3703
    • Eaton, R.W.1
  • 31
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
    • Sugimoto, K., Senda, T., Aoshima, H., Masai, E., Fukuda, M., and Mitsui, Y. (1999) Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions Structure (London) 7, 953-965
    • (1999) Structure (London) , vol.7 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 32
    • 6344291632 scopus 로고    scopus 로고
    • Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)
    • Mendel, S., Arndt, A., and Bugg, T. D. H. (2004) Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) Biochemistry 43, 13390-13396
    • (2004) Biochemistry , vol.43 , pp. 13390-13396
    • Mendel, S.1    Arndt, A.2    Bugg, T.D.H.3
  • 33
    • 33845404294 scopus 로고    scopus 로고
    • Directed evolution of non-heme-iron-dependent extradiol catechol dioxygenase: Identification of mutants with intradiol oxidative cleavage activity
    • Schlosrich, J., Eley, K. L., Crowley, P. J., and Bugg, T. D. H. (2006) Directed evolution of non-heme-iron-dependent extradiol catechol dioxygenase: Identification of mutants with intradiol oxidative cleavage activity ChemBioChem 7, 1899-1908
    • (2006) ChemBioChem , vol.7 , pp. 1899-1908
    • Schlosrich, J.1    Eley, K.L.2    Crowley, P.J.3    Bugg, T.D.H.4
  • 34
    • 0001830934 scopus 로고
    • Cloning and expression of Pseudomonas paucimobilis SYK-6 genes involved in the degradation of vanillate and protocatechuate in P putida
    • Katayama, Y., Nishikawa, S., Nakamura, M., Yano, K., Yamasaki, M., Morohoshi, N., and Haraguchi, T. (1987) Cloning and expression of Pseudomonas paucimobilis SYK-6 genes involved in the degradation of vanillate and protocatechuate in P. putida Mokuzai Gakkaishi 33, 77-79
    • (1987) Mokuzai Gakkaishi , vol.33 , pp. 77-79
    • Katayama, Y.1    Nishikawa, S.2    Nakamura, M.3    Yano, K.4    Yamasaki, M.5    Morohoshi, N.6    Haraguchi, T.7
  • 35
    • 0024962078 scopus 로고
    • Detection and localization of a new enzyme catalyzing the β-aryl ether cleavage in the soil bacterium (Pseudomonas paucimobilis SYK-6)
    • Masai, E., Katayama, Y., Nishikawa, S., Yamasaki, M., Morohoshi, N., and Haraguchi, T. (1989) Detection and localization of a new enzyme catalyzing the β-aryl ether cleavage in the soil bacterium (Pseudomonas paucimobilis SYK-6) FEBS Lett. 249, 348-352
    • (1989) FEBS Lett. , vol.249 , pp. 348-352
    • Masai, E.1    Katayama, Y.2    Nishikawa, S.3    Yamasaki, M.4    Morohoshi, N.5    Haraguchi, T.6
  • 36
    • 0033383704 scopus 로고    scopus 로고
    • Characterization of Sphingomonas paucimobilis SYK-6 genes involved in degredation of lignin-related compounds
    • Masai, E., Katayama, Y., Nishikawa, S., and Fukuda, M. (1999) Characterization of Sphingomonas paucimobilis SYK-6 genes involved in degredation of lignin-related compounds J. Ind. Microbiol. Biotechnol. 23, 364-373
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.23 , pp. 364-373
    • Masai, E.1    Katayama, Y.2    Nishikawa, S.3    Fukuda, M.4
  • 37
    • 0009626717 scopus 로고    scopus 로고
    • Purification and crystallization of a protocatechuate 4,5-dioxygenase LigAB from Sphingomonas paucimobilis SYK-6
    • Sugimoto, K., Aoshima, H., Senda, T., Masai, E., Fukuda, M., and Mitsui, Y. (1999) Purification and crystallization of a protocatechuate 4,5-dioxygenase LigAB from Sphingomonas paucimobilis SYK-6 Protein Pept. Lett. 6, 55-58
    • (1999) Protein Pept. Lett. , vol.6 , pp. 55-58
    • Sugimoto, K.1    Aoshima, H.2    Senda, T.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 38
    • 3242810505 scopus 로고    scopus 로고
    • Characterization of the 3-O-methylgallate dioxygenase gene and evidence of multiple 3-O-methylgallate catabolic pathways in Sphingomonas paucimobilis SYK-6
    • Kasai, D., Masai, E., Miyauchi, K., Katayama, Y., and Fukuda, M. (2004) Characterization of the 3-O-methylgallate dioxygenase gene and evidence of multiple 3-O-methylgallate catabolic pathways in Sphingomonas paucimobilis SYK-6 J. Bacteriol. 186, 4951-4959
    • (2004) J. Bacteriol. , vol.186 , pp. 4951-4959
    • Kasai, D.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 39
    • 22544457598 scopus 로고    scopus 로고
    • Characterization of the gallate dioxygenase gene: Three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6
    • Kasai, D., Masai, E., Miyauchi, K., Katayama, Y., and Fukuda, M. (2005) Characterization of the gallate dioxygenase gene: Three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6 J. Bacteriol. 187, 5067-5074
    • (2005) J. Bacteriol. , vol.187 , pp. 5067-5074
    • Kasai, D.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 40
    • 34547915576 scopus 로고    scopus 로고
    • Degredation of 3-O-methylgallate in Sphingomonas paucimobilis SYK-6 by pathways involving protocatechuate 4,5-dioxygenase
    • Kasai, D., Masai, E., Katayama, Y., and Fukuda, M. (2007) Degredation of 3-O-methylgallate in Sphingomonas paucimobilis SYK-6 by pathways involving protocatechuate 4,5-dioxygenase FEMS Microbiol. Lett. 274, 323-328
    • (2007) FEMS Microbiol. Lett. , vol.274 , pp. 323-328
    • Kasai, D.1    Masai, E.2    Katayama, Y.3    Fukuda, M.4
  • 41
    • 33846485037 scopus 로고    scopus 로고
    • Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds
    • Masai, E., Katayama, Y., and Fukuda, M. (2007) Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds Biosci., Biotechnol., Biochem. 71, 1-15
    • (2007) Biosci., Biotechnol., Biochem. , vol.71 , pp. 1-15
    • Masai, E.1    Katayama, Y.2    Fukuda, M.3
  • 42
    • 22544460781 scopus 로고    scopus 로고
    • Effects of electron-withdrawing substituents on DPPH radical scavenging reactions of protocatechuic acid and its analogues in alcoholic solvents
    • Saito, S. and Kawabata, J. (2005) Effects of electron-withdrawing substituents on DPPH radical scavenging reactions of protocatechuic acid and its analogues in alcoholic solvents Tetrahedron 61, 8101-8108
    • (2005) Tetrahedron , vol.61 , pp. 8101-8108
    • Saito, S.1    Kawabata, J.2
  • 43
    • 80052421542 scopus 로고    scopus 로고
    • Identification of novel matrix metalloproteinase inhibitors by screening of phenol fragments library
    • Rubino, M. T., Maggi, D., Laghezza, A., Loiodice, F., and Tortorella, P. (2011) Identification of novel matrix metalloproteinase inhibitors by screening of phenol fragments library Arch. Pharm. (Weinheim) 344, 557-563
    • (2011) Arch. Pharm. (Weinheim) , vol.344 , pp. 557-563
    • Rubino, M.T.1    Maggi, D.2    Laghezza, A.3    Loiodice, F.4    Tortorella, P.5
  • 44
    • 84857361285 scopus 로고    scopus 로고
    • Efficient synthesis of the siderophore petrobactin via antimony triethoxide mediated coupling
    • Pandey, R. K., Jarvis, G. G., and Low, P. S. (2012) Efficient synthesis of the siderophore petrobactin via antimony triethoxide mediated coupling Tetrahedron Lett. 53, 1627-1629
    • (2012) Tetrahedron Lett. , vol.53 , pp. 1627-1629
    • Pandey, R.K.1    Jarvis, G.G.2    Low, P.S.3
  • 45
    • 0037127253 scopus 로고    scopus 로고
    • The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates
    • Vaillancourt, F. H., Labbe, G., Drouin, N. M., Fortin, P. D., and Eltis, L. D. (2002) The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates J. Biol. Chem. 277, 2019-2027
    • (2002) J. Biol. Chem. , vol.277 , pp. 2019-2027
    • Vaillancourt, F.H.1    Labbe, G.2    Drouin, N.M.3    Fortin, P.D.4    Eltis, L.D.5
  • 46
    • 2142832239 scopus 로고
    • New aromatic ring-splitting enzyme, protocatechuic acid 4,5-oxygenase
    • Cain, R. B. (1962) New aromatic ring-splitting enzyme, protocatechuic acid 4,5-oxygenase Nature 193, 842-844
    • (1962) Nature , vol.193 , pp. 842-844
    • Cain, R.B.1
  • 47
    • 0017854725 scopus 로고
    • Purification and properties of α-hydroxy-γ-carboxymuconic- ε-semialdehyde dehydrogenase
    • Maruyama, K., Ariga, N., Tsuda, M., and Deguchi, K. (1978) Purification and properties of α-hydroxy-γ-carboxymuconic-ε-semialdehyde dehydrogenase J. Biochem. 83, 1125-1134
    • (1978) J. Biochem. , vol.83 , pp. 1125-1134
    • Maruyama, K.1    Ariga, N.2    Tsuda, M.3    Deguchi, K.4
  • 48
    • 0014346766 scopus 로고
    • The metabolism of protocatechuate by Pseudomonas testosteroni
    • Dagley, S., Geary, P. J., and Wood, J. M. (1968) The metabolism of protocatechuate by Pseudomonas testosteroni Biochem. J. 109, 559-568
    • (1968) Biochem. J. , vol.109 , pp. 559-568
    • Dagley, S.1    Geary, P.J.2    Wood, J.M.3
  • 50
    • 84961980477 scopus 로고    scopus 로고
    • Quantum mechanical continuum solvation models
    • Tomasi, J., Mennucci, B., and Cammi, R. (2005) Quantum mechanical continuum solvation models Chem. Rev. 105, 2999-3093
    • (2005) Chem. Rev. , vol.105 , pp. 2999-3093
    • Tomasi, J.1    Mennucci, B.2    Cammi, R.3
  • 51
    • 11744256643 scopus 로고
    • Molecular interactions in solution - An overview of methods based on continuous distributions of the solvent
    • Tomasi, J. and Persico, M. (1994) Molecular interactions in solution-An overview of methods based on continuous distributions of the solvent Chem. Rev. 94, 2027-2094
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 52
    • 78649557525 scopus 로고    scopus 로고
    • Experimental and computed absolute redox potentials of polycyclic aromatic hydrocarbons are highly linearly correlated over a wide range of structures and potentials
    • Davis, A. P. and Fry, A. J. (2010) Experimental and computed absolute redox potentials of polycyclic aromatic hydrocarbons are highly linearly correlated over a wide range of structures and potentials J. Phys. Chem. A 114, 12299-12304
    • (2010) J. Phys. Chem. A , vol.114 , pp. 12299-12304
    • Davis, A.P.1    Fry, A.J.2
  • 53
    • 65649132303 scopus 로고    scopus 로고
    • Characterization of 3-ketosteroid 9α-hydroxylase, a Rieske-oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis
    • Capyk, J. K., D'Angelo, I., Strynadka, N., and Eltis, L. D. (2009) Characterization of 3-ketosteroid 9α-hydroxylase, a Rieske-oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis J. Biol. Chem. 284, 9937-9946
    • (2009) J. Biol. Chem. , vol.284 , pp. 9937-9946
    • Capyk, J.K.1    D'Angelo, I.2    Strynadka, N.3    Eltis, L.D.4
  • 55
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t -butanol
    • Vaillancourt, F. H., Han, S., Fortin, P. D., Bolin, J. T., and Eltis, L. D. (1998) Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t -butanol J. Biol. Chem. 273, 34887-34895
    • (1998) J. Biol. Chem. , vol.273 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5
  • 57
    • 44949225065 scopus 로고    scopus 로고
    • Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state
    • Emerson, J. P., Kovaleva, E. G., Farquhar, E. R., Lipscomb, J. D., and Que, L. (2008) Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state Proc. Natl. Acad. Sci. U.S.A. 105, 7347-7352
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7347-7352
    • Emerson, J.P.1    Kovaleva, E.G.2    Farquhar, E.R.3    Lipscomb, J.D.4    Que, L.5
  • 58
    • 0141732267 scopus 로고    scopus 로고
    • Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme
    • Groce, S. L. and Lipscomb, J. D. (2003) Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme J. Am. Chem. Soc. 125, 11780-11781
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11780-11781
    • Groce, S.L.1    Lipscomb, J.D.2
  • 59
    • 17844384785 scopus 로고    scopus 로고
    • Structural and catalytic diversity within the amidohydrolase superfamily
    • Seibert, C. M. and Raushel, F. M. (2005) Structural and catalytic diversity within the amidohydrolase superfamily Biochemistry 44, 6383-6391
    • (2005) Biochemistry , vol.44 , pp. 6383-6391
    • Seibert, C.M.1    Raushel, F.M.2
  • 60
    • 67650072614 scopus 로고    scopus 로고
    • Annotating enzymes of uncertain function: The deacylation of d-amino acids by members of the amidohydrolase superfamily
    • Cummings, J. A., Fedorov, A. A., Xu, C., Brown, S., Fedorov, E., Babbitt, P. C., Almo, S. C., and Raushel, F. M. (2009) Annotating enzymes of uncertain function: the deacylation of d-amino acids by members of the amidohydrolase superfamily Biochemistry 48, 6469-6481
    • (2009) Biochemistry , vol.48 , pp. 6469-6481
    • Cummings, J.A.1    Fedorov, A.A.2    Xu, C.3    Brown, S.4    Fedorov, E.5    Babbitt, P.C.6    Almo, S.C.7    Raushel, F.M.8
  • 61
    • 0014941894 scopus 로고
    • Purification and some properties of protocatechuate 4,5-dioxygenase
    • Ono, K., Nozaki, M., and Hayaishi, O. (1970) Purification and some properties of protocatechuate 4,5-dioxygenase Biochim. Biophys. Acta 220, 224-238
    • (1970) Biochim. Biophys. Acta , vol.220 , pp. 224-238
    • Ono, K.1    Nozaki, M.2    Hayaishi, O.3
  • 62
    • 0030066104 scopus 로고    scopus 로고
    • Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis CM-2
    • Whiting, A. K., Boldt, Y. R., Hendrich, M. P., Wackett, L. P., and Que, L. (1996) Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis CM-2 Biochemistry 35, 160-170
    • (1996) Biochemistry , vol.35 , pp. 160-170
    • Whiting, A.K.1    Boldt, Y.R.2    Hendrich, M.P.3    Wackett, L.P.4    Que, L.5
  • 64
    • 0015510099 scopus 로고
    • Kinetic and Mossbauer studies on mechanism of protocatechuic acid 4,5-oxygenase
    • Zabinski, R., Wood, J. M., Champion, P. M., and Munck, E. (1972) Kinetic and Mossbauer studies on mechanism of protocatechuic acid 4,5-oxygenase Biochemistry 11, 3212 &.
    • (1972) Biochemistry , vol.11 , pp. 3212
    • Zabinski, R.1    Wood, J.M.2    Champion, P.M.3    Munck, E.4
  • 65
    • 34447643050 scopus 로고    scopus 로고
    • The effect of pH on the kinetics of spontaneous Fe(II) oxidation by O-2 in aqueous solution - Basic principles and a simple heuristic description
    • Morgan, B. and Lahav, O. (2007) The effect of pH on the kinetics of spontaneous Fe(II) oxidation by O-2 in aqueous solution-basic principles and a simple heuristic description Chemosphere 68, 2080-2084
    • (2007) Chemosphere , vol.68 , pp. 2080-2084
    • Morgan, B.1    Lahav, O.2
  • 66
    • 0015220239 scopus 로고
    • Apo- and reconsitututed holoenzymes of metapyrocatechase from Pseudomonas putida
    • Takemori, S., Komiyama, T., and Katagiri, M. (1971) Apo- and reconsitututed holoenzymes of metapyrocatechase from Pseudomonas putida Eur. J. Biochem. 23, 178-184
    • (1971) Eur. J. Biochem. , vol.23 , pp. 178-184
    • Takemori, S.1    Komiyama, T.2    Katagiri, M.3
  • 67
    • 84856868395 scopus 로고    scopus 로고
    • A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase
    • Tchesnokov, E. P., Wilbanks, S. M., and Jameson, G. N. L. (2012) A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase Biochemistry 51, 257-264
    • (2012) Biochemistry , vol.51 , pp. 257-264
    • Tchesnokov, E.P.1    Wilbanks, S.M.2    Jameson, G.N.L.3
  • 68
    • 61449234236 scopus 로고    scopus 로고
    • 2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii
    • 2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii Biochem. J. 418, 403-411
    • (2009) Biochem. J. , vol.418 , pp. 403-411
    • Leitgeb, S.1    Straganz, G.D.2    Nidetzky, B.3
  • 70
    • 34547383525 scopus 로고
    • New pathways in the oxidative metabolism of aromatic compounds by micro-organisms
    • Dagley, S., Evans, W. C., and Ribbons, D. W. (1960) New pathways in the oxidative metabolism of aromatic compounds by micro-organisms Nature 188, 560-566
    • (1960) Nature , vol.188 , pp. 560-566
    • Dagley, S.1    Evans, W.C.2    Ribbons, D.W.3
  • 72
    • 3142594034 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship for the cleavage of C3/C4-substituted catechols by a prototypal extradiol catechol dioxygenase with broad substrate specificity
    • Ishida, T., Tanaka, H., and Horiike, K. (2004) Quantitative structure-activity relationship for the cleavage of C3/C4-substituted catechols by a prototypal extradiol catechol dioxygenase with broad substrate specificity J. Biochem. 135, 721-730
    • (2004) J. Biochem. , vol.135 , pp. 721-730
    • Ishida, T.1    Tanaka, H.2    Horiike, K.3
  • 73
    • 27544492782 scopus 로고    scopus 로고
    • Single-turnover kinetics of 2,3-dihydroxybiphenyl 1,2-dioxygenase reacting with 3-formylcatechol
    • Ishida, T., Senda, T., Tanaka, H., Yamamoto, A., and Horiike, K. (2005) Single-turnover kinetics of 2,3-dihydroxybiphenyl 1,2-dioxygenase reacting with 3-formylcatechol Biochem. Biophys. Res. Commun. 338, 223-229
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 223-229
    • Ishida, T.1    Senda, T.2    Tanaka, H.3    Yamamoto, A.4    Horiike, K.5
  • 74
    • 0025216788 scopus 로고
    • Gentisate 1,2-dioxygenase from Pseudomonas - Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans
    • Harpel, M. R. and Lipscomb, J. D. (1990) Gentisate 1,2-dioxygenase from Pseudomonas-Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans J. Biol. Chem. 265, 6301-6311
    • (1990) J. Biol. Chem. , vol.265 , pp. 6301-6311
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 75
    • 0039136118 scopus 로고    scopus 로고
    • Purification and characterization of gentisate 1,2-dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869
    • Feng, Y. M., Khoo, H. E., and Poh, C. L. (1999) Purification and characterization of gentisate 1,2-dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869 Appl. Environ. Microbiol. 65, 946-950
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 946-950
    • Feng, Y.M.1    Khoo, H.E.2    Poh, C.L.3
  • 76
    • 0035967509 scopus 로고    scopus 로고
    • Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae
    • Dai, Y., Pochapsky, T. C., and Abeles, R. H. (2001) Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae Biochemistry 40, 6379-6387
    • (2001) Biochemistry , vol.40 , pp. 6379-6387
    • Dai, Y.1    Pochapsky, T.C.2    Abeles, R.H.3
  • 77
    • 33644846369 scopus 로고    scopus 로고
    • The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine
    • Sauter, M., Lorbiecke, R., Bo, O. Y., Pochapsky, T. C., and Rzewuski, G. (2005) The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine Plant J. 44, 718-729
    • (2005) Plant J. , vol.44 , pp. 718-729
    • Sauter, M.1    Lorbiecke, R.2    Bo, O.Y.3    Pochapsky, T.C.4    Rzewuski, G.5
  • 78
    • 0037023710 scopus 로고    scopus 로고
    • The trans-anethole degradation pathway in an Arthrobacter sp
    • Shimoni, E., Baasov, T., Ravid, U., and Shoham, Y. (2002) The trans-anethole degradation pathway in an Arthrobacter sp J. Biol. Chem. 277, 11866-11872
    • (2002) J. Biol. Chem. , vol.277 , pp. 11866-11872
    • Shimoni, E.1    Baasov, T.2    Ravid, U.3    Shoham, Y.4
  • 79
    • 3242689919 scopus 로고    scopus 로고
    • Characterization of protocatechuate 4,5-dioxygenase induced from p -hydroxybenzoate cultured Pseudomonas sp. K82
    • Yun, S.-H., Yun, C.-Y., and Kim, S. I. (2004) Characterization of protocatechuate 4,5-dioxygenase induced from p -hydroxybenzoate cultured Pseudomonas sp. K82 J. Microbiol. 42, 152-155
    • (2004) J. Microbiol. , vol.42 , pp. 152-155
    • Yun, S.-H.1    Yun, C.-Y.2    Kim, S.I.3
  • 80
    • 33846471046 scopus 로고    scopus 로고
    • Cloning of p -hydroxybenzoate degradation genes and the overexpression of protocatechuate 4,5-dioxygenase from Pseudomonas sp. K82
    • Yoon, Y.-H., Park, S.-H., Leem, S.-H., and Kim, S. I. (2006) Cloning of p -hydroxybenzoate degradation genes and the overexpression of protocatechuate 4,5-dioxygenase from Pseudomonas sp. K82 J. Microbiol. Biotechnol. 16, 1995-1999
    • (2006) J. Microbiol. Biotechnol. , vol.16 , pp. 1995-1999
    • Yoon, Y.-H.1    Park, S.-H.2    Leem, S.-H.3    Kim, S.I.4
  • 81
    • 0019457548 scopus 로고
    • Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
    • Klecka, G. M. and Gibson, D. T. (1981) Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol Appl. Environ. Microbiol. 41, 1159-1165
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 1159-1165
    • Klecka, G.M.1    Gibson, D.T.2


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