메뉴 건너뛰기




Volumn 179, Issue 8, 1997, Pages 2573-2581

Genetic characterization and expression in heterologous hosts of the 3- (3-hydroxyphenyl) propionate catabolic pathway of Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

PROPIONIC ACID DERIVATIVE;

EID: 0030948489     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.8.2573-2581.1997     Document Type: Article
Times cited : (79)

References (78)
  • 2
    • 0022443952 scopus 로고
    • Comparative analysis of different Pseudomonas strains that degrade cinnamic acid
    • Andreoni, V., and G. Bestetti. 1986. Comparative analysis of different Pseudomonas strains that degrade cinnamic acid. Appl. Environ. Microbiol. 52:930-934.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 930-934
    • Andreoni, V.1    Bestetti, G.2
  • 3
    • 0028278158 scopus 로고
    • Structural and functional diversity among bacterial interspersed mosaic elements (BIMEs)
    • Bachellier, S., W. Saurin, D. Perrin, M. Hofnung, and E. Gilson. 1994. Structural and functional diversity among bacterial interspersed mosaic elements (BIMEs). Mol. Microbiol. 12:61-70.
    • (1994) Mol. Microbiol. , vol.12 , pp. 61-70
    • Bachellier, S.1    Saurin, W.2    Perrin, D.3    Hofnung, M.4    Gilson, E.5
  • 4
  • 5
    • 0024818293 scopus 로고
    • Complete maps of IS1, IS2, IS3, IS4, IS5, IS30, and IS50 locations in Escherichia coli K12
    • Birkenbihl, R. P., and W. Vielmetter. 1989. Complete maps of IS1, IS2, IS3, IS4, IS5, IS30, and IS50 locations in Escherichia coli K12. Mol. Gen. Genet. 220:147-153.
    • (1989) Mol. Gen. Genet. , vol.220 , pp. 147-153
    • Birkenbihl, R.P.1    Vielmetter, W.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0024571640 scopus 로고
    • The helix-turn-helix DNA bind- Ing motif
    • Brennan, R. G., and B. W. Matthews. 1989. The helix-turn-helix DNA bind- ing motif. J. Biol. Chem. 264:1903-1906.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1903-1906
    • Brennan, R.G.1    Matthews, B.W.2
  • 8
    • 0027431230 scopus 로고
    • Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli
    • Bugg, T. D. H. 1993. Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli. Biochim. Biophys. Acta 1202:258-264.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 258-264
    • Bugg, T.D.H.1
  • 9
    • 0020625023 scopus 로고
    • Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli
    • Burlingame, R., and P. J. Chapman. 1983. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155:113-121.
    • (1983) J. Bacteriol. , vol.155 , pp. 113-121
    • Burlingame, R.1    Chapman, P.J.2
  • 10
    • 0020504898 scopus 로고
    • Stereospecificity in meta-fission catabolic pathways
    • Burlingame, R., and P. J. Chapman. 1983. Stereospecificity in meta-fission catabolic pathways. J. Bacteriol. 155:424-426.
    • (1983) J. Bacteriol. , vol.155 , pp. 424-426
    • Burlingame, R.1    Chapman, P.J.2
  • 11
    • 85036441249 scopus 로고
    • Ph.D. thesis. University of Minnesota, Minneapolis
    • Burlingame, R. P. 1983. Ph.D. thesis. University of Minnesota, Minneapolis.
    • (1983)
    • Burlingame, R.P.1
  • 12
    • 0022483943 scopus 로고
    • Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation
    • Burlingame, R. P., L. Wyman, and P. J. Chapman. 1986. Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation. J. Bacteriol. 168:55-64.
    • (1986) J. Bacteriol. , vol.168 , pp. 55-64
    • Burlingame, R.P.1    Wyman, L.2    Chapman, P.J.3
  • 13
    • 0002657642 scopus 로고
    • DNA replication and the division cycle of Escherichia coli
    • Clark, D. J., and O. Maaloe. 1967. DNA replication and the division cycle of Escherichia coli. J. Mol. Biol. 23:99-112.
    • (1967) J. Mol. Biol. , vol.23 , pp. 99-112
    • Clark, D.J.1    Maaloe, O.2
  • 14
    • 0017085802 scopus 로고
    • A colony bank containing synthetic ColE1 hybrid plasmids representative of the entire E. coli genome
    • Clarke, L., and J. Carbon. 1976. A colony bank containing synthetic ColE1 hybrid plasmids representative of the entire E. coli genome. Cell 9:91-99.
    • (1976) Cell , vol.9 , pp. 91-99
    • Clarke, L.1    Carbon, J.2
  • 15
    • 0006678940 scopus 로고
    • Microbiological degradation of trans-cinnamic acid by soil Pseudomonas
    • Coulson, C. B., and W. C. Evans. 1959. Microbiological degradation of trans-cinnamic acid by soil Pseudomonas. Chem. Ind. 17:543-544.
    • (1959) Chem. Ind. , vol.17 , pp. 543-544
    • Coulson, C.B.1    Evans, W.C.2
  • 16
    • 0013823373 scopus 로고
    • The metabolism of β-phenylpropionic acid by an Achromobacter
    • Dagley, S., P. J. Chapman, and D. T. Gibson. 1965. The metabolism of β-phenylpropionic acid by an Achromobacter. Biochem. J. 97:643-650.
    • (1965) Biochem. J. , vol.97 , pp. 643-650
    • Dagley, S.1    Chapman, P.J.2    Gibson, D.T.3
  • 17
    • 0027243104 scopus 로고
    • Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens
    • Decker, H., H. Motamedi, and C. R. Hutchinson. 1993. Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens. J. Bacteriol. 175:3876-3886.
    • (1993) J. Bacteriol. , vol.175 , pp. 3876-3886
    • Decker, H.1    Motamedi, H.2    Hutchinson, C.R.3
  • 18
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- And Tn10-derived minitransposons
    • de Lorenzo, V., and K. N. Timmis. 1994. Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Methods Hnzymol. 235:386-405.
    • (1994) Methods Hnzymol. , vol.235 , pp. 386-405
    • De Lorenzo, V.1    Timmis, K.N.2
  • 20
    • 0028943123 scopus 로고
    • Identification of functional residues in a 2-hydroxymuconic scmialdehyde hydrolase. A new member of the α/β hydrolase-fold family of enzymes which cleaves carbon-carbon bonds
    • Díaz, E., and K. N. Timmis. 1995. Identification of functional residues in a 2-hydroxymuconic scmialdehyde hydrolase. A new member of the α/β hydrolase-fold family of enzymes which cleaves carbon-carbon bonds. J. Biol. Chem. 270:6403-6411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6403-6411
    • Díaz, E.1    Timmis, K.N.2
  • 21
    • 0027978161 scopus 로고
    • Universal barrier to lateral spread of specific genes among microorganisms
    • Díaz, E., M. Munthali, V. de Lorenzo, and K. N. Timmis. 1994. Universal barrier to lateral spread of specific genes among microorganisms. Mol. Microbiol. 13:855-861.
    • (1994) Mol. Microbiol. , vol.13 , pp. 855-861
    • Díaz, E.1    Munthali, M.2    De Lorenzo, V.3    Timmis, K.N.4
  • 22
    • 0028365190 scopus 로고
    • Regulation of p-hydroxybenzoate hydroxylase synthesis by PobR bound to an operator in Acinetobacter calcoaceticus
    • DiMarco, A. A., and L. N. Ornston. 1994. Regulation of p-hydroxybenzoate hydroxylase synthesis by PobR bound to an operator in Acinetobacter calcoaceticus. J. Bacteriol. 176:4277-4284.
    • (1994) J. Bacteriol. , vol.176 , pp. 4277-4284
    • Dimarco, A.A.1    Ornston, L.N.2
  • 23
    • 0027483332 scopus 로고
    • Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase, in an Acinetobacter calcoaceticus strain well-suited for genetic analysis
    • DiMarco, A. A., B. A. Averhoff, E. E. Kim, and L. N. Ornston. 1993. Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase, in an Acinetobacter calcoaceticus strain well-suited for genetic analysis. Gene 125:25-33.
    • (1993) Gene , vol.125 , pp. 25-33
    • Dimarco, A.A.1    Averhoff, B.A.2    Kim, E.E.3    Ornston, L.N.4
  • 24
    • 0027321256 scopus 로고
    • Identification of the transcriptional activator pobR and characterization of its role in the expression of pobA, the structural gene for p-hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus
    • DiMarco, A. A., B. Averhoff, and L. N. Ornston. 1993. Identification of the transcriptional activator pobR and characterization of its role in the expression of pobA, the structural gene for p-hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus. J. Bacteriol. 175:4499-4506.
    • (1993) J. Bacteriol. , vol.175 , pp. 4499-4506
    • Dimarco, A.A.1    Averhoff, B.2    Ornston, L.N.3
  • 25
    • 0022507290 scopus 로고
    • Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonas putida mt-2
    • Duggleby, C. J., and P. A. Williams. 1986. Purification and some properties of the 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (2-hydroxymuconic semialdehyde hydrolase) encoded by the TOL plasmid pWW0 from Pseudomonas putida mt-2. J. Gen. Microbiol. 132:717-726.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 717-726
    • Duggleby, C.J.1    Williams, P.A.2
  • 26
    • 0029864057 scopus 로고    scopus 로고
    • P-Cumate catabolic pathway in Pseudomonas putida F1: Cloning and characterization of DNA carrying the cmt operon
    • Eaton, R. W. 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
  • 27
    • 0029063837 scopus 로고
    • Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains
    • Fernández, S., V. de Lorenzo, and J. Peαrez-Martín. 1995. Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains. Mol. Microbiol. 16:205-213.
    • (1995) Mol. Microbiol. , vol.16 , pp. 205-213
    • Fernández, S.1    De Lorenzo, V.2    Perez-Martín, J.3
  • 28
    • 0023886015 scopus 로고
    • Posttranscriptional regulatory mechanisms in Escherichia coli
    • Gold, L. 1988. Posttranscriptional regulatory mechanisms in Escherichia coli. Annu. Rev. Biochem. 57:199-233.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 199-233
    • Gold, L.1
  • 29
    • 0027232202 scopus 로고
    • Comparison of the nucleotide sequences of the meta-cleavage pathway genes of TOL plasmid pWW0 from Pseudomonas putida with other meta-cleavage genes suggests that both single and multiple nucleotide substitutions contribute to enzyme evolution
    • Harayama, S., and M. Rekik. 1993. Comparison of the nucleotide sequences of the meta-cleavage pathway genes of TOL plasmid pWW0 from Pseudomonas putida with other meta-cleavage genes suggests that both single and multiple nucleotide substitutions contribute to enzyme evolution. Mol. Gen. Genet. 239:81-89.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 81-89
    • Harayama, S.1    Rekik, M.2
  • 30
    • 0028172818 scopus 로고
    • Identification of the pcaRKF gene cluster from Pseudomonas putida: Involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate
    • Harwood, C. S., N. N. Nichols, M.-K. Kim, J. L. Ditty, and R. E. Parales. 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
  • 31
    • 0025296087 scopus 로고
    • The homologous glucose transport proteins of prokaryotes and eukaryotes
    • Henderson, P. J. F. 1990. The homologous glucose transport proteins of prokaryotes and eukaryotes. Res. Microbiol. 141:316-328.
    • (1990) Res. Microbiol. , vol.141 , pp. 316-328
    • Henderson, P.J.F.1
  • 32
    • 0028287911 scopus 로고
    • The biphenyl/polychlorinated biphenyl-degradation locus (bph) of Pseudomonas sp. LB400 encodes four additional metabolic enzymes
    • Hofer, B., S. Backhaus, and K. N. Timmis. 1994. The biphenyl/polychlorinated biphenyl-degradation locus (bph) of Pseudomonas sp. LB400 encodes four additional metabolic enzymes. Gene 144:9-16.
    • (1994) Gene , vol.144 , pp. 9-16
    • Hofer, B.1    Backhaus, S.2    Timmis, K.N.3
  • 34
    • 0029762461 scopus 로고    scopus 로고
    • A stringently controlled expression system for analysing lateral gene transfer between bacteria
    • Jaenecke, S., V. de Lorenzo, K. N. Timmis, and E. Díaz. 1996. A stringently controlled expression system for analysing lateral gene transfer between bacteria. Mol. Microbiol. 21:293-300.
    • (1996) Mol. Microbiol. , vol.21 , pp. 293-300
    • Jaenecke, S.1    De Lorenzo, V.2    Timmis, K.N.3    Díaz, E.4
  • 35
    • 0025296680 scopus 로고
    • Nucleotide sequence of metapyrocat- Echase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222
    • Kabisch, M., and P. Fortnagel. 1990. Nucleotide sequence of metapyrocat- echase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222. Nucleic Acids Res. 18:3405-3406.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3405-3406
    • Kabisch, M.1    Fortnagel, P.2
  • 36
    • 0028241452 scopus 로고
    • Nucleotide sequence and functional analysis of the meta-cleavage pathway involved in biphenyl and polychlorinated biphenyl degradation in Pseudomonas sp. strain KKS102
    • Kikuchi, Y., Y. Yasukochi, Y. Nagata, M. Fukuda, and M. Takagi. 1994. Nucleotide sequence and functional analysis of the meta-cleavage pathway involved in biphenyl and polychlorinated biphenyl degradation in Pseudomonas sp. strain KKS102. J. Bacteriol. 176:4269-4276.
    • (1994) J. Bacteriol. , vol.176 , pp. 4269-4276
    • Kikuchi, Y.1    Yasukochi, Y.2    Nagata, Y.3    Fukuda, M.4    Takagi, M.5
  • 37
    • 0028040511 scopus 로고
    • Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon
    • Kowalchuk, G. A., G. B. Hartnett, A. Benson, J. E. Houghton, K.-L. Ngai, and L. N. Ornston. 1994. Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon. Gene 146:23-30.
    • (1994) Gene , vol.146 , pp. 23-30
    • Kowalchuk, G.A.1    Hartnett, G.B.2    Benson, A.3    Houghton, J.E.4    Ngai, K.-L.5    Ornston, L.N.6
  • 38
    • 0029991334 scopus 로고    scopus 로고
    • Compilation of DNA sequences of Escherichia coli K12 (ECD and ECDC: Update 1995)
    • Kröger, M., and R. Wahl. 1996. Compilation of DNA sequences of Escherichia coli K12 (ECD and ECDC: update 1995). Nucleic Acids Res. 24:29-31.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 29-31
    • Kröger, M.1    Wahl, R.2
  • 39
    • 37049081027 scopus 로고
    • Chemistry of extradiol aromatic ring cleavage: Isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic cleavage
    • Lam, W. W. Y., and T. D. H. Bugg. 1994. Chemistry of extradiol aromatic ring cleavage: isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic cleavage. J. Chem. Soc. Chem. Commun. 1994:1163-1164.
    • (1994) J. Chem. Soc. Chem. Commun. , vol.1994 , pp. 1163-1164
    • Lam, W.W.Y.1    Bugg, T.D.H.2
  • 40
    • 0019944629 scopus 로고
    • Discontinuity of homology of Escherichia coli and Salmonella typhimurium DNA in the lac region
    • Lampel, K. A., and M. Riley. 1982. Discontinuity of homology of Escherichia coli and Salmonella typhimurium DNA in the lac region. Mol. Gen. Genet. 186:82-86.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 82-86
    • Lampel, K.A.1    Riley, M.2
  • 41
    • 0024412752 scopus 로고
    • Transcriptional repression of eukaryotic promoters
    • Levine, M., and J. Manley. 1989. Transcriptional repression of eukaryotic promoters. Cell 59:405-408.
    • (1989) Cell , vol.59 , pp. 405-408
    • Levine, M.1    Manley, J.2
  • 42
    • 0014216173 scopus 로고
    • Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group
    • Levy, C. C. 1967. Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group. J. Biol. Chem. 242:747-753.
    • (1967) J. Biol. Chem. , vol.242 , pp. 747-753
    • Levy, C.C.1
  • 44
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger, M. D., and M. H. Saier, Jr. 1993. A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. Trends Biochem. Sci. 18:13-20.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 13-20
    • Marger, M.D.1    Saier Jr., M.H.2
  • 45
  • 46
    • 0013596021 scopus 로고
    • The guanine and cytosine content of genomic DNA and bacterial evolution
    • Muto, A., and S. Osawa. 1987. The guanine and cytosine content of genomic DNA and bacterial evolution. Proc. Natl. Acad. Sci. USA 84:166-169.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 166-169
    • Muto, A.1    Osawa, S.2
  • 48
    • 0027082961 scopus 로고
    • Genes in PHT plasmid encoding the initial degradation pathway of phthalate in Pseudomonas putida
    • Nomura, Y., M. Nakagawa, N. Ogawa, S. Harashima, and Y. Oshima. 1992. Genes in PHT plasmid encoding the initial degradation pathway of phthalate in Pseudomonas putida. J. Ferment. Bioeng. 74:333-344.
    • (1992) J. Ferment. Bioeng. , vol.74 , pp. 333-344
    • Nomura, Y.1    Nakagawa, M.2    Ogawa, N.3    Harashima, S.4    Oshima, Y.5
  • 49
    • 0025815712 scopus 로고
    • Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: Expression in Escherichia coli and Pseudomonas putida
    • Nurk, A., L. Kasak, and M. Kivisaar. 1991. Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: expression in Escherichia coli and Pseudomonas putida. Gene 102:13-18.
    • (1991) Gene , vol.102 , pp. 13-18
    • Nurk, A.1    Kasak, L.2    Kivisaar, M.3
  • 50
    • 0027476196 scopus 로고
    • Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli
    • Orser, C. S., C. C. Lange, L. Xun, T. C. Zahrt, and B. J. Schneider. 1993. Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli. J. Bacteriol. 175:411-416.
    • (1993) J. Bacteriol. , vol.175 , pp. 411-416
    • Orser, C.S.1    Lange, C.C.2    Xun, L.3    Zahrt, T.C.4    Schneider, B.J.5
  • 51
    • 0029886743 scopus 로고    scopus 로고
    • The binding site of the IclR repressor protein overlaps the promoter of aceBAK
    • Pan, B., I. Unnikrishnan, and D. C. LaPorte. 1996. The binding site of the IclR repressor protein overlaps the promoter of aceBAK. J. Bacteriol. 178:3982-3984.
    • (1996) J. Bacteriol. , vol.178 , pp. 3982-3984
    • Pan, B.1    Unnikrishnan, I.2    Laporte, D.C.3
  • 52
    • 0025357079 scopus 로고
    • Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4
    • Perkins, E. J., M. P. Gordon, O. Caceres, and P. F. Lurquin. 1990. Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4. J. Bacteriol. 172:2351-2359.
    • (1990) J. Bacteriol. , vol.172 , pp. 2351-2359
    • Perkins, E.J.1    Gordon, M.P.2    Caceres, O.3    Lurquin, P.F.4
  • 53
    • 0027240357 scopus 로고
    • XbaI and BlnI genomic cleavage maps of Escherichia coli K-12 strain MG1655 and comparative analysis of other strains
    • Perkins, J. D., J. D. Heath, B. R. Sharma, and G. M. Weinstock. 1993. XbaI and BlnI genomic cleavage maps of Escherichia coli K-12 strain MG1655 and comparative analysis of other strains. J. Mol. Biol. 232:419-445.
    • (1993) J. Mol. Biol. , vol.232 , pp. 419-445
    • Perkins, J.D.1    Heath, J.D.2    Sharma, B.R.3    Weinstock, G.M.4
  • 54
    • 0028970727 scopus 로고
    • The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences
    • Platt, A., V. Shingler, S. C. Taylor, and P. A. Williams. 1995. The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences. Microbiology 141:2223-2233.
    • (1995) Microbiology , vol.141 , pp. 2223-2233
    • Platt, A.1    Shingler, V.2    Taylor, S.C.3    Williams, P.A.4
  • 55
    • 0027466130 scopus 로고
    • Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600
    • Powlowski, J., L. Sahlman, and V. Shingler. 1993. Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600. J. Bacteriol. 175:377-385.
    • (1993) J. Bacteriol. , vol.175 , pp. 377-385
    • Powlowski, J.1    Sahlman, L.2    Shingler, V.3
  • 57
    • 0030029182 scopus 로고    scopus 로고
    • Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: Engineering a mobile aromatic degradative cluster
    • Prieto, M. A., E. Díaz, and J. L. García. 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    Díaz, E.2    García, J.L.3
  • 58
    • 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 R. A. Cooper. 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
  • 59
    • 0028958247 scopus 로고
    • Sequence of the hpcC and hpcG genes of the mito-fission homoprotocatechuic acid pathway of Escherichia coli C: Nearly 40% amino-acid identity with the analogous enzymes of the catechol pathway
    • Roper, D. I., J. M. Stringfellow, and R. A. Cooper. 1995. Sequence of the hpcC and hpcG genes of the mito-fission homoprotocatechuic acid pathway of Escherichia coli C: nearly 40% amino-acid identity with the analogous enzymes of the catechol pathway. Gene 156:47-51.
    • (1995) Gene , vol.156 , pp. 47-51
    • Roper, D.I.1    Stringfellow, J.M.2    Cooper, R.A.3
  • 62
    • 0017341656 scopus 로고
    • Microbial ecology of the gastrointestinal tract
    • Savage, D. C. 1977. Microbial ecology of the gastrointestinal tract. Annu. Rev. Microbiol. 31:107-133.
    • (1977) Annu. Rev. Microbiol. , vol.31 , pp. 107-133
    • Savage, D.C.1
  • 63
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 64
    • 0026567783 scopus 로고
    • Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600
    • Shingler, V., J. Powlowski, and U. Marklund. 1992. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174:711-724.
    • (1992) J. Bacteriol. , vol.174 , pp. 711-724
    • Shingler, V.1    Powlowski, J.2    Marklund, U.3
  • 65
    • 0029911753 scopus 로고    scopus 로고
    • Enantioselective metabolism of chiral 3-phenylbutyric acid, an intermediate of linear alkylbenzene degradation, by Rhodococcus rhodochrous PB1
    • Simoni, S., S. Klinke, C. Zipper, W. Angst, and H.-P. E. Kohler. 1996. Enantioselective metabolism of chiral 3-phenylbutyric acid, an intermediate of linear alkylbenzene degradation, by Rhodococcus rhodochrous PB1. Appl. Environ. Microbiol. 62:749-755.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 749-755
    • Simoni, S.1    Klinke, S.2    Zipper, C.3    Angst, W.4    Kohler, H.-P.E.5
  • 66
    • 0020411362 scopus 로고
    • An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase
    • Skinner, M. A., and R. A. Cooper. 1982. An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase. Arch. Microbiol. 132:270-275.
    • (1982) Arch. Microbiol. , vol.132 , pp. 270-275
    • Skinner, M.A.1    Cooper, R.A.2
  • 67
    • 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., M. Kawamukai, J. Sanvoisin, H. Braven, and T. D. H. Bugg. 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
  • 68
    • 0015935415 scopus 로고
    • The purification and properties of the flavoprotein melilotate hydroxylase
    • Strickland, S., and V. Massey. 1973. The purification and properties of the flavoprotein melilotate hydroxylase. J. Biol. Chem. 248:2944-2952.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2944-2952
    • Strickland, S.1    Massey, V.2
  • 69
    • 0028803761 scopus 로고
    • Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH)
    • Stringfellow, J. M., B. Turpin, and R. A. Cooper. 1995. Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH). Gene 166:73-76.
    • (1995) Gene , vol.166 , pp. 73-76
    • Stringfellow, J.M.1    Turpin, B.2    Cooper, R.A.3
  • 70
    • 0025355399 scopus 로고
    • Regulation of the glyoxylate bypass operon: Cloning and characterization of iclR
    • Sunnarborg, A., D. Klumpp, T. Chung, and D. C. LaPorte. 1990. Regulation of the glyoxylate bypass operon: cloning and characterization of iclR. J. Bacteriol. 172:2642-2649.
    • (1990) J. Bacteriol. , vol.172 , pp. 2642-2649
    • Sunnarborg, A.1    Klumpp, D.2    Chung, T.3    Laporte, D.C.4
  • 71
    • 0029773416 scopus 로고    scopus 로고
    • Three, four or more: The translational stop signal at length
    • Tate, W. P., and S. A. Mannering. 1996. Three, four or more: the translational stop signal at length. Mol. Microbiol. 21:213-219.
    • (1996) Mol. Microbiol. , vol.21 , pp. 213-219
    • Tate, W.P.1    Mannering, S.A.2
  • 72
    • 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, J. D., D. G. Higgins, and T. J. Gibson. 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.G.2    Gibson, T.J.3
  • 74
    • 0028924094 scopus 로고
    • Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1
    • Wang, Y., M. Rawlings, D. T. Gibson, D. Labbé, H. Bergeron, R. Brousseau, and P. C. K. Lau. 1995. Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1. Mol. Gen. Genet. 246:570-579.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 570-579
    • Wang, Y.1    Rawlings, M.2    Gibson, D.T.3    Labbé, D.4    Bergeron, H.5    Brousseau, R.6    Lau, P.C.K.7
  • 76
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Tepstra, and W. G. J. Hol. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Tepstra, P.2    Hol, W.G.J.3
  • 77
    • 0020714456 scopus 로고
    • Rapid similarity searches of nucleic acid and protein data banks
    • Wilbur, W. J., and D. J. Lipman. 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
  • 78
    • 0028672045 scopus 로고
    • The evolution of pathways for aromatic hydrocarbon oxidation in Pseudomonas
    • Williams, P. A., and J. R. Sayers. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.