메뉴 건너뛰기




Volumn 4, Issue 12, 2002, Pages 824-841

Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440

Author keywords

[No Author keywords available]

Indexed keywords

ADIPIC ACIDS; BACTERIAL PROTEINS; BASE COMPOSITION; BASE SEQUENCE; BIODEGRADATION, ENVIRONMENTAL; GENES, BACTERIAL; GENOME, BACTERIAL; HETEROCYCLIC COMPOUNDS; HYDROCARBONS, AROMATIC; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PSEUDOMONAS PUTIDA;

EID: 0036933805     PISSN: 14622912     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1462-2920.2002.00370.x     Document Type: Article
Times cited : (418)

References (74)
  • 2
    • 0037089140 scopus 로고    scopus 로고
    • Species-specific repetitive extragenic palindromic (REP) sequences in Pseudomonas putida
    • Aranda-Olmedo, I., Tobes, R., Manzanera, M., Ramos, J.L., and Marqués, S. (2002) Species-specific repetitive extragenic palindromic (REP) sequences in Pseudomonas putida. Nucleic Acids Res 30: 1826-1833.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1826-1833
    • Aranda-Olmedo, I.1    Tobes, R.2    Manzanera, M.3    Ramos, J.L.4    Marqués, S.5
  • 3
    • 0025005226 scopus 로고
    • The TOL plasmids: Determinants of the catabolism of toluene and the xylenes
    • Assinder, S.J., and Williams, P.A. (1990) The TOL plasmids: Determinants of the catabolism of toluene and the xylenes. Adv Microbiol Physiol 31: 1-69.
    • (1990) Adv Microbiol Physiol , vol.31 , pp. 1-69
    • Assinder, S.J.1    Williams, P.A.2
  • 4
    • 0019805971 scopus 로고
    • Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas
    • Bagdasarian, M., Lurz, R., Rückert, B., Franklin, F.C.H., Bagdasarian, M.M., and Timmis, K.N. (1981) Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas. Gene 16: 237-247.
    • (1981) Gene , vol.16 , pp. 237-247
    • Bagdasarian, M.1    Lurz, R.2    Rückert, B.3    Franklin, F.C.H.4    Bagdasarian, M.M.5    Timmis, K.N.6
  • 6
    • 0034977060 scopus 로고    scopus 로고
    • Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358
    • Bertani, I., Kojic, M., and Venturi, V. (2001) Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. Microbiology 147: 1611-1620.
    • (2001) Microbiology , vol.147 , pp. 1611-1620
    • Bertani, I.1    Kojic, M.2    Venturi, V.3
  • 7
    • 0035863067 scopus 로고    scopus 로고
    • The black cat/white cat principle of signal integration in bacterial promoters
    • Cases, I., and de Lorenzo, V. (2001) The black cat/white cat principle of signal integration in bacterial promoters. EMBO J 20: 1-11.
    • (2001) EMBO J , vol.20 , pp. 1-11
    • Cases, I.1    De Lorenzo, V.2
  • 8
    • 0031958208 scopus 로고    scopus 로고
    • Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator
    • Collier, L.S., Gaines, G.L.I., and Neidle, E.L. (1998) Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator. J Bacteriol 180: 2493-2501.
    • (1998) J Bacteriol , vol.180 , pp. 2493-2501
    • Collier, L.S.1    Gaines, G.L.I.2    Neidle, E.L.3
  • 9
    • 0033623422 scopus 로고    scopus 로고
    • BenR, a XylS homologue, regulates three different pathways of aromatic acid degradation in Pseudomonas putida
    • Cowles, C.E., Nichols, N.N., and Harwood, C.S. (2000) BenR, a XylS homologue, regulates three different pathways of aromatic acid degradation in Pseudomonas putida. J Bacteriol 182: 6339-6346.
    • (2000) J Bacteriol , vol.182 , pp. 6339-6346
    • Cowles, C.E.1    Nichols, N.N.2    Harwood, C.S.3
  • 10
    • 0023227045 scopus 로고
    • Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: Pathway description, mapping of mutations, and cloning of essential genes
    • Cuskey, S.M., Peccoraro, V., and Olsen, R.H. (1987) Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: Pathway description, mapping of mutations, and cloning of essential genes. J Bacteriol 169: 2398-2404.
    • (1987) J Bacteriol , vol.169 , pp. 2398-2404
    • Cuskey, S.M.1    Peccoraro, V.2    Olsen, R.H.3
  • 11
    • 0033000387 scopus 로고    scopus 로고
    • The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK
    • D'Argenio, D.A., Segura, A., Coco, W.M., Bünz, P.V., and Ornston, L.N. (1999) The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK. J Bacteriol 181: 3505-3515.
    • (1999) J Bacteriol , vol.181 , pp. 3505-3515
    • D'Argenio, D.A.1    Segura, A.2    Coco, W.M.3    Bünz, P.V.4    Ornston, L.N.5
  • 13
    • 0018099544 scopus 로고
    • Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida
    • Durham, D.R., and Perry, J.J. (1978) Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida. J Bacteriol 134: 837-843.
    • (1978) J Bacteriol , vol.134 , pp. 837-843
    • Durham, D.R.1    Perry, J.J.2
  • 14
    • 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
  • 15
    • 0028820070 scopus 로고
    • Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus
    • Elsemore, D.A., and Ornston, L.N. (1995) Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus. J Bacteriol 177: 5971-5978.
    • (1995) J Bacteriol , vol.177 , pp. 5971-5978
    • Elsemore, D.A.1    Ornston, L.N.2
  • 16
    • 0031024669 scopus 로고    scopus 로고
    • Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP
    • Eulberg, D., Golovleva, L.A., and Schlomann, M. (1997) Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP. J Bacteriol 179: 370-381.
    • (1997) J Bacteriol , vol.179 , pp. 370-381
    • Eulberg, D.1    Golovleva, L.A.2    Schlomann, M.3
  • 17
    • 0031909725 scopus 로고    scopus 로고
    • Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: Evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
    • Eulberg, D., Lakner, S., Golovleva, L.A., and Schlömann, M. (1998) Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: Evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J Bacteriol 180: 1072-1081.
    • (1998) J Bacteriol , vol.180 , pp. 1072-1081
    • Eulberg, D.1    Lakner, S.2    Golovleva, L.A.3    Schlömann, M.4
  • 18
    • 0040942636 scopus 로고    scopus 로고
    • Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue
    • Fernández-Cañón, J., and Peñalva, M.A. (1998) Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. J Biol Chem 273: 329-337.
    • (1998) J Biol Chem , vol.273 , pp. 329-337
    • Fernández-Cañón, J.1    Peñalva, M.A.2
  • 19
    • 0032476062 scopus 로고    scopus 로고
    • Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway
    • Ferrández, A., Miñambres, B., García, B., Olivera, E.R., Luengo, J.M., García, J.L., and Díaz, E. (1998) Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem 273: 25974-25986.
    • (1998) J Biol Chem , vol.273 , pp. 25974-25986
    • Ferrández, A.1    Miñambres, B.2    García, B.3    Olivera, E.R.4    Luengo, J.M.5    García, J.L.6    Díaz, E.7
  • 20
    • 0031944612 scopus 로고    scopus 로고
    • Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions
    • Fetzner, S. (1998) Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions. Appl Microbiol Biotechnol 49: 237-250.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 237-250
    • Fetzner, S.1
  • 21
    • 0005536404 scopus 로고
    • Molecular and functional analysis of the TOL plasmid pWW0 from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway
    • Franklin, F.C.H., Bagdasarian, M., Bagdasarian, M.M., and Timmis, K.N. (1981) Molecular and functional analysis of the TOL plasmid pWW0 from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway. Proc Natl Acad Sci USA 78: 7458-7462.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7458-7462
    • Franklin, F.C.H.1    Bagdasarian, M.2    Bagdasarian, M.M.3    Timmis, K.N.4
  • 22
    • 0032211968 scopus 로고    scopus 로고
    • Isolation and transposon mutagenesis of a Pseudomonas putida KT2442 toluene-resistant variant: Involvement of an efflux system in solvent resistance
    • Fukimori, F., Hirayama, H., Takami, H., Inoue, A., and Horikoshi, K. (1998) Isolation and transposon mutagenesis of a Pseudomonas putida KT2442 toluene-resistant variant: Involvement of an efflux system in solvent resistance. Extremophiles 2: 395-400.
    • (1998) Extremophiles , vol.2 , pp. 395-400
    • Fukimori, F.1    Hirayama, H.2    Takami, H.3    Inoue, A.4    Horikoshi, K.5
  • 23
    • 0035958746 scopus 로고    scopus 로고
    • The composite genome of the legume symbiont Sinorhizobium meliloti
    • Galibert, F., Finan, T.M., Long, S.R., Puhler, A., Abola, P., Ampe, F., et al. (2001) The composite genome of the legume symbiont Sinorhizobium meliloti. Science 293: 668-672.
    • (2001) Science , vol.293 , pp. 668-672
    • Galibert, F.1    Finan, T.M.2    Long, S.R.3    Puhler, A.4    Abola, P.5    Ampe, F.6
  • 24
    • 0035861511 scopus 로고    scopus 로고
    • Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58
    • Goodner, B., Hinkle, G., Gattung, S., Miller, N., Blanchard, M., Qurollo, B., et al. (2001) Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58. Science 294: 2323-2328.
    • (2001) Science , vol.294 , pp. 2323-2328
    • Goodner, B.1    Hinkle, G.2    Gattung, S.3    Miller, N.4    Blanchard, M.5    Qurollo, B.6
  • 25
    • 0031767240 scopus 로고    scopus 로고
    • PhhC is an essential aminotransferase for aromatic amino acid catabolism in Pseudomonas aeruginosa
    • Gu, W., Song, J., Bonner, C.A., Xie, G., and Jensen, R.A. (1998) PhhC is an essential aminotransferase for aromatic amino acid catabolism in Pseudomonas aeruginosa. Microbiology 144: 3127-3134.
    • (1998) Microbiology , vol.144 , pp. 3127-3134
    • Gu, W.1    Song, J.2    Bonner, C.A.3    Xie, G.4    Jensen, R.A.5
  • 26
    • 0031042325 scopus 로고    scopus 로고
    • Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca
    • Hacisalihoglu, A., Jongejan, J.A., and Duine, J.A. (1997) Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology 143: 505-512.
    • (1997) Microbiology , vol.143 , pp. 505-512
    • Hacisalihoglu, A.1    Jongejan, J.A.2    Duine, J.A.3
  • 27
    • 0000494359 scopus 로고
    • Catabolism of aromatic hydrocarbons by Pseudomonas
    • Hopwood, A., and Chater, K.F. (eds). London: Academic Press
    • Harayama, S., and Timmis, K.N. (1989) Catabolism of aromatic hydrocarbons by Pseudomonas. In Genetics of Bacterial Diversity. Hopwood, A., and Chater, K.F. (eds). London: Academic Press, pp. 151-174.
    • (1989) Genetics of Bacterial Diversity , pp. 151-174
    • Harayama, S.1    Timmis, K.N.2
  • 28
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood, C.S., and Parales, R.E. (1996) The β-ketoadipate pathway and the biology of self-identity. Annu Rev Microbiol 50: 553-590.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 29
    • 0028172818 scopus 로고
    • Identification of the pcaRKF gene cluster from Pseudomonas putida: Involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate
    • Harwood, C.S., Nichols, N.N., Kim, M.-K., Ditty, J.L., and Parales, R.E. (1994) Identification of the pcaRKF gene cluster from Pseudomonas putida: Involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate. J Bacteriol 176: 6479-6488.
    • (1994) J Bacteriol , vol.176 , pp. 6479-6488
    • Harwood, C.S.1    Nichols, N.N.2    Kim, M.-K.3    Ditty, J.L.4    Parales, R.E.5
  • 30
    • 0020032290 scopus 로고
    • Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans
    • Hawkins, A.R., Giles, N.H., and Kinghorn, J.R. (1982) Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem Genet 20: 271-286.
    • (1982) Biochem Genet , vol.20 , pp. 271-286
    • Hawkins, A.R.1    Giles, N.H.2    Kinghorn, J.R.3
  • 31
    • 0024103054 scopus 로고
    • Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans
    • Hawkins, A.R., Lamb, H.K., Smith, M., Keyte, J.W., and Roberts, C.F. (1988) Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans. Mol Gen Genet 214: 224-231.
    • (1988) Mol Gen Genet , vol.214 , pp. 224-231
    • Hawkins, A.R.1    Lamb, H.K.2    Smith, M.3    Keyte, J.W.4    Roberts, C.F.5
  • 33
    • 0015458822 scopus 로고
    • Quinate metabolism in Pseudomonas aeruginosa
    • Ingledew, W.M., and Tai, C.C. (1972) Quinate metabolism in Pseudomonas aeruginosa. Can J Microbiol 18: 1817-1824.
    • (1972) Can J Microbiol , vol.18 , pp. 1817-1824
    • Ingledew, W.M.1    Tai, C.C.2
  • 34
    • 0020680275 scopus 로고
    • Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp.
    • Iwaki, M., Yagi, T., Horiike, K., Saeki, Y., Ushijima, T., and Nozaki, M. (1983) Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp. Arch Biochem Biophys 220: 253-262.
    • (1983) Arch Biochem Biophys , vol.220 , pp. 253-262
    • Iwaki, M.1    Yagi, T.2    Horiike, K.3    Saeki, Y.4    Ushijima, T.5    Nozaki, M.6
  • 35
    • 0026718930 scopus 로고
    • Characterization of Pseudomonas putida mutants unable to catabolize benzoate: Cloning and characterization of Pseudomonas genes involved in benzoate catabolism and isolation of a chromosomal DNA fragment able to substitute for xylS in activation of the TOL lower-pathway promoter
    • Jeffrey, W.H., Cuskey, S.M., Chapman, P.J., Resnick, S., and Olsen, R.H. (1992) Characterization of Pseudomonas putida mutants unable to catabolize benzoate: Cloning and characterization of Pseudomonas genes involved in benzoate catabolism and isolation of a chromosomal DNA fragment able to substitute for xylS in activation of the TOL lower-pathway promoter. J Bacteriol 174: 4986-4996.
    • (1992) J Bacteriol , vol.174 , pp. 4986-4996
    • Jeffrey, W.H.1    Cuskey, S.M.2    Chapman, P.J.3    Resnick, S.4    Olsen, R.H.5
  • 36
    • 0034750149 scopus 로고    scopus 로고
    • The TOL plasmid pWW0 xylN gene product from Pseudomonas putida is involved in m-xylene uptake
    • Kasai, Y., Inoue, J., and Harayama, S. (2001) The TOL plasmid pWW0 xylN gene product from Pseudomonas putida is involved in m-xylene uptake. J Bacteriol 183: 6662-6666.
    • (2001) J Bacteriol , vol.183 , pp. 6662-6666
    • Kasai, Y.1    Inoue, J.2    Harayama, S.3
  • 37
    • 0023740409 scopus 로고
    • Cloning and expression of the catA and catBC gene clusters from Pseudomonas aeruginosa PAO
    • Kukor, J.J., Olsen, R.H., and Ballou, D.P. (1988) Cloning and expression of the catA and catBC gene clusters from Pseudomonas aeruginosa PAO. J Bacteriol 170: 4458-4465.
    • (1988) J Bacteriol , vol.170 , pp. 4458-4465
    • Kukor, J.J.1    Olsen, R.H.2    Ballou, D.P.3
  • 38
    • 0034306448 scopus 로고    scopus 로고
    • Gene context conservation of a higher order than operons
    • Lathe, W.C., Ill, Snel, B., and Bork, P. (2000) Gene context conservation of a higher order than operons. Trends Biochem Sci 25: 474-479.
    • (2000) Trends Biochem Sci , vol.25 , pp. 474-479
    • Lathe W.C. III1    Snel, B.2    Bork, P.3
  • 39
    • 0035057115 scopus 로고    scopus 로고
    • The phenylacetyl-CoA catabolon: A complex catabolic unit with broad biotechnological applications
    • Luengo, J.M., García, J.L., and Olivera, E.R. (2001) The phenylacetyl-CoA catabolon: A complex catabolic unit with broad biotechnological applications. Mol Microbiol 39: 1434-1442.
    • (2001) Mol Microbiol , vol.39 , pp. 1434-1442
    • Luengo, J.M.1    García, J.L.2    Olivera, E.R.3
  • 40
    • 0032935821 scopus 로고    scopus 로고
    • Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine
    • Milcamps, A., and de Bruijn, F.J. (1999) Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine. Microbiology 145: 935-947.
    • (1999) Microbiology , vol.145 , pp. 935-947
    • Milcamps, A.1    De Bruijn, F.J.2
  • 41
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 42
    • 0033134220 scopus 로고    scopus 로고
    • 4-Hydroxycinnamoyl-CoA hydratase/lyase (HCHL) - An enzyme of phenylpropanoid chain cleavage from Pseudomonas
    • Mitra, A., Kitamura, Y., Gasson, M.J., Narbad, A., Parr, A.J., Payne, J., et al. (1999) 4-Hydroxycinnamoyl-CoA hydratase/lyase (HCHL) - An enzyme of phenylpropanoid chain cleavage from Pseudomonas. Arch Biochem Biophys 365: 10-16.
    • (1999) Arch Biochem Biophys , vol.365 , pp. 10-16
    • Mitra, A.1    Kitamura, Y.2    Gasson, M.J.3    Narbad, A.4    Parr, A.J.5    Payne, J.6
  • 43
    • 0036360982 scopus 로고    scopus 로고
    • Aerobic metabolism of phenylacetic acids in Azoarcus evansii
    • Mohamed, M.E., Ismail, W., Heider, J., and Fuchs, G. (2002) Aerobic metabolism of phenylacetic acids in Azoarcus evansii. Arch Microbiol 178: 180-192.
    • (2002) Arch Microbiol , vol.178 , pp. 180-192
    • Mohamed, M.E.1    Ismail, W.2    Heider, J.3    Fuchs, G.4
  • 44
    • 0034212264 scopus 로고    scopus 로고
    • Repression of Acinetobacter vanillate demethylase synthesis by VanR, a member of the GntR family of transcriptional regulators
    • Morawski, B., Segura, A., and Ornston, L.N. (2000) Repression of Acinetobacter vanillate demethylase synthesis by VanR, a member of the GntR family of transcriptional regulators. FEMS Microbiol Lett 187: 65-68.
    • (2000) FEMS Microbiol Lett , vol.187 , pp. 65-68
    • Morawski, B.1    Segura, A.2    Ornston, L.N.3
  • 45
    • 0025159432 scopus 로고
    • Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1
    • Nakai, C., Horiike, K., Kuramitsu, S., Kagamiyama, H., and Nozaki, M. (1990) Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, and 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
  • 46
    • 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., Uyeyama, H., Kagamiyama, H., Nakazawa, T., Inouye, S., Kishi, F., et al. (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 321: 353-362.
    • (1995) Arch Biochem Biophys , vol.321 , pp. 353-362
    • Nakai, C.1    Uyeyama, H.2    Kagamiyama, H.3    Nakazawa, T.4    Inouye, S.5    Kishi, F.6
  • 47
    • 0030818839 scopus 로고    scopus 로고
    • PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida
    • Nichols, N.N., and Harwood, C.S. (1997) PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida. J Bacteriol 179: 5056-5061.
    • (1997) J Bacteriol , vol.179 , pp. 5056-5061
    • Nichols, N.N.1    Harwood, C.S.2
  • 50
    • 0035117157 scopus 로고    scopus 로고
    • Two different pathways are involved in the β-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U: Genetic studies and biotechnological applications
    • Olivera, E.R., Carnicero, D., García, B., Miñambres, B., Moreno, M.A., Cañedo, L., et al. (2001) Two different pathways are involved in the β-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U: Genetic studies and biotechnological applications. Mol Microbiol 39: 863-874.
    • (2001) Mol Microbiol , vol.39 , pp. 863-874
    • Olivera, E.R.1    Carnicero, D.2    García, B.3    Miñambres, B.4    Moreno, M.A.5    Cañedo, L.6
  • 51
    • 0026481406 scopus 로고
    • Traits of fluorescent Pseudomonas spp. involved in suppression of plant root pathogens
    • O'Sullivan, D.J., and O'Gara, F. (1992) Traits of fluorescent Pseudomonas spp. involved in suppression of plant root pathogens. Microbiol Rev 56: 662-676.
    • (1992) Microbiol Rev , vol.56 , pp. 662-676
    • O'Sullivan, D.J.1    O'Gara, F.2
  • 52
    • 0032703295 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. strain HR199
    • Overhage, J., Priefert, H., and Steinbüchel, A. (1999) Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. strain HR199. Appl Environ Microbiol 65: 4837-4847.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4837-4847
    • Overhage, J.1    Priefert, H.2    Steinbüchel, A.3
  • 53
    • 0036277082 scopus 로고    scopus 로고
    • Bacterial chemotaxis to pollutants and plant-derived aromatic molecules
    • Parales, R.E., and Harwood, C.S. (2002) Bacterial chemotaxis to pollutants and plant-derived aromatic molecules. Curr Opin Microbiol 5: 266-273.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 266-273
    • Parales, R.E.1    Harwood, C.S.2
  • 54
    • 0030041622 scopus 로고    scopus 로고
    • Characterization of PcaQ, a LysR-type transcriptional activator required for catabolism of phenolic compounds, from Agrobacterium tumefaciens
    • Parke, D. (1996) Characterization of PcaQ, a LysR-type transcriptional activator required for catabolism of phenolic compounds, from Agrobacterium tumefaciens. J Bacteriol 178: 266-272.
    • (1996) J Bacteriol , vol.178 , pp. 266-272
    • Parke, D.1
  • 55
    • 0033987616 scopus 로고    scopus 로고
    • Bacteria are not what they eat: That is why they are so diverse
    • Parke, D., D'Argenio, D.A., and Ornston, L.N. (2000) Bacteria are not what they eat: That is why they are so diverse. J Bacteriol 182: 257-263.
    • (2000) J Bacteriol , vol.182 , pp. 257-263
    • Parke, D.1    D'Argenio, D.A.2    Ornston, L.N.3
  • 56
    • 0035490405 scopus 로고    scopus 로고
    • Cloning and genetic characterization of dca genes required for β-oxidation of straight-chain dicarboxylic acids in Acinetobacter sp. strain ADP1
    • Parke, D., García, M.A., and Ornston, L.N. (2001) Cloning and genetic characterization of dca genes required for β-oxidation of straight-chain dicarboxylic acids in Acinetobacter sp. strain ADP1. Appl Environ Microbiol 67: 4817-4827.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4817-4827
    • Parke, D.1    García, M.A.2    Ornston, L.N.3
  • 57
    • 0030981938 scopus 로고    scopus 로고
    • Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate
    • Priefert, H., Rabenhorst, J., and Steinbüchel, A. (1997) Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J Bacteriol 179: 2595-2607.
    • (1997) J Bacteriol , vol.179 , pp. 2595-2607
    • Priefert, H.1    Rabenhorst, J.2    Steinbüchel, A.3
  • 59
    • 0035819564 scopus 로고    scopus 로고
    • Analysis of the pobA and pobR genes controlling expression of p-hydroxybenzoate hydroxylase in Azotobacter chroococcum
    • Quinn, J.A., McKay, D.B., and Entsch, B. (2001) Analysis of the pobA and pobR genes controlling expression of p-hydroxybenzoate hydroxylase in Azotobacter chroococcum. Gene 264: 77-85.
    • (2001) Gene , vol.264 , pp. 77-85
    • Quinn, J.A.1    McKay, D.B.2    Entsch, B.3
  • 61
    • 0031780304 scopus 로고    scopus 로고
    • Efflux pumps involved in toluene tolerance in Pseudomonas putida DOT-T1E
    • Ramos, J.L., Duque, E., Godoy, P., and Segura, A. (1998) Efflux pumps involved in toluene tolerance in Pseudomonas putida DOT-T1E. J Bacteriol 180: 3323-3329.
    • (1998) J Bacteriol , vol.180 , pp. 3323-3329
    • Ramos, J.L.1    Duque, E.2    Godoy, P.3    Segura, A.4
  • 62
    • 0023644204 scopus 로고
    • Assemblage of ortho cleavage route for simultaneous degradation of chloro- and methylaromatics
    • Rojo, F., Pieper, D.H., Engesser, K.-H., Knackmuss, H.-J., and Timmis, K.N. (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
  • 63
    • 0031733149 scopus 로고    scopus 로고
    • Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea, and eukarya
    • Saier, M.H., Jr (1998) Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea, and eukarya. Adv Microb Physiol 40: 81-136.
    • (1998) Adv Microb Physiol , vol.40 , pp. 81-136
    • Saier M.H., Jr.1
  • 64
    • 0345346392 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing vanA and vanB, genes required for conversion of either ferulate or vanillate to protocatechuate in Acinetobacter
    • Segura, A., Bünz, P.V., D'Argenio, D.A., and Ornston, L.N. (1999) Genetic analysis of a chromosomal region containing vanA and vanB, genes required for conversion of either ferulate or vanillate to protocatechuate in Acinetobacter. J Bacteriol 181: 3494-3504.
    • (1999) J Bacteriol , vol.181 , pp. 3494-3504
    • Segura, A.1    Bünz, P.V.2    D'Argenio, D.A.3    Ornston, L.N.4
  • 65
    • 0033566995 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway
    • Serre, L., Sailland, A., Sy, D., Boudec, P., Rolland, A., Pebay-Peyroula, E., and Cohen-Addad, C. (1999) Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway. Structure 7: 977-988.
    • (1999) Structure , vol.7 , pp. 977-988
    • Serre, L.1    Sailland, A.2    Sy, D.3    Boudec, P.4    Rolland, A.5    Pebay-Peyroula, E.6    Cohen-Addad, C.7
  • 66
    • 0029808625 scopus 로고    scopus 로고
    • PhhR, a divergently transcribed activator of the phenylalanine hydroxylase gene cluster of Pseudomonas aeruginosa
    • Song, J., and Jensen, R.A. (1996) PhhR, a divergently transcribed activator of the phenylalanine hydroxylase gene cluster of Pseudomonas aeruginosa. Mol Microbiol 22: 497-507.
    • (1996) Mol Microbiol , vol.22 , pp. 497-507
    • Song, J.1    Jensen, R.A.2
  • 67
    • 0032953634 scopus 로고    scopus 로고
    • PhhB, a Pseudomonas aeruginosa homolog of mammalian pterin 4a-carbinolamine dehydratase/DcoH, does not regulate expression of phenylalanine hydroxylase at the transcriptional level
    • Song, J., Xia, T., and Jensen, R.A. (1999) PhhB, a Pseudomonas aeruginosa homolog of mammalian pterin 4a-carbinolamine dehydratase/DcoH, does not regulate expression of phenylalanine hydroxylase at the transcriptional level. J Bacteriol 181: 2789-2796.
    • (1999) J Bacteriol , vol.181 , pp. 2789-2796
    • Song, J.1    Xia, T.2    Jensen, R.A.3
  • 69
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
    • Stover, C.K., Pham, X.Q., Erwin, A.L., Mizoguchi, S.D., Warrener, P., Hickey, M.J., et al. (2000) Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature 406: 959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1    Pham, X.Q.2    Erwin, A.L.3    Mizoguchi, S.D.4    Warrener, P.5    Hickey, M.J.6
  • 70
    • 0034327380 scopus 로고    scopus 로고
    • Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis
    • Takami, H., Nakasone, K., Takaki, Y., Maeno, G., Sasaki, Y., Masui, N., et al. (2000) Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. Nucleic Acids Res 28: 4317-4331.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4317-4331
    • Takami, H.1    Nakasone, K.2    Takaki, Y.3    Maeno, G.4    Sasaki, Y.5    Masui, N.6
  • 71
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-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.G.2    Gibson, T.J.3
  • 72
    • 0031956615 scopus 로고    scopus 로고
    • Genetics of ferulic acid bioconversion to protocatechuic acid in plant-growth-promoting Pseudomonas putida WCS358
    • Venturi, V., Zennaro, F., Degrassi, G., Okeke, B.C., and Bruschi, C.V. (1998) Genetics of ferulic acid bioconversion to protocatechuic acid in plant-growth-promoting Pseudomonas putida WCS358. Microbiology 144: 965-973.
    • (1998) Microbiology , vol.144 , pp. 965-973
    • Venturi, V.1    Zennaro, F.2    Degrassi, G.3    Okeke, B.C.4    Bruschi, C.V.5
  • 73
    • 0020714456 scopus 로고
    • Rapid similarity searches of nucleic acid and protein data banks
    • Wilbur, W.J., and Lipman, D.J. (1983) Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci USA 80: 726-730.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 726-730
    • Wilbur, W.J.1    Lipman, D.J.2
  • 74
    • 0030864852 scopus 로고    scopus 로고
    • Group II intron from Pseudomonas alcaligenes NCIB 9867 (P25X): Entrapment in plasmid RP4 and sequence analysis
    • Yeo, C.C., Tham, J.M., Yap, M.W.-C., and Poh, C.L. (1997) Group II intron from Pseudomonas alcaligenes NCIB 9867 (P25X): Entrapment in plasmid RP4 and sequence analysis. Microbiology 143: 2833-2840.
    • (1997) Microbiology , vol.143 , pp. 2833-2840
    • Yeo, C.C.1    Tham, J.M.2    Yap, M.W.-C.3    Poh, C.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.