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Volumn 28, Issue 4, 2004, Pages 503-518

Aromatic metabolism versus carbon availability: The regulatory network that controls catabolism of less-preferred carbon sources in Escherichia coli

Author keywords

Aromatic compounds; Catabolic pathways; Catabolism; Catabolite repression; CRP; Escherichia coli; Less preferred carbon sources; Transcriptional regulation

Indexed keywords

AROMATIC COMPOUND; BACTERIAL DNA; BETA LACTAM ANTIBIOTIC; CARBON; PENICILLIN G;

EID: 4444366933     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsre.2004.04.004     Document Type: Review
Times cited : (21)

References (68)
  • 1
    • 0032464663 scopus 로고    scopus 로고
    • What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli
    • Peekhaus N., Conway T. What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli. J. Bacteriol. 180:1998;3495-3502
    • (1998) J. Bacteriol. , vol.180 , pp. 3495-3502
    • Peekhaus, N.1    Conway, T.2
  • 2
    • 0017341656 scopus 로고
    • Microbial ecology of the gastrointestinal tract
    • Savage D.C. Microbial ecology of the gastrointestinal tract. Ann. Rev. Microbiol. 31:1977;107-133
    • (1977) Ann. Rev. Microbiol. , vol.31 , pp. 107-133
    • Savage, D.C.1
  • 3
    • 0002437481 scopus 로고    scopus 로고
    • The enteric bacterial cell and the age of bacteria
    • F.C. Neidhardt, R. III Curtiss, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, & H.E. Umbarger. Washington, D.C.: ASM Press
    • Neidhardt F.C. The enteric bacterial cell and the age of bacteria. Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella: Cellular and Molecular Biology. 2nd ed.:1996;1-3 ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology 2nd Ed. , pp. 1-3
    • Neidhardt, F.C.1
  • 4
    • 0033042276 scopus 로고    scopus 로고
    • Survival of Escherichia coli 0157 in a soil protozoan: Implications for disease
    • Barker J., Humphrey T.J., Brown M.W.R. Survival of Escherichia coli 0157 in a soil protozoan: implications for disease. FEMS Microbiol. Lett. 173:1999;291-295
    • (1999) FEMS Microbiol. Lett. , vol.173 , pp. 291-295
    • Barker, J.1    Humphrey, T.J.2    Brown, M.W.R.3
  • 6
    • 0035813115 scopus 로고    scopus 로고
    • Superimposed levels of regulation of the 4-hydroxyphenylacetate catabolic pathway in Escherichia coli.
    • Galán B., Kolb A., García J.L., Prieto M.A. Superimposed levels of regulation of the 4-hydroxyphenylacetate catabolic pathway in Escherichia coli. J. Biol. Chem. 276:2001;37060-37068
    • (2001) J. Biol. Chem. , vol.276 , pp. 37060-37068
    • Galán, B.1    Kolb, A.2    García, J.L.3    Prieto, M.A.4
  • 7
    • 0035863067 scopus 로고    scopus 로고
    • The black cat/white cat principle of signal integration in bacterial promoters
    • Cases I., de Lorenzo V. The black cat/white cat principle of signal integration in bacterial promoters. EMBO J. 20:2001;1-11
    • (2001) EMBO J. , vol.20 , pp. 1-11
    • Cases, I.1    De Lorenzo, V.2
  • 8
    • 0033772905 scopus 로고    scopus 로고
    • Bacterial promoters triggering biodegradation of environmental pollutants
    • Díaz E., Prieto M.A. Bacterial promoters triggering biodegradation of environmental pollutants. Curr. Opin. Biotechnol. 11:2000;467-475
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 467-475
    • Díaz, E.1    Prieto, M.A.2
  • 10
    • 0020625023 scopus 로고
    • Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli
    • Burlingame R., Chapman P.J. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155:1983;113-121
    • (1983) J. Bacteriol. , vol.155 , pp. 113-121
    • Burlingame, R.1    Chapman, P.J.2
  • 11
    • 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., Díaz E., García J.L. Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: engineering a mobile aromatic degradative cluster. J. Bacteriol. 178:1996;111-120
    • (1996) J. Bacteriol. , vol.178 , pp. 111-120
    • Prieto, M.A.1    Díaz, E.2    García, J.L.3
  • 12
    • 0030948489 scopus 로고    scopus 로고
    • Genetic characterization and expression in heterologous hosts of the 3 (3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12
    • Ferrández A., García J.L., Díaz E. Genetic characterization and expression in heterologous hosts of the 3 (3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12. J. Bacteriol. 179:1997;2573-2581
    • (1997) J. Bacteriol. , vol.179 , pp. 2573-2581
    • Ferrández, A.1    García, J.L.2    Díaz, E.3
  • 13
    • 0032463020 scopus 로고    scopus 로고
    • Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12
    • Díaz E., Ferrández A., García J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180:1998;2915-2923
    • (1998) J. Bacteriol. , vol.180 , pp. 2915-2923
    • Díaz, E.1    Ferrández, A.2    García, J.L.3
  • 16
    • 0029913774 scopus 로고    scopus 로고
    • MaoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli
    • Yamashita M., Azakami H., Yokoro N., Roh J.H., Suzuki H., Kumagai H., Murooka Y. maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli. J. Bacteriol. 178:1996;2941-2947
    • (1996) J. Bacteriol. , vol.178 , pp. 2941-2947
    • Yamashita, M.1    Azakami, H.2    Yokoro, N.3    Roh, J.H.4    Suzuki, H.5    Kumagai, H.6    Murooka, Y.7
  • 17
    • 0039224934 scopus 로고    scopus 로고
    • Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli
    • Ferrández A., Prieto M.A., García J.L., Díaz E. Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli. FEBS Lett. 406:1997;23-27
    • (1997) FEBS Lett. , vol.406 , pp. 23-27
    • Ferrández, A.1    Prieto, M.A.2    García, J.L.3    Díaz, E.4
  • 18
    • 0031587777 scopus 로고    scopus 로고
    • Identification of a novel positive regulator of the 4- hydroxyphenylacetate catabolic pathway of Escherichia coli
    • Prieto M.A., García J.L. Identification of a novel positive regulator of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli. Biochem. Biophys. Res. Commun. 232:1997;759-765
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 759-765
    • Prieto, M.A.1    García, J.L.2
  • 19
    • 0028093362 scopus 로고
    • Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli
    • Prieto M.A., García J.L. Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. J. Biol. Chem. 269:1994;22823-22829
    • (1994) J. Biol. Chem. , vol.269 , pp. 22823-22829
    • Prieto, M.A.1    García, J.L.2
  • 21
    • 0034617418 scopus 로고    scopus 로고
    • Mutational analysis of the highly conserved C-terminal residues of the XylS protein, a member of the AraC family of transcriptional regulators
    • Manzanera M., Marqués S., Ramos J.L. Mutational analysis of the highly conserved C-terminal residues of the XylS protein, a member of the AraC family of transcriptional regulators. FEBS Lett. 476:2000;312-317
    • (2000) FEBS Lett. , vol.476 , pp. 312-317
    • Manzanera, M.1    Marqués, S.2    Ramos, J.L.3
  • 22
    • 0036083835 scopus 로고    scopus 로고
    • AraC-XylS database: A family of positive transcriptional regulators in bacteria
    • Tobes R., Ramos J.L. AraC-XylS database: a family of positive transcriptional regulators in bacteria. Nucl. Acids Res. 30:2002;318-321
    • (2002) Nucl. Acids Res. , vol.30 , pp. 318-321
    • Tobes, R.1    Ramos, J.L.2
  • 23
    • 0033967976 scopus 로고    scopus 로고
    • Functional domains of the TOL plasmid transcription factor XylS
    • Kaldalu N., Toots U., de Lorenzo V., Ustav M. Functional domains of the TOL plasmid transcription factor XylS. J. Bacteriol. 182:2000;1118-1126
    • (2000) J. Bacteriol. , vol.182 , pp. 1118-1126
    • Kaldalu, N.1    Toots, U.2    De Lorenzo, V.3    Ustav, M.4
  • 24
    • 0035057115 scopus 로고    scopus 로고
    • The phenylacetyl-CoA catabolon: A complex catabolic unit with broad biotechnological applications
    • Luengo J.M., García J.L., Olivera E.R. The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications. Mol. Microbiol. 39:2001;1434-1442
    • (2001) Mol. Microbiol. , vol.39 , pp. 1434-1442
    • Luengo, J.M.1    García, J.L.2    Olivera, E.R.3
  • 25
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell M.A. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:1993;597-626
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 26
    • 0042346417 scopus 로고    scopus 로고
    • Regulation of the mhp cluster responsible for 3-(3-hydroxyphenyl) propionic acid degradation in Escherichia coli.
    • Torres B., Porras G., García J.L., Díaz E. Regulation of the mhp cluster responsible for 3-(3-hydroxyphenyl)propionic acid degradation in Escherichia coli. J. Biol. Chem. 278:2003;27575-27585
    • (2003) J. Biol. Chem. , vol.278 , pp. 27575-27585
    • Torres, B.1    Porras, G.2    García, J.L.3    Díaz, E.4
  • 27
    • 0028365190 scopus 로고
    • Regulation of p-hydroxybenzoate hydroxylase synthesis by PobR bound to an operator in Acinetobacter calcoaceticus
    • DiMarco A.A., Ornston L.N. Regulation of p-hydroxybenzoate hydroxylase synthesis by PobR bound to an operator in Acinetobacter calcoaceticus. J. Bacteriol. 176:1994;4277-4284
    • (1994) J. Bacteriol. , vol.176 , pp. 4277-4284
    • Dimarco, A.A.1    Ornston, L.N.2
  • 28
    • 0032923396 scopus 로고    scopus 로고
    • PcaR-mediated activation and repression of pca genes from Pseudomonas putida are propagated by its binding to both the -35 and the -10 promoter elements
    • Guo Z., Houghton J.E. PcaR-mediated activation and repression of pca genes from Pseudomonas putida are propagated by its binding to both the -35 and the -10 promoter elements. Mol. Microbiol. 32:1999;253-263
    • (1999) Mol. Microbiol. , vol.32 , pp. 253-263
    • Guo, Z.1    Houghton, J.E.2
  • 29
    • 0035153271 scopus 로고    scopus 로고
    • Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Trautwein G., Gerischer U. Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 183:2001;873-881
    • (2001) J. Bacteriol. , vol.183 , pp. 873-881
    • Trautwein, G.1    Gerischer, U.2
  • 30
    • 0036203062 scopus 로고    scopus 로고
    • Differential DNA binding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Popp R., Kohl T., Patz P., Trautwein G., Gerischer U. Differential DNA binding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 184:2002;1988-1997
    • (2002) J. Bacteriol. , vol.184 , pp. 1988-1997
    • Popp, R.1    Kohl, T.2    Patz, P.3    Trautwein, G.4    Gerischer, U.5
  • 31
    • 0037126615 scopus 로고    scopus 로고
    • A simple mechanism for co-dependence on two activators at an Escherichia coli promoter
    • Wade J.T., Belyaeva T.A., Hyde E.I., Busby S.J.W. A simple mechanism for co-dependence on two activators at an Escherichia coli promoter. EMBO J. 20:2001;7160-7167
    • (2001) EMBO J. , vol.20 , pp. 7160-7167
    • Wade, J.T.1    Belyaeva, T.A.2    Hyde, E.I.3    Busby, S.J.W.4
  • 32
    • 0345531110 scopus 로고    scopus 로고
    • Molecular determinants of the hpa regulatory system of Escherichia coli: The HpaR repressor
    • Galán B., Kolb A., Sanz J., García J.L., Prieto M.A. Molecular determinants of the hpa regulatory system of Escherichia coli: the HpaR repressor. Nucl. Acids Res. 31:2003;6598-6609
    • (2003) Nucl. Acids Res. , vol.31 , pp. 6598-6609
    • Galán, B.1    Kolb, A.2    Sanz, J.3    García, J.L.4    Prieto, M.A.5
  • 33
    • 0029079304 scopus 로고
    • Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences
    • Martin R.G., Rosner J.L. Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences. Proc. Natl. Acad. Sci. USA. 92:1995;5456-5460
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5456-5460
    • Martin, R.G.1    Rosner, J.L.2
  • 34
    • 0034887133 scopus 로고    scopus 로고
    • The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3A resolution
    • Alekshun M.N., Levy S.B., Mealy T.R., Seaton B.A., Head J.F. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3A resolution. Nature Struct. Biol. 8:2001;710-714
    • (2001) Nature Struct. Biol. , vol.8 , pp. 710-714
    • Alekshun, M.N.1    Levy, S.B.2    Mealy, T.R.3    Seaton, B.A.4    Head, J.F.5
  • 35
    • 0037047395 scopus 로고    scopus 로고
    • Crystal structure of the MexR repressor of the mexRAB-oprM multidrug efflux operon of Pseudomonas aeruginosa
    • Lim D., Poole K., Strynadka N.C. Crystal structure of the MexR repressor of the mexRAB-oprM multidrug efflux operon of Pseudomonas aeruginosa. J. Biol. Chem. 277:2002;29253-29259
    • (2002) J. Biol. Chem. , vol.277 , pp. 29253-29259
    • Lim, D.1    Poole, K.2    Strynadka, N.C.3
  • 37
    • 0034107895 scopus 로고    scopus 로고
    • Mutational analysis of MarR, the negative regulator of marRAB expression in Escherichia coli, suggests the presence of two regions required for DNA binding
    • Alekshun M.N., Kim Y.S., Levy S.B. Mutational analysis of MarR, the negative regulator of marRAB expression in Escherichia coli, suggests the presence of two regions required for DNA binding. Mol. Microbiol. 35:2000;1394-1404
    • (2000) Mol. Microbiol. , vol.35 , pp. 1394-1404
    • Alekshun, M.N.1    Kim, Y.S.2    Levy, S.B.3
  • 38
    • 0039771974 scopus 로고    scopus 로고
    • Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli
    • Ferrández A., García J.L., Díaz E. Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli. J. Biol. Chem. 275:2000;12214-12222
    • (2000) J. Biol. Chem. , vol.275 , pp. 12214-12222
    • Ferrández, A.1    García, J.L.2    Díaz, E.3
  • 39
    • 1642378560 scopus 로고    scopus 로고
    • PaaX repressor, a link between Penicillin G acylase and the Phenylacetyl-CoA catabolon of Escherichia coli W
    • Galán B., García J.L., Prieto M.A. PaaX repressor, a link between Penicillin G acylase and the Phenylacetyl-CoA catabolon of Escherichia coli W. J. Bacteriol. 186:2004;2215-2220
    • (2004) J. Bacteriol. , vol.186 , pp. 2215-2220
    • Galán, B.1    García, J.L.2    Prieto, M.A.3
  • 42
    • 0014642629 scopus 로고
    • Hydrolysis of penicillins and related compounds by the cell-bound penicillin acylase of Escherichia coli
    • Cole B.M. Hydrolysis of penicillins and related compounds by the cell-bound penicillin acylase of Escherichia coli. Biochem. J. 115:1969;733-739
    • (1969) Biochem. J. , vol.115 , pp. 733-739
    • Cole, B.M.1
  • 43
    • 0014632276 scopus 로고
    • Penicillins and other acylamino compounds synthesized by the cell-bound penicillin acylase of Escherichia coli
    • Cole B.M. Penicillins and other acylamino compounds synthesized by the cell-bound penicillin acylase of Escherichia coli. Biochem. J. 115:1969;747-764
    • (1969) Biochem. J. , vol.115 , pp. 747-764
    • Cole, B.M.1
  • 44
    • 0038236925 scopus 로고    scopus 로고
    • Industrial production of β-lactam antibiotics
    • Elander R.P. Industrial production of β-lactam antibiotics. Appl. Microbiol. Biotechnol. 61:2003;385-392
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 385-392
    • Elander, R.P.1
  • 46
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby S., Ebright H. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 293:1999;199-213
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, H.2
  • 47
    • 0014076155 scopus 로고
    • Glucose-lactose diauxie in Escherichia coli
    • Loomis W.F., Magasanik B. Glucose-lactose diauxie in Escherichia coli. J. Bacteriol. 93:1967;1397-1401
    • (1967) J. Bacteriol. , vol.93 , pp. 1397-1401
    • Loomis, W.F.1    Magasanik, B.2
  • 48
    • 0030698856 scopus 로고    scopus 로고
    • CAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli
    • Kimata K., Takahashi H., Inada T., Postma P., Aiba H. cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli. Proc. Natl. Acad. Sci. USA. 94:1997;12914-12919
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12914-12919
    • Kimata, K.1    Takahashi, H.2    Inada, T.3    Postma, P.4    Aiba, H.5
  • 49
    • 0028298782 scopus 로고
    • Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: Role of autoregulation of the crp gene
    • Ishizuka H., Hanamura A., Inada T., Aiba H. Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: role of autoregulation of the crp gene. EMBO J. 13:1994;3077-3082
    • (1994) EMBO J. , vol.13 , pp. 3077-3082
    • Ishizuka, H.1    Hanamura, A.2    Inada, T.3    Aiba, H.4
  • 50
    • 0031559956 scopus 로고    scopus 로고
    • Identification of the 4-hydroxyphenylacetate transport gene of Escherichia coli W: Construction of a highly sensitive cellular biosensor
    • Prieto M.A., García J.L. Identification of the 4-hydroxyphenylacetate transport gene of Escherichia coli W: construction of a highly sensitive cellular biosensor. FEBS Lett. 414:1997;293-297
    • (1997) FEBS Lett. , vol.414 , pp. 293-297
    • Prieto, M.A.1    García, J.L.2
  • 51
    • 0030436351 scopus 로고    scopus 로고
    • Cultivation of Escherichia coli with mixtures of 3-phenylpropionic acid and glucose: Dynamics of growth and substrate consumption
    • Kovárová K., Käch A., Chaloupka V., Egli T. Cultivation of Escherichia coli with mixtures of 3-phenylpropionic acid and glucose: dynamics of growth and substrate consumption. Biodegradation. 7:1996;445-453
    • (1996) Biodegradation , vol.7 , pp. 445-453
    • Kovárová, K.1    Käch, A.2    Chaloupka, V.3    Egli, T.4
  • 52
    • 0031719199 scopus 로고    scopus 로고
    • Growth kinetics of suspended microbial cells: From single-substrate- controlled growth to mixed-substrate kinetics
    • Kovárová-Kovar K., Egli T. Growth kinetics of suspended microbial cells: from single-substrate-controlled growth to mixed-substrate kinetics. Microbiol. Mol. Biol. Rev. 62:1998;646-666
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 646-666
    • Kovárová-Kovar, K.1    Egli, T.2
  • 53
    • 0042535907 scopus 로고    scopus 로고
    • Cultivation of Escherichia coli with mixtures of 3-phenylpropionic acid and glucose: Steady-state growth kinetics
    • Kovárová K., Käch A., Zehnder A.J.B., Egli T. Cultivation of Escherichia coli with mixtures of 3-phenylpropionic acid and glucose: steady-state growth kinetics. Appl. Environ. Microbiol. 63:1997;2619-2624
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2619-2624
    • Kovárová, K.1    Käch, A.2    Zehnder, A.J.B.3    Egli, T.4
  • 54
    • 0029009026 scopus 로고
    • Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme a synthetase in Escherichia coli.
    • Kumari S., Tishel R., Eisenbach M., Wolfe A.J. Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli. J. Bacteriol. 177:1995;2878-2886
    • (1995) J. Bacteriol. , vol.177 , pp. 2878-2886
    • Kumari, S.1    Tishel, R.2    Eisenbach, M.3    Wolfe, A.J.4
  • 56
    • 0033082849 scopus 로고    scopus 로고
    • Interactions between the Escherichia coli cAMP receptor protein and the C-terminal domain of the alpha subunit of RNA polymerase at class I promoters
    • Law E.C., Savery N.J., Busby S.J. Interactions between the Escherichia coli cAMP receptor protein and the C-terminal domain of the alpha subunit of RNA polymerase at class I promoters. Biochem. J. 337:1999;415-423
    • (1999) Biochem. J. , vol.337 , pp. 415-423
    • Law, E.C.1    Savery, N.J.2    Busby, S.J.3
  • 57
    • 0032589264 scopus 로고    scopus 로고
    • The IIANtr (PtsN) protein of Pseudomonas putida mediates the C source inhibition of the sigma 54-dependent Pu promoter of the TOL plasmid
    • Cases I., Pérez-Martín J., de Lorenzo V. The IIANtr (PtsN) protein of Pseudomonas putida mediates the C source inhibition of the sigma 54-dependent Pu promoter of the TOL plasmid. J. Biol. Chem. 274:1999;15562-15568
    • (1999) J. Biol. Chem. , vol.274 , pp. 15562-15568
    • Cases, I.1    Pérez-Martín, J.2    De Lorenzo, V.3
  • 58
    • 0036306439 scopus 로고    scopus 로고
    • Inactivation of cytochrome o ubiquinol oxidase relieves catabolic repression of the Pseudomonas putida GPo1 alkane degradation pathway
    • Dinamarca M.A., Ruiz-Manzano A., Rojo F. Inactivation of cytochrome o ubiquinol oxidase relieves catabolic repression of the Pseudomonas putida GPo1 alkane degradation pathway. J. Bacteriol. 184:2002;3785-3793
    • (2002) J. Bacteriol. , vol.184 , pp. 3785-3793
    • Dinamarca, M.A.1    Ruiz-Manzano, A.2    Rojo, F.3
  • 59
    • 0034784867 scopus 로고    scopus 로고
    • The cyo operon of Pseudomonas putida is involved in carbon catabolite repression of phenol degradation
    • Petruschka L., Burchhardt G., Muller C., Weihe C., Herrmann H. The cyo operon of Pseudomonas putida is involved in carbon catabolite repression of phenol degradation. Mol. Genet. Genomics. 266:2001;199-206
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 199-206
    • Petruschka, L.1    Burchhardt, G.2    Muller, C.3    Weihe, C.4    Herrmann, H.5
  • 60
    • 0033039322 scopus 로고    scopus 로고
    • The alarmone (p)ppGpp mediates physiological-responsive control at the sigma 54-dependent Po promoter
    • Sze C.C., Shingler V. The alarmone (p)ppGpp mediates physiological- responsive control at the sigma 54-dependent Po promoter. Mol. Microbiol. 31:1999;1217-1228
    • (1999) Mol. Microbiol. , vol.31 , pp. 1217-1228
    • Sze, C.C.1    Shingler, V.2
  • 61
    • 0001493114 scopus 로고    scopus 로고
    • 54- dependent Po promoter controlling the Pseudomonas derived (methyl) phenol dmp operon of pVI150
    • 54-dependent Po promoter controlling the Pseudomonas derived (methyl) phenol dmp operon of pVI150 J. Bacteriol. 178:1996;3727-3735
    • (1996) J. Bacteriol. , vol.178 , pp. 3727-3735
    • Sze, C.C.1    Moore, T.2    Shingler, V.3
  • 62
    • 0032544080 scopus 로고    scopus 로고
    • Identification of an UP element consensus sequence for bacterial promoters
    • Estrem S.T., Gaal T., Ross W., Gourse R.L. Identification of an UP element consensus sequence for bacterial promoters. Proc. Natl. Acad. Sci. USA. 95:1998;9761-9766
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9761-9766
    • Estrem, S.T.1    Gaal, T.2    Ross, W.3    Gourse, R.L.4
  • 63
    • 0032797410 scopus 로고    scopus 로고
    • New insights into the regulation of pac gene from Escherichia coli W ATCC 11105
    • Roa A., García J.L. New insights into the regulation of pac gene from Escherichia coli W ATCC 11105. FEMS Microbiol. Lett. 177:1999;7-14
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 7-14
    • Roa, A.1    García, J.L.2
  • 64
    • 0026705620 scopus 로고
    • Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene
    • Merino E., Balbas P., Recillas F., Becerril B., Valle F., Bolivar F. Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene. Mol. Microbiol. 6:1992;2175-2182
    • (1992) Mol. Microbiol. , vol.6 , pp. 2175-2182
    • Merino, E.1    Balbas, P.2    Recillas, F.3    Becerril, B.4    Valle, F.5    Bolivar, F.6
  • 65
    • 0017259809 scopus 로고
    • Regulation of penicillin acylase in Escherichia coli by cyclic AMP
    • Gang D.M., Shaikh K. Regulation of penicillin acylase in Escherichia coli by cyclic AMP. Biochim. Biophys. Acta. 425:1976;110-114
    • (1976) Biochim. Biophys. Acta , vol.425 , pp. 110-114
    • Gang, D.M.1    Shaikh, K.2
  • 66
    • 0035128568 scopus 로고    scopus 로고
    • DNA architecture and transcriptional regulation of the Escherichia coli penicillin amidase (pac) gene
    • Stojcevic N., Moric I., Begovic J., Radoja S., Konstantinovic M. DNA architecture and transcriptional regulation of the Escherichia coli penicillin amidase (pac) gene. Biomol. Eng. 17:2001;113-117
    • (2001) Biomol. Eng. , vol.17 , pp. 113-117
    • Stojcevic, N.1    Moric, I.2    Begovic, J.3    Radoja, S.4    Konstantinovic, M.5
  • 67
    • 0027672619 scopus 로고
    • Molecular basis of the exclusive low temperature synthesis of an enzyme in E. coli: Penicillin acylase
    • Keilmann C., Wanner G., Bock A. Molecular basis of the exclusive low temperature synthesis of an enzyme in E. coli: Penicillin acylase. Biol. Chem. Hoppe-Seyler. 374:1993;983-992
    • (1993) Biol. Chem. Hoppe-Seyler. , vol.374 , pp. 983-992
    • Keilmann, C.1    Wanner, G.2    Bock, A.3
  • 68
    • 0034730417 scopus 로고    scopus 로고
    • Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft
    • Hewitt L., Kasche V., Lummer K., Lewis R.J., Murshudov G.N., Verma C.S., Dodson G.G., Wilson K.S. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft. J. Mol. Biol. 302:2000;887-898
    • (2000) J. Mol. Biol. , vol.302 , pp. 887-898
    • Hewitt, L.1    Kasche, V.2    Lummer, K.3    Lewis, R.J.4    Murshudov, G.N.5    Verma, C.S.6    Dodson, G.G.7    Wilson, K.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.