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Volumn 172, Issue 5, 1999, Pages 330-339

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

Author keywords

2 Aminophenol; Biodegradation; Catechol; Dioxygenase; Meta Cleavage pathway; Pseudomonas

Indexed keywords

2 AMINOPHENOL; CATECHOL; IRON; NITROBENZENE; OXYGENASE; RNA HELICASE;

EID: 0032721192     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050787     Document Type: Conference Paper
Times cited : (38)

References (54)
  • 1
    • 0030895358 scopus 로고    scopus 로고
    • Partial purification and characterization of a bacterial dioxygenase that catalyzes the ring fission of 2-aminophenol
    • Aoki K, Takenaka S, Murakami S, Shinke R (1997) Partial purification and characterization of a bacterial dioxygenase that catalyzes the ring fission of 2-aminophenol. Microbiol Res 152 : 33-38
    • (1997) Microbiol Res , vol.152 , pp. 33-38
    • Aoki, K.1    Takenaka, S.2    Murakami, S.3    Shinke, R.4
  • 2
    • 0028987137 scopus 로고
    • A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family
    • Boldt YR, Sadowsky MJ, Ellis LBM, Que L Jr, Wackett LP (1995) A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family. J Bacteriol 1995 : 1225-1232
    • (1995) J Bacteriol , vol.1995 , pp. 1225-1232
    • Boldt, Y.R.1    Sadowsky, M.J.2    Ellis, L.B.M.3    Que L., Jr.4    Wackett, L.P.5
  • 3
    • 0031057367 scopus 로고    scopus 로고
    • Exploring the catalytic mechanism of the extradiol catechol dioxygenases
    • Bugg TD, Sanvoisin J, Spence EL (1997) Exploring the catalytic mechanism of the extradiol catechol dioxygenases. Biochem Soc Trans 25 : 81-5
    • (1997) Biochem Soc Trans , vol.25 , pp. 81-85
    • Bugg, T.D.1    Sanvoisin, J.2    Spence, E.L.3
  • 4
    • 0030590532 scopus 로고    scopus 로고
    • The primary structure of UK114 tumor antigen
    • Ceciliani F, et al (1996) The primary structure of UK114 tumor antigen. FEBS Lett 393 : 147-150
    • (1996) FEBS Lett , vol.393 , pp. 147-150
    • Ceciliani, F.1
  • 5
    • 0029864057 scopus 로고    scopus 로고
    • p-Cumate catabolic pathway in Pseudomonas putida F1: Cloning and characterization of DNA carrying the cmt operon
    • Eaton RW (1996) p-Cumate catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA carrying the cmt operon. J Bacteriol 178 : 1351-1362
    • (1996) J Bacteriol , vol.178 , pp. 1351-1362
    • Eaton, R.W.1
  • 6
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis LD, Bolin JT (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
  • 7
    • 0032444814 scopus 로고    scopus 로고
    • Complex metabolic phenotypes caused by a mutation in yjgF, encoding a member of the highly conserved YER057c/YjgF family of proteins
    • Enos-Berlage JL, Langendorf MJ, Downs DM (1998) Complex metabolic phenotypes caused by a mutation in yjgF, encoding a member of the highly conserved YER057c/YjgF family of proteins. J Bacteriol 180 : 6519-6528
    • (1998) J Bacteriol , vol.180 , pp. 6519-6528
    • Enos-Berlage, J.L.1    Langendorf, M.J.2    Downs, D.M.3
  • 8
    • 0001106373 scopus 로고
    • Degradative plasmids in Pseudomonas
    • Sokatch JR (ed) Academic Press, New York
    • Frantz B, Chakrabarty AM (1986) Degradative plasmids in Pseudomonas. In: Sokatch JR (ed) The Bacteria, vol 10. Academic Press, New York, pp 295-323
    • (1986) The Bacteria , vol.10 , pp. 295-323
    • Frantz, B.1    Chakrabarty, A.M.2
  • 10
    • 77956815543 scopus 로고
    • Preparation and electrophoresis of plasmid DNA
    • Grinsted J, Bennett PM (eds) Academic Press, New York
    • Grinsted J, Bennett PM (1988) Preparation and electrophoresis of plasmid DNA. In: Grinsted J, Bennett PM (eds) Plasmid technology. Academic Press, New York, pp 129-153
    • (1988) Plasmid Technology , pp. 129-153
    • Grinsted, J.1    Bennett, P.M.2
  • 11
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomad
    • Han S, Eltis LD, Timmis KN, Muchmore SW, Bolin JT (1995) Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomad. 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
  • 12
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166 : 557-580
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 13
    • 0025318026 scopus 로고
    • The meta cleavage operon of TOL degradative plasmid pWW0 comprises 13 genes
    • Harayama S, Rekik M (1990) The meta cleavage operon of TOL degradative plasmid pWW0 comprises 13 genes. Mol Gen Genet 221 : 113-120
    • (1990) Mol Gen Genet , vol.221 , pp. 113-120
    • Harayama, S.1    Rekik, M.2
  • 14
    • 0025787605 scopus 로고
    • Potential DNA slippage structures acquired during evolutionary divergence of Acinetobacter calcoaceticus chromosomal benABC and Pseudomonas putida TOL pWW0 plasmid xylXYZ gene encoding benzoate dioxygenases
    • Harayama S, Rekik M, Bairoch A, Neidle EL, Ornston LN (1991) Potential DNA slippage structures acquired during evolutionary divergence of Acinetobacter calcoaceticus chromosomal benABC and Pseudomonas putida TOL pWW0 plasmid xylXYZ gene encoding benzoate dioxygenases. J Bacteriol 173 : 7540-7548
    • (1991) J Bacteriol , vol.173 , pp. 7540-7548
    • Harayama, S.1    Rekik, M.2    Bairoch, A.3    Neidle, E.L.4    Ornston, L.N.5
  • 15
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama S, Kok M, Neidle EL (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
  • 16
    • 0030833913 scopus 로고    scopus 로고
    • Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: Removal of the amino group from 2-aminomuconic semi-aldehyde
    • He Z, Spain JC (1997) Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semi-aldehyde. Appl Environ Microbiol 63 : 4839-4843
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4839-4843
    • He, Z.1    Spain, J.C.2
  • 17
    • 0031956099 scopus 로고    scopus 로고
    • A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45
    • He Z, Spain JC (1998) A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45. J Bacteriol 180 : 2502-2506
    • (1998) J Bacteriol , vol.180 , pp. 2502-2506
    • He, Z.1    Spain, J.C.2
  • 18
    • 0032923747 scopus 로고    scopus 로고
    • Comparison of the downstream pathways for degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45 (2-aminophenol pathway) and by Comamonas sp. JS765 (catechol pathway)
    • He Z, Spain JC (1999) Comparison of the downstream pathways for degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45 (2-aminophenol pathway) and by Comamonas sp. JS765 (catechol pathway). Arch Microbiol 171 : 309-316
    • (1999) Arch Microbiol , vol.171 , pp. 309-316
    • He, Z.1    Spain, J.C.2
  • 19
    • 0031721043 scopus 로고    scopus 로고
    • Purification, characterization, and sequence analysis of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas pseudoalcaligenes JS45
    • He Z, Davis JK, Spain JC (1998) Purification, characterization, and sequence analysis of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas pseudoalcaligenes JS45. J Bacteriol 180 : 4591-4595
    • (1998) J Bacteriol , vol.180 , pp. 4591-4595
    • He, Z.1    Davis, J.K.2    Spain, J.C.3
  • 20
    • 0032540352 scopus 로고    scopus 로고
    • A novel [2Fe-2S] ferredoxin from Pseudomonas putida mt2 promotes the reductive reaction of catechol 2,3-dioxygenase
    • Hugo N, Armengaud J, Gaillard J, Timmis KN, Jouanneau Y (1998) A novel [2Fe-2S] ferredoxin from Pseudomonas putida mt2 promotes the reductive reaction of catechol 2,3-dioxygenase. J Biol Chem 273 : 9622-9629
    • (1998) J Biol Chem , vol.273 , pp. 9622-9629
    • Hugo, N.1    Armengaud, J.2    Gaillard, J.3    Timmis, K.N.4    Jouanneau, Y.5
  • 21
    • 0000936823 scopus 로고
    • Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues: 2. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid
    • Ichiyama A, et al (1965) Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. 2. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J Biol Chem 240 : 740-749
    • (1965) J Biol Chem , vol.240 , pp. 740-749
    • Ichiyama, A.1
  • 22
    • 0025296680 scopus 로고
    • Nucleotide sequence of metapyrocatechase I (catechol 2,3-dioxygenaseI) gene mpcI from Al-caligenes eutrophus JMP222
    • Kabisch M, Fortnagel P (1990a) Nucleotide sequence of metapyrocatechase I (catechol 2,3-dioxygenaseI) gene mpcI from Al-caligenes eutrophus JMP222. Nucleic Acids Res 18 : 3405-3406
    • (1990) Nucleic Acids Res , vol.18 , pp. 3405-3406
    • Kabisch, M.1    Fortnagel, P.2
  • 23
    • 0025165613 scopus 로고
    • Nucleotide sequence of the metapyrocatechase II (catechol 2,3-dioxygenase II) gene mpcII from Alcaligenes eutrophus JMP 222
    • Kabisch M, Fortnagel P (1990b) Nucleotide sequence of the metapyrocatechase II (catechol 2,3-dioxygenase II) gene mpcII from Alcaligenes eutrophus JMP 222. Nucleic Acids Res 18 : 5543
    • (1990) Nucleic Acids Res , vol.18 , pp. 5543
    • Kabisch, M.1    Fortnagel, P.2
  • 24
    • 0018387765 scopus 로고
    • Priority pollutants: 1. A perspective view
    • Keith LH, Telliard WA (1979) Priority pollutants. 1. A perspective view. Environ Sci Technol 13 : 416-423
    • (1979) Environ Sci Technol , vol.13 , pp. 416-423
    • Keith, L.H.1    Telliard, W.A.2
  • 25
    • 0031558780 scopus 로고    scopus 로고
    • Nucleotide sequence of the Pseudomonas sp. DJ77 phnG gene encoding 2-hydroxymuconic semialdehyde dehydrogenase
    • Kim S, Shin H-J, Kim Y, Kim SJ, Kim Y-C (1997) Nucleotide sequence of the Pseudomonas sp. DJ77 phnG gene encoding 2-hydroxymuconic semialdehyde dehydrogenase. Biochem Biophys Res Commun 240 : 41-45
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 41-45
    • Kim, S.1    Shin, H.-J.2    Kim, Y.3    Kim, S.J.4    Kim, Y.-C.5
  • 26
    • 0032039677 scopus 로고    scopus 로고
    • Oxygen activating nonheme iron enzymes
    • Lange SJ, Que L Jr (1998) Oxygen activating nonheme iron enzymes. Curr Opin Chem Biol 2 : 159-172
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 159-172
    • Lange, S.J.1    Que L., Jr.2
  • 27
    • 0032900505 scopus 로고    scopus 로고
    • The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism
    • Laurie AD, 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
  • 28
    • 0029858048 scopus 로고    scopus 로고
    • 2-aminophenol 1,6-dioxygenase: A novel aromatic ring-cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45
    • Lendenmann U, Spain JC (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
  • 29
    • 0028336792 scopus 로고
    • Molecular cloning and functional expression of human 3-hydroxyanthranilic-dioxygenase
    • Malherbe P, et al (1994) Molecular cloning and functional expression of human 3-hydroxyanthranilic-dioxygenase. J Biol Chem 269 : 13792-13797
    • (1994) J Biol Chem , vol.269 , pp. 13792-13797
    • Malherbe, P.1
  • 30
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing J (1983) New M13 vectors for cloning. Methods Enzymol 101 : 20-78
    • (1983) Methods Enzymol , vol.101 , pp. 20-78
    • Messing, J.1
  • 31
    • 0027251005 scopus 로고
    • Degradation of nitrobenzene by a Pseudomonas pseudoalcaligenes
    • Nishino SF, Spain JC (1993) Degradation of nitrobenzene by a Pseudomonas pseudoalcaligenes. Appl Environ Microbiol 59 : 2520-2525
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2520-2525
    • Nishino, S.F.1    Spain, J.C.2
  • 32
    • 0029070669 scopus 로고
    • Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765
    • Nishino SF, Spain JC (1995) Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765. Appl Environ Microbiol 61 : 2308-2313
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2308-2313
    • Nishino, S.F.1    Spain, J.C.2
  • 33
    • 77957011787 scopus 로고
    • Metabolism of the benzene ring of tryptophan (mammals)
    • Nishizuka Y, Ichiyama A, Hayaishi O (1970) Metabolism of the benzene ring of tryptophan (mammals). Methods Enzymol 17A: 463-491
    • (1970) Methods Enzymol , vol.17 A , pp. 463-491
    • Nishizuka, Y.1    Ichiyama, A.2    Hayaishi, O.3
  • 34
    • 0025271597 scopus 로고
    • Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis
    • Noda Y, et al (1990) Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis. J Bacteriol 172 : 2704-2709
    • (1990) J Bacteriol , vol.172 , pp. 2704-2709
    • Noda, Y.1
  • 35
    • 0014941882 scopus 로고
    • Metapyrocatechase. 3. Subtrate specificity and mode of ring fission
    • Nozaki M, Kotani S, Ono K, Senoh S (1970) Metapyrocatechase. 3. subtrate specificity and mode of ring fission. Biochim Biophys Acta 220 : 213-223
    • (1970) Biochim Biophys Acta , vol.220 , pp. 213-223
    • Nozaki, M.1    Kotani, S.2    Ono, K.3    Senoh, S.4
  • 36
    • 0029585753 scopus 로고
    • Isolation and characterization of a novel perchloric acid-soluble protein inhibiting cell-free protein synthesis
    • Oka T, et al (1995) Isolation and characterization of a novel perchloric acid-soluble protein inhibiting cell-free protein synthesis. J Biol Chem 270 : 30060-30067
    • (1995) J Biol Chem , vol.270 , pp. 30060-30067
    • Oka, T.1
  • 37
    • 0028672047 scopus 로고
    • Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600
    • Powlowski J, Shingler V (1994) Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600. Biodegradation 5 : 219-236
    • (1994) Biodegradation , vol.5 , pp. 219-236
    • Powlowski, J.1    Shingler, V.2
  • 38
    • 0030029182 scopus 로고    scopus 로고
    • Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: Engineering a mobile aromatic degradative cluster
    • Prieto MA, Diaz E, Garcia JL (1996) Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: engineering a mobile aromatic degradative cluster. J Bacteriol 178 : 111-120
    • (1996) J Bacteriol , vol.178 , pp. 111-120
    • Prieto, M.A.1    Diaz, E.2    Garcia, J.L.3
  • 39
    • 0019778558 scopus 로고
    • 3,4-dihydroxyphenylacetate 2,3-dioxygenase: A manganese(II) dioxygenase from Bacillus brevis
    • Que L Jr, Widom J, Crawford RL (1981) 3,4-Dihydroxyphenylacetate 2,3-dioxygenase: a manganese(II) dioxygenase from Bacillus brevis. J Biol Chem 256 : 10941-10944
    • (1981) J Biol Chem , vol.256 , pp. 10941-10944
    • Que L., Jr.1    Widom, J.2    Crawford, R.L.3
  • 40
    • 0018351747 scopus 로고
    • Construction of haloaromatics utilising bacteria
    • Reineke W, Kuackmuss H-J (1979) Construction of haloaromatics utilising bacteria. Nature 277 : 385-386
    • (1979) Nature , vol.277 , pp. 385-386
    • Reineke, W.1    Kuackmuss, H.-J.2
  • 41
    • 0027410220 scopus 로고
    • The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression
    • Roper DI, Fawcett T, Cooper RA (1993) The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression. Mol Gen Genet 237 : 241-250
    • (1993) Mol Gen Genet , vol.237 , pp. 241-250
    • Roper, D.I.1    Fawcett, T.2    Cooper, R.A.3
  • 43
    • 20644451612 scopus 로고    scopus 로고
    • Hrp12, a novel heat-responsive, tissue-specific, phosphorylated protein isolated from mouse liver
    • Samuel SJ, Tzung SP, Cohen SA (1997) Hrp12, a novel heat-responsive, tissue-specific, phosphorylated protein isolated from mouse liver. Hepatology 25 : 1213-1222
    • (1997) Hepatology , vol.25 , pp. 1213-1222
    • Samuel, S.J.1    Tzung, S.P.2    Cohen, S.A.3
  • 44
    • 0029806258 scopus 로고    scopus 로고
    • Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation
    • Schmiedeknecht G, et al (1996) Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation. Eur J Biochem 242 : 393-351
    • (1996) Eur J Biochem , vol.242 , pp. 393-351
    • Schmiedeknecht, G.1
  • 45
    • 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, et al (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
  • 46
    • 0029007418 scopus 로고
    • Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45
    • Somerville CC, Nishino SF, Spain JC (1995) Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45. J Bacteriol 177 : 3837-3842
    • (1995) J Bacteriol , vol.177 , pp. 3837-3842
    • Somerville, C.C.1    Nishino, S.F.2    Spain, J.C.3
  • 47
    • 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 EL, Kawamukai M, Sanvoisin J, Braven H, Bugg TD (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.5
  • 48
    • 0003181453 scopus 로고    scopus 로고
    • Facts & figures for the chemical industry
    • Storck WJ, et al (1996) Facts & figures for the chemical industry. Chem Eng News June 24 : 38-79
    • (1996) Chem Eng News June , vol.24 , pp. 38-79
    • Storck, W.J.1
  • 49
    • 0030990383 scopus 로고    scopus 로고
    • Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme
    • Takenaka S, Murakami S, Shinke R, Hatakeyama K, Yukawa H, Aoki K (1997) Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J Biol Chem 272 : 14727-14732
    • (1997) J Biol Chem , vol.272 , pp. 14727-14732
    • Takenaka, S.1    Murakami, S.2    Shinke, R.3    Hatakeyama, K.4    Yukawa, H.5    Aoki, K.6
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DJ, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 : 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 51
    • 0030066104 scopus 로고    scopus 로고
    • Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis CM-2
    • Whiting AK, Boldt YR, Hendrich MP, Wackett LP, Que L Jr (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., Jr.5
  • 52
    • 0028672045 scopus 로고
    • The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas
    • Williams PA, Sayers JR (1994) The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas. Biodegradation 5 : 195-217
    • (1994) Biodegradation , vol.5 , pp. 195-217
    • Williams, P.A.1    Sayers, J.R.2
  • 54
    • 0342872072 scopus 로고    scopus 로고
    • Novel organization of catechol meta pathway genes in Sphingomonas sp. HV3 pSKY4 plasmid
    • Yrjala K, Paulin L, Romantschuk M (1997) Novel organization of catechol meta pathway genes in Sphingomonas sp. HV3 pSKY4 plasmid. FEMS Microbiol Lett 154 : 403-408
    • (1997) FEMS Microbiol Lett , vol.154 , pp. 403-408
    • Yrjala, K.1    Paulin, L.2    Romantschuk, M.3


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