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Volumn 18, Issue 10, 2016, Pages 3565-3582

Pyridine nucleotide transhydrogenases enable redox balance of Pseudomonas putida during biodegradation of aromatic compounds

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC HYDROCARBON; BACTERIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 84991447132     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.13434     Document Type: Article
Times cited : (50)

References (88)
  • 1
    • 84991491115 scopus 로고    scopus 로고
    • The RNA chaperone Hfq enables the environmental stress tolerance super-phenotype of Pseudomonas putida
    • in press
    • Arce-Rodríguez, A., Calles, B., Nikel, P.I., and de Lorenzo, V. (2015) The RNA chaperone Hfq enables the environmental stress tolerance super-phenotype of Pseudomonas putida. Environ Microbiol in press, doi: 10.1111/1462-2920.13052.
    • (2015) Environ Microbiol
    • Arce-Rodríguez, A.1    Calles, B.2    Nikel, P.I.3    de Lorenzo, V.4
  • 2
    • 0033405777 scopus 로고    scopus 로고
    • The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence
    • Auzat, I., Chapuy-Regaud, S., Le Bras, G., Dos Santos, D., Ogunniyi, A.D., Le Thomas, I., et al. (1999) The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence. Mol Microbiol 34: 1018–1028.
    • (1999) Mol Microbiol , vol.34 , pp. 1018-1028
    • Auzat, I.1    Chapuy-Regaud, S.2    Le Bras, G.3    Dos Santos, D.4    Ogunniyi, A.D.5    Le Thomas, I.6
  • 3
    • 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., Frey, J., 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    Frey, J.6    Timmis, K.N.7
  • 4
    • 84964771581 scopus 로고    scopus 로고
    • The revisited genome of Pseudomonas putida KT2440 enlightens its value as a robust metabolic chassis
    • in press
    • Belda, E., van Heck, R.G.A., López-Sánchez, M.J., Cruveiller, S., Barbe, V., Fraser, C., et al. (2016) The revisited genome of Pseudomonas putida KT2440 enlightens its value as a robust metabolic chassis. Environ Microbiol in press, doi: 10.1111/1462-2920.13230.
    • (2016) Environ Microbiol
    • Belda, E.1    van Heck, R.G.A.2    López-Sánchez, M.J.3    Cruveiller, S.4    Barbe, V.5    Fraser, C.6
  • 5
    • 84956522448 scopus 로고    scopus 로고
    • Data on the standardization of a cyclohexanone-responsive expression system for Gram-negative bacteria
    • Benedetti, I., Nikel, P.I., and de Lorenzo, V. (2016) Data on the standardization of a cyclohexanone-responsive expression system for Gram-negative bacteria. Data Brief 6: 738–744.
    • (2016) Data Brief , vol.6 , pp. 738-744
    • Benedetti, I.1    Nikel, P.I.2    de Lorenzo, V.3
  • 6
    • 52449130902 scopus 로고    scopus 로고
    • Metabolic response of Pseudomonas putida during redox biocatalysis in the presence of a second octanol phase
    • Blank, L.M., Ionidis, G., Ebert, B.E., Bühler, B., and Schmid, A. (2008) Metabolic response of Pseudomonas putida during redox biocatalysis in the presence of a second octanol phase. FEBS J 275: 5173–5190.
    • (2008) FEBS J , vol.275 , pp. 5173-5190
    • Blank, L.M.1    Ionidis, G.2    Ebert, B.E.3    Bühler, B.4    Schmid, A.5
  • 7
    • 77954141406 scopus 로고    scopus 로고
    • Redox biocatalysis and metabolism: molecular mechanisms and metabolic network analysis
    • Blank, L.M., Ebert, B.E., Buehler, K., and Bühler, B. (2010) Redox biocatalysis and metabolism: molecular mechanisms and metabolic network analysis. Antiox Red Signal 13: 349–394.
    • (2010) Antiox Red Signal , vol.13 , pp. 349-394
    • Blank, L.M.1    Ebert, B.E.2    Buehler, K.3    Bühler, B.4
  • 8
    • 57649123534 scopus 로고    scopus 로고
    • Global phenotypic characterization of bacteria
    • Bochner, B.R. (2009) Global phenotypic characterization of bacteria. FEMS Microbiol Rev 33: 191–205.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 191-205
    • Bochner, B.R.1
  • 9
    • 0034911878 scopus 로고    scopus 로고
    • Phenotype microarrays for high-throughput phenotypic testing and assay of gene function
    • Bochner, B.R., Gadzinski, P., and Panomitros, E. (2001) Phenotype microarrays for high-throughput phenotypic testing and assay of gene function. Genome Res 11: 1246–1255.
    • (2001) Genome Res , vol.11 , pp. 1246-1255
    • Bochner, B.R.1    Gadzinski, P.2    Panomitros, E.3
  • 10
    • 0034466694 scopus 로고    scopus 로고
    • Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone
    • Boonstra, B., Rathbone, D.A., French, C.E., Walker, E.H., and Bruce, N.C. (2000) Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone. Appl Environ Microbiol 66: 5161–5166.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5161-5166
    • Boonstra, B.1    Rathbone, D.A.2    French, C.E.3    Walker, E.H.4    Bruce, N.C.5
  • 11
    • 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
  • 12
    • 40549093298 scopus 로고    scopus 로고
    • NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • Bühler, B., Park, J.B., Blank, L.M., and Schmid, A. (2008) NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl Environ Microbiol 74: 1436–1446.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1436-1446
    • Bühler, B.1    Park, J.B.2    Blank, L.M.3    Schmid, A.4
  • 13
    • 84876838057 scopus 로고    scopus 로고
    • Evolution after introduction of a novel metabolic pathway consistently leads to restoration of wild-type physiology
    • Carroll, S.M., and Marx, C.J. (2013) Evolution after introduction of a novel metabolic pathway consistently leads to restoration of wild-type physiology. PLoS Genet 9: e1003427.
    • (2013) PLoS Genet , vol.9
    • Carroll, S.M.1    Marx, C.J.2
  • 14
    • 84878639396 scopus 로고    scopus 로고
    • The Entner-Doudoroff pathway empowers Pseudomonas putida KT2440 with a high tolerance to oxidative stress
    • Chavarría, M., Nikel, P.I., Pérez-Pantoja, D., and de Lorenzo, V. (2013) The Entner-Doudoroff pathway empowers Pseudomonas putida KT2440 with a high tolerance to oxidative stress. Environ Microbiol 15: 1772–1785.
    • (2013) Environ Microbiol , vol.15 , pp. 1772-1785
    • Chavarría, M.1    Nikel, P.I.2    Pérez-Pantoja, D.3    de Lorenzo, V.4
  • 15
    • 84942279620 scopus 로고    scopus 로고
    • High speed BLASTN: an accelerated MegaBLAST search tool
    • Chen, Y., Ye, W., Zhang, Y., and Xu, Y. (2015) High speed BLASTN: an accelerated MegaBLAST search tool. Nucleic Acids Res 43: 7762–7768.
    • (2015) Nucleic Acids Res , vol.43 , pp. 7762-7768
    • Chen, Y.1    Ye, W.2    Zhang, Y.3    Xu, Y.4
  • 16
    • 84924408551 scopus 로고    scopus 로고
    • Transhydrogenase promotes the robustness and evolvability of E. coli deficient in NADPH production
    • Chou, H.H., Marx, C.J., and Sauer, U. (2015) Transhydrogenase promotes the robustness and evolvability of E. coli deficient in NADPH production. PLoS Genet 11: e1005007.
    • (2015) PLoS Genet , vol.11
    • Chou, H.H.1    Marx, C.J.2    Sauer, U.3
  • 17
    • 0021955390 scopus 로고
    • Cloning and expression of the transhydrogenase gene of Escherichia coli
    • Clarke, D.M., and Bragg, P.D. (1985) Cloning and expression of the transhydrogenase gene of Escherichia coli. J Bacteriol 162: 367–373.
    • (1985) J Bacteriol , vol.162 , pp. 367-373
    • Clarke, D.M.1    Bragg, P.D.2
  • 18
    • 0014939683 scopus 로고
    • Purification and properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa
    • Cohen, P.T., and Kaplan, N.O. (1970) Purification and properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa. J Biol Chem 245: 2825–2836.
    • (1970) J Biol Chem , vol.245 , pp. 2825-2836
    • Cohen, P.T.1    Kaplan, N.O.2
  • 19
    • 0008848282 scopus 로고
    • Pyridine nucleotide transhydrogenase. I. Indirect evidence for the reaction and purification of the enzyme
    • Colowick, S.P., Kaplan, N.O., Neufeld, E.F., and Ciotti, M.M. (1952) Pyridine nucleotide transhydrogenase. I. Indirect evidence for the reaction and purification of the enzyme. J Biol Chem 195: 95–105.
    • (1952) J Biol Chem , vol.195 , pp. 95-105
    • Colowick, S.P.1    Kaplan, N.O.2    Neufeld, E.F.3    Ciotti, M.M.4
  • 20
    • 84952638985 scopus 로고    scopus 로고
    • 13C-metabolic flux analysis of the extremely thermophilic, fast growing, xylose-utilizing Geobacillus strain LC300
    • 13C-metabolic flux analysis of the extremely thermophilic, fast growing, xylose-utilizing Geobacillus strain LC300. Metab Eng 33: 148–157.
    • (2016) Metab Eng , vol.33 , pp. 148-157
    • Cordova, L.T.1    Antoniewicz, M.R.2
  • 21
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A. and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640–6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 22
    • 80053384406 scopus 로고    scopus 로고
    • Characterization of a Cr(VI)-sensitive Pseudomonas corrugata 28 mutant impaired in a pyridine nucleotide transhydrogenase gene
    • Decorosi, F., Lori, L., Santopolo, L., Tatti, E., Giovannetti, L., and Viti, C. (2011) Characterization of a Cr(VI)-sensitive Pseudomonas corrugata 28 mutant impaired in a pyridine nucleotide transhydrogenase gene. Res Microbiol 162: 747–755.
    • (2011) Res Microbiol , vol.162 , pp. 747-755
    • Decorosi, F.1    Lori, L.2    Santopolo, L.3    Tatti, E.4    Giovannetti, L.5    Viti, C.6
  • 23
    • 33744951971 scopus 로고    scopus 로고
    • Transcriptional tradeoff between metabolic and stress-response programs in Pseudomonas putida KT2440 cells exposed to toluene
    • Domínguez-Cuevas, P., González-Pastor, J.E., Marqués, S., Ramos, J.L., and de Lorenzo, V. (2006) Transcriptional tradeoff between metabolic and stress-response programs in Pseudomonas putida KT2440 cells exposed to toluene. J Biol Chem 281: 11981–11991.
    • (2006) J Biol Chem , vol.281 , pp. 11981-11991
    • Domínguez-Cuevas, P.1    González-Pastor, J.E.2    Marqués, S.3    Ramos, J.L.4    de Lorenzo, V.5
  • 25
    • 80052787409 scopus 로고    scopus 로고
    • Response of Pseudomonas putida KT2440 to increased NADH and ATP demand
    • Ebert, B.E., Kurth, F., Grund, M., Blank, L.M., and Schmid, A. (2011) Response of Pseudomonas putida KT2440 to increased NADH and ATP demand. Appl Environ Microbiol 77: 6597–6605.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 6597-6605
    • Ebert, B.E.1    Kurth, F.2    Grund, M.3    Blank, L.M.4    Schmid, A.5
  • 26
    • 84934909312 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit
    • Fisher-Wellman, K.H., Lin, C.T., Ryan, T.E., Reese, L.R., Gilliam, L.A., Cathey, B.L., et al. (2015) Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit. Biochem J 467: 271–280.
    • (2015) Biochem J , vol.467 , pp. 271-280
    • Fisher-Wellman, K.H.1    Lin, C.T.2    Ryan, T.E.3    Reese, L.R.4    Gilliam, L.A.5    Cathey, B.L.6
  • 27
    • 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
  • 28
    • 64049099490 scopus 로고    scopus 로고
    • Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism
    • Fuhrer, T., and Sauer, U. (2009) Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism. J Bacteriol 191: 2112–2121.
    • (2009) J Bacteriol , vol.191 , pp. 2112-2121
    • Fuhrer, T.1    Sauer, U.2
  • 29
    • 29244444522 scopus 로고    scopus 로고
    • Fluorescence probes used for detection of reactive oxygen species
    • Gomes, A., Fernandes, E., and Lima, J.L.F.C. (2005) Fluorescence probes used for detection of reactive oxygen species. J Biochem Biophys Methods 65: 45–80.
    • (2005) J Biochem Biophys Methods , vol.65 , pp. 45-80
    • Gomes, A.1    Fernandes, E.2    Lima, J.L.F.C.3
  • 31
    • 0036291504 scopus 로고    scopus 로고
    • Measuring β-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays
    • Griffith, K.L., and Wolf, R.E. (2002) Measuring β-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays. Biochem Biophys Res Commun 290: 397–402.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 397-402
    • Griffith, K.L.1    Wolf, R.E.2
  • 32
    • 0018866929 scopus 로고
    • Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli
    • Hanson, R.L., and Rose, C. (1980) Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli. J Bacteriol 141: 401–404.
    • (1980) J Bacteriol , vol.141 , pp. 401-404
    • Hanson, R.L.1    Rose, C.2
  • 33
    • 33947228075 scopus 로고    scopus 로고
    • Solvent-tolerant bacteria for biotransformations in two-phase fermentation systems
    • Heipieper, H.J., Neumann, G., Cornelissen, S., and Meinhardt, F. (2007) Solvent-tolerant bacteria for biotransformations in two-phase fermentation systems. Appl Microbiol Biotechnol 74: 961–973.
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 961-973
    • Heipieper, H.J.1    Neumann, G.2    Cornelissen, S.3    Meinhardt, F.4
  • 34
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • Hoek, J.B., and Rydström, J. (1988) Physiological roles of nicotinamide nucleotide transhydrogenase. Biochem J 254: 1–10.
    • (1988) Biochem J , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydström, J.2
  • 35
    • 77952911331 scopus 로고    scopus 로고
    • Metabolic and transcriptional response to cofactor perturbations in Escherichia coli
    • Holm, A.K., Blank, L.M., Oldiges, M., Schmid, A., Solem, C., Jensen, P.R., and Vemuri, G.N. (2010) Metabolic and transcriptional response to cofactor perturbations in Escherichia coli. J Biol Chem 285: 17498–17506.
    • (2010) J Biol Chem , vol.285 , pp. 17498-17506
    • Holm, A.K.1    Blank, L.M.2    Oldiges, M.3    Schmid, A.4    Solem, C.5    Jensen, P.R.6    Vemuri, G.N.7
  • 36
    • 84886747287 scopus 로고    scopus 로고
    • Metabolic engineering and transhydrogenase effects on NADPH availability in Escherichia coli
    • Jan, J., Martínez, I., Wang, Y., Bennett, G.N., and San, K.Y. (2013) Metabolic engineering and transhydrogenase effects on NADPH availability in Escherichia coli. Biotechnol Prog 29: 1124–1130.
    • (2013) Biotechnol Prog , vol.29 , pp. 1124-1130
    • Jan, J.1    Martínez, I.2    Wang, Y.3    Bennett, G.N.4    San, K.Y.5
  • 37
    • 0036933805 scopus 로고    scopus 로고
    • Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440
    • Jiménez, J.I., Miñambres, B., García, J.L., and Díaz, E. (2002) Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440. Environ Microbiol 4: 824–841.
    • (2002) Environ Microbiol , vol.4 , pp. 824-841
    • Jiménez, J.I.1    Miñambres, B.2    García, J.L.3    Díaz, E.4
  • 38
    • 13944279087 scopus 로고
    • Pyridine nucleotide transhydrogenase. II. Direct evidence for and mechanism of the transhydrogenase reaction
    • Kaplan, N.O., Colowick, S.P., and Neufeld, E.F. (1952) Pyridine nucleotide transhydrogenase. II. Direct evidence for and mechanism of the transhydrogenase reaction. J Biol Chem 195: 107–119.
    • (1952) J Biol Chem , vol.195 , pp. 107-119
    • Kaplan, N.O.1    Colowick, S.P.2    Neufeld, E.F.3
  • 39
    • 84905965348 scopus 로고    scopus 로고
    • Oxidative stress response in Pseudomonas putida
    • Kim, J., and Park, W. (2014) Oxidative stress response in Pseudomonas putida. Appl Microbiol Biotechnol 98: 6933–6946.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 6933-6946
    • Kim, J.1    Park, W.2
  • 40
    • 84887648944 scopus 로고    scopus 로고
    • Transcriptomic fingerprinting of Pseudomonas putida under alternative physiological regimes
    • Kim, J., Oliveros, J.C., Nikel, P.I., de Lorenzo, V., and Silva-Rocha, R. (2013) Transcriptomic fingerprinting of Pseudomonas putida under alternative physiological regimes. Environ Microbiol Rep 5: 883–891.
    • (2013) Environ Microbiol Rep , vol.5 , pp. 883-891
    • Kim, J.1    Oliveros, J.C.2    Nikel, P.I.3    de Lorenzo, V.4    Silva-Rocha, R.5
  • 42
    • 84876674407 scopus 로고    scopus 로고
    • Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation
    • Lee, W.H., Kim, M.D., Jin, Y.S., and Seo, J.H. (2013) Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation. Appl Microbiol Biotechnol 97: 2761–2772.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2761-2772
    • Lee, W.H.1    Kim, M.D.2    Jin, Y.S.3    Seo, J.H.4
  • 43
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
    • López de Felipe, F., Kleerebezem, M., de Vos, W.M., and Hugenholtz, J. (1998) Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J Bacteriol 180: 3804–3808.
    • (1998) J Bacteriol , vol.180 , pp. 3804-3808
    • López de Felipe, F.1    Kleerebezem, M.2    de Vos, W.M.3    Hugenholtz, J.4
  • 44
    • 84934300609 scopus 로고    scopus 로고
    • Chemical reactivity drives spatiotemporal organisation of bacterial metabolism
    • de Lorenzo, V., Sekowska, A., and Danchin, A. (2015) Chemical reactivity drives spatiotemporal organisation of bacterial metabolism. FEMS Microbiol Rev 39: 96–119.
    • (2015) FEMS Microbiol Rev , vol.39 , pp. 96-119
    • de Lorenzo, V.1    Sekowska, A.2    Danchin, A.3
  • 45
    • 79952489564 scopus 로고    scopus 로고
    • Metabolic networks to combat oxidative stress in Pseudomonas fluorescens
    • Mailloux, R.J., Lemire, J., and Appanna, V.D. (2011) Metabolic networks to combat oxidative stress in Pseudomonas fluorescens. Antonie van Leeuwenhoek 99: 433–442.
    • (2011) Antonie van Leeuwenhoek , vol.99 , pp. 433-442
    • Mailloux, R.J.1    Lemire, J.2    Appanna, V.D.3
  • 46
    • 84887177785 scopus 로고    scopus 로고
    • Comparative proteomic analysis reveals mechanistic insights into Pseudomonas putida F1 growth on benzoate and citrate
    • Mandalakis, M., Panikov, N., Dai, S., Ray, S., and Karger, B.L. (2013) Comparative proteomic analysis reveals mechanistic insights into Pseudomonas putida F1 growth on benzoate and citrate. AMB Express 3: 64.
    • (2013) AMB Express , vol.3 , pp. 64
    • Mandalakis, M.1    Panikov, N.2    Dai, S.3    Ray, S.4    Karger, B.L.5
  • 48
    • 80053648189 scopus 로고    scopus 로고
    • Engineering multiple genomic deletions in Gram-negative bacteria: analysis of the multi-resistant antibiotic profile of Pseudomonas putida KT2440
    • Martínez-García, E., and de Lorenzo, V. (2011) Engineering multiple genomic deletions in Gram-negative bacteria: analysis of the multi-resistant antibiotic profile of Pseudomonas putida KT2440. Environ Microbiol 13: 2702–2716.
    • (2011) Environ Microbiol , vol.13 , pp. 2702-2716
    • Martínez-García, E.1    de Lorenzo, V.2
  • 49
    • 84946019816 scopus 로고    scopus 로고
    • New transposon tools tailored for metabolic engineering of Gram-negative microbial cell factories
    • Martínez-García, E., Aparicio, T., de Lorenzo, V., and Nikel, P.I. (2014a) New transposon tools tailored for metabolic engineering of Gram-negative microbial cell factories. Front Bioeng Biotechnol 2: 46.
    • (2014) Front Bioeng Biotechnol , vol.2 , pp. 46
    • Martínez-García, E.1    Aparicio, T.2    de Lorenzo, V.3    Nikel, P.I.4
  • 52
  • 53
    • 84940646298 scopus 로고    scopus 로고
    • Reversal of mitochondrial transhydrogenase causes oxidative stress in heart failure
    • Nickel, A.G., von Hardenberg, A., Hohl, M., Löffler, J.R., Kohlhaas, M., Becker, J., et al. (2015) Reversal of mitochondrial transhydrogenase causes oxidative stress in heart failure. Cell Metab 22: 472–484.
    • (2015) Cell Metab , vol.22 , pp. 472-484
    • Nickel, A.G.1    von Hardenberg, A.2    Hohl, M.3    Löffler, J.R.4    Kohlhaas, M.5    Becker, J.6
  • 54
    • 84872193848 scopus 로고    scopus 로고
    • Implantation of unmarked regulatory and metabolic modules in Gram-negative bacteria with specialised mini-transposon delivery vectors
    • Nikel, P.I., and de Lorenzo, V. (2013a) Implantation of unmarked regulatory and metabolic modules in Gram-negative bacteria with specialised mini-transposon delivery vectors. J Biotechnol 163: 143–154.
    • (2013) J Biotechnol , vol.163 , pp. 143-154
    • Nikel, P.I.1    de Lorenzo, V.2
  • 55
    • 84871436225 scopus 로고    scopus 로고
    • Engineering an anaerobic metabolic regime in Pseudomonas putida KT2440 for the anoxic biodegradation of 1,3-dichloroprop-1-ene
    • Nikel, P.I., and de Lorenzo, V. (2013b) Engineering an anaerobic metabolic regime in Pseudomonas putida KT2440 for the anoxic biodegradation of 1,3-dichloroprop-1-ene. Metab Eng 15: 98–112.
    • (2013) Metab Eng , vol.15 , pp. 98-112
    • Nikel, P.I.1    de Lorenzo, V.2
  • 56
    • 85019615262 scopus 로고    scopus 로고
    • Quantitative physiology approaches to understand and optimize reducing power availability in environmental bacteria
    • In, McGenity, T.J., Timmis, K.N., Nogales-Fernández, B., (eds)., Heidelberg, Germany, Humana Press
    • Nikel, P.I., and Chavarría, M. (2015) Quantitative physiology approaches to understand and optimize reducing power availability in environmental bacteria. In Hydrocarbon and Lipid Microbiology Protocols. McGenity, T.J., Timmis, K.N., and Nogales-Fernández, B. (eds). Heidelberg, Germany: Humana Press, pp. 1–32.
    • (2015) Hydrocarbon and Lipid Microbiology Protocols , pp. 1-32
    • Nikel, P.I.1    Chavarría, M.2
  • 57
    • 84875059461 scopus 로고    scopus 로고
    • Why are chlorinated pollutants so difficult to degrade aerobically? Redox stress limits 1,3-dichloroprop-1-ene metabolism by Pseudomonas pavonaceae
    • Nikel, P.I., Pérez-Pantoja, D., and de Lorenzo, V. (2013a) Why are chlorinated pollutants so difficult to degrade aerobically? Redox stress limits 1,3-dichloroprop-1-ene metabolism by Pseudomonas pavonaceae. Philos Trans R Soc Lond B Biol Sci 368: 20120377.
    • (2013) Philos Trans R Soc Lond B Biol Sci , vol.368 , pp. 20120377
    • Nikel, P.I.1    Pérez-Pantoja, D.2    de Lorenzo, V.3
  • 58
    • 84877842924 scopus 로고    scopus 로고
    • Accumulation of inorganic polyphosphate enables stress endurance and catalytic vigour in Pseudomonas putida KT2440
    • Nikel, P.I., Chavarría, M., Martínez-García, E., Taylor, A.C., and de Lorenzo, V. (2013b) Accumulation of inorganic polyphosphate enables stress endurance and catalytic vigour in Pseudomonas putida KT2440. Microb Cell Fact 12: 50.
    • (2013) Microb Cell Fact , vol.12 , pp. 50
    • Nikel, P.I.1    Chavarría, M.2    Martínez-García, E.3    Taylor, A.C.4    de Lorenzo, V.5
  • 59
    • 84891635026 scopus 로고    scopus 로고
    • Metabolic and regulatory rearrangements underlying glycerol metabolism in Pseudomonas putida KT2440
    • Nikel, P.I., Kim, J., and de Lorenzo, V. (2014a) Metabolic and regulatory rearrangements underlying glycerol metabolism in Pseudomonas putida KT2440. Environ Microbiol 16: 239–254.
    • (2014) Environ Microbiol , vol.16 , pp. 239-254
    • Nikel, P.I.1    Kim, J.2    de Lorenzo, V.3
  • 60
    • 84898874640 scopus 로고    scopus 로고
    • Biotechnological domestication of pseudomonads using synthetic biology
    • Nikel, P.I., Martínez-García, E., and de Lorenzo, V. (2014b) Biotechnological domestication of pseudomonads using synthetic biology. Nat Rev Microbiol 12: 368–379.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 368-379
    • Nikel, P.I.1    Martínez-García, E.2    de Lorenzo, V.3
  • 61
    • 84896710626 scopus 로고    scopus 로고
    • The private life of environmental bacteria: pollutant biodegradation at the single cell level
    • Nikel, P.I., Silva-Rocha, R., Benedetti, I., and de Lorenzo, V. (2014c) The private life of environmental bacteria: pollutant biodegradation at the single cell level. Environ Microbiol 16: 628–642.
    • (2014) Environ Microbiol , vol.16 , pp. 628-642
    • Nikel, P.I.1    Silva-Rocha, R.2    Benedetti, I.3    de Lorenzo, V.4
  • 62
    • 84944910018 scopus 로고    scopus 로고
    • Pseudomonas putida KT2440 strain metabolizes glucose through a cycle formed by enzymes of the Entner-Doudoroff, Embden-Meyerhof-Parnas, and pentose phosphate pathways
    • Nikel, P.I., Chavarría, M., Fuhrer, T., Sauer, U., and de Lorenzo, V. (2015) Pseudomonas putida KT2440 strain metabolizes glucose through a cycle formed by enzymes of the Entner-Doudoroff, Embden-Meyerhof-Parnas, and pentose phosphate pathways. J Biol Chem 290: 25920–25932.
    • (2015) J Biol Chem , vol.290 , pp. 25920-25932
    • Nikel, P.I.1    Chavarría, M.2    Fuhrer, T.3    Sauer, U.4    de Lorenzo, V.5
  • 63
    • 84969963522 scopus 로고    scopus 로고
    • From dirt to industrial applications: Pseudomonas putida as a synthetic biology chassis for hosting harsh biochemical reactions
    • Nikel, P.I., Chavarría, M., Danchin, A., and de Lorenzo, V. (2016) From dirt to industrial applications: Pseudomonas putida as a synthetic biology chassis for hosting harsh biochemical reactions. Curr Opin Chem Biol 34: 20–29.
    • (2016) Curr Opin Chem Biol , vol.34 , pp. 20-29
    • Nikel, P.I.1    Chavarría, M.2    Danchin, A.3    de Lorenzo, V.4
  • 65
    • 84864767803 scopus 로고    scopus 로고
    • A protocol for in vivo detection of reactive oxygen species
    • Owusu-Ansah, E., Yavari, A., and Banerjee, U. (2008) A protocol for in vivo detection of reactive oxygen species. Prot Exchange doi: 10.1038/nprot.2008.1023.
    • (2008) Prot Exchange
    • Owusu-Ansah, E.1    Yavari, A.2    Banerjee, U.3
  • 66
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
    • Pérez, J.M., Arenas, F.A., Pradenas, G.A., Sandoval, J.M., and Vásquez, C.C. (2008) Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes. J Biol Chem 283: 7346–7353.
    • (2008) J Biol Chem , vol.283 , pp. 7346-7353
    • Pérez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vásquez, C.C.5
  • 67
    • 58149197596 scopus 로고    scopus 로고
    • OperonDB: a comprehensive database of predicted operons in microbial genomes
    • Pertea, M., Ayanbule, K., Smedinghoff, M., and Salzberg, S.L. (2009) OperonDB: a comprehensive database of predicted operons in microbial genomes. Nucleic Acids Res 37: D479–D482.
    • (2009) Nucleic Acids Res , vol.37 , pp. D479-D482
    • Pertea, M.1    Ayanbule, K.2    Smedinghoff, M.3    Salzberg, S.L.4
  • 68
    • 84884653783 scopus 로고    scopus 로고
    • Endogenous stress caused by faulty oxidation reactions fosters evolution of 2,4-dinitrotoluene-degrading bacteria
    • Pérez-Pantoja, D., Nikel, P.I., Chavarría, M., and de Lorenzo, V. (2013) Endogenous stress caused by faulty oxidation reactions fosters evolution of 2,4-dinitrotoluene-degrading bacteria. PLoS Genet 9: e1003764.
    • (2013) PLoS Genet , vol.9
    • Pérez-Pantoja, D.1    Nikel, P.I.2    Chavarría, M.3    de Lorenzo, V.4
  • 70
    • 0030860391 scopus 로고    scopus 로고
    • Transcriptional control of the Pseudomonas TOL plasmid catabolic operons is achieved through an interplay of host factors and plasmid-encoded regulators
    • Ramos, J.L., Marqués, S., and Timmis, K.N. (1997) Transcriptional control of the Pseudomonas TOL plasmid catabolic operons is achieved through an interplay of host factors and plasmid-encoded regulators. Annu Rev Microbiol 51: 341–373.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 341-373
    • Ramos, J.L.1    Marqués, S.2    Timmis, K.N.3
  • 72
    • 2642659608 scopus 로고
    • Translational efficiency of the Escherichia coli adenylate cyclase gene: mutating the UUG initiation codon to GUG or AUG results in increased gene expression
    • Reddy, P., Peterkofsky, A., and McKenney, K. (1985) Translational efficiency of the Escherichia coli adenylate cyclase gene: mutating the UUG initiation codon to GUG or AUG results in increased gene expression. Proc Natl Acad Sci USA 82: 5656–5660.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5656-5660
    • Reddy, P.1    Peterkofsky, A.2    McKenney, K.3
  • 73
    • 33645464499 scopus 로고    scopus 로고
    • dye (arc) mutants: insights into an unexplained phenotype and its suppression by the synthesis of poly(3-hydroxybutyrate) in Escherichia coli recombinants
    • Ruiz, J.A., Fernández, R.O., Nikel, P.I., Méndez, B.S., and Pettinari, M.J. (2006) dye (arc) mutants: insights into an unexplained phenotype and its suppression by the synthesis of poly(3-hydroxybutyrate) in Escherichia coli recombinants. FEMS Microbiol Lett 258: 55–60.
    • (2006) FEMS Microbiol Lett , vol.258 , pp. 55-60
    • Ruiz, J.A.1    Fernández, R.O.2    Nikel, P.I.3    Méndez, B.S.4    Pettinari, M.J.5
  • 74
    • 33646045867 scopus 로고    scopus 로고
    • Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli
    • Sánchez, A.M., Andrews, J., Hussein, I., Bennett, G.N., and San, K.Y. (2006) Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli. Biotechnol Prog 22: 420–425.
    • (2006) Biotechnol Prog , vol.22 , pp. 420-425
    • Sánchez, A.M.1    Andrews, J.2    Hussein, I.3    Bennett, G.N.4    San, K.Y.5
  • 75
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • Sauer, U., Canonaco, F., Heri, S., Perrenoud, A., and Fischer, E. (2004) The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J Biol Chem 279: 6613–6619.
    • (2004) J Biol Chem , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 76
    • 27844581259 scopus 로고    scopus 로고
    • Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli
    • Semchyshyn, H., Bagnyukova, T., Storey, K., and Lushchak, V. (2005) Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli. Cell Biol Int 29: 898–902.
    • (2005) Cell Biol Int , vol.29 , pp. 898-902
    • Semchyshyn, H.1    Bagnyukova, T.2    Storey, K.3    Lushchak, V.4
  • 77
    • 84876567509 scopus 로고    scopus 로고
    • The standard European vector architecture (SEVA): a coherent platform for the analysis and deployment of complex prokaryotic phenotypes
    • Silva-Rocha, R., Martínez-García, E., Calles, B., Chavarría, M., Arce-Rodríguez, A., de las Heras, A., et al. (2013) The standard European vector architecture (SEVA): a coherent platform for the analysis and deployment of complex prokaryotic phenotypes. Nucleic Acids Res 41: D666–D675.
    • (2013) Nucleic Acids Res , vol.41 , pp. D666-D675
    • Silva-Rocha, R.1    Martínez-García, E.2    Calles, B.3    Chavarría, M.4    Arce-Rodríguez, A.5    de las Heras, A.6
  • 78
    • 34548563918 scopus 로고    scopus 로고
    • Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens
    • Singh, R., Mailloux, R.J., Puiseux-Dao, S., and Appanna, V.D. (2007) Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens. J Bacteriol 189: 6665–6675.
    • (2007) J Bacteriol , vol.189 , pp. 6665-6675
    • Singh, R.1    Mailloux, R.J.2    Puiseux-Dao, S.3    Appanna, V.D.4
  • 81
    • 84943273496 scopus 로고    scopus 로고
    • Pseudomonas putida mt-2 tolerates reactive oxygen species generated during matric stress by inducing a major oxidative defense response
    • Svenningsen, N.B., Pérez-Pantoja, D., Nikel, P.I., Nicolaisen, M.H., de Lorenzo, V., and Nybroe, O. (2015) Pseudomonas putida mt-2 tolerates reactive oxygen species generated during matric stress by inducing a major oxidative defense response. BMC Microbiol 15: 202.
    • (2015) BMC Microbiol , vol.15 , pp. 202
    • Svenningsen, N.B.1    Pérez-Pantoja, D.2    Nikel, P.I.3    Nicolaisen, M.H.4    de Lorenzo, V.5    Nybroe, O.6
  • 82
    • 10444278093 scopus 로고    scopus 로고
    • Expression of glutathione S-transferase and peptide methionine sulphoxide reductase in Ochrobactrum anthropi is correlated to the production of reactive oxygen species caused by aromatic substrates
    • Tamburro, A., Robuffo, I., Heipieper, H.J., Allocati, N., Rotilio, D., Di Ilio, C., and Favaloro, B. (2004) Expression of glutathione S-transferase and peptide methionine sulphoxide reductase in Ochrobactrum anthropi is correlated to the production of reactive oxygen species caused by aromatic substrates. FEMS Microbiol Lett 241: 151–156.
    • (2004) FEMS Microbiol Lett , vol.241 , pp. 151-156
    • Tamburro, A.1    Robuffo, I.2    Heipieper, H.J.3    Allocati, N.4    Rotilio, D.5    Di Ilio, C.6    Favaloro, B.7
  • 83
    • 33646578756 scopus 로고    scopus 로고
    • Overflow metabolism in Escherichia coli during steady-state growth: transcriptional regulation and effect of the redox ratio
    • Vemuri, G.N., Altman, E., Sangurdekar, D.P., Khodursky, A.B., and Eiteman, M.A. (2006) Overflow metabolism in Escherichia coli during steady-state growth: transcriptional regulation and effect of the redox ratio. Appl Environ Microbiol 72: 3653–3661.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3653-3661
    • Vemuri, G.N.1    Altman, E.2    Sangurdekar, D.P.3    Khodursky, A.B.4    Eiteman, M.A.5
  • 84
    • 0021095336 scopus 로고
    • Why are two different types of pyridine nucleotide transhydrogenase found in living organisms?
    • Voordouw, G., van der Vies, S.M., and Themmen, A.P. (1983) Why are two different types of pyridine nucleotide transhydrogenase found in living organisms? Eur J Biochem 131: 527–533.
    • (1983) Eur J Biochem , vol.131 , pp. 527-533
    • Voordouw, G.1    van der Vies, S.M.2    Themmen, A.P.3
  • 85
    • 0031056720 scopus 로고    scopus 로고
    • Bacterial glutathione S-transferases: what are they good for?
    • Vuilleumier, S. (1997) Bacterial glutathione S-transferases: what are they good for? J Bacteriol 179: 1431–1441.
    • (1997) J Bacteriol , vol.179 , pp. 1431-1441
    • Vuilleumier, S.1
  • 86
    • 0016197816 scopus 로고
    • Metabolism of benzoate and the methylbenzoates by Pseudomonas putida (arvilla) mt-2: evidence for the existence of a TOL plasmid
    • Williams, P.A., and Murray, K. (1974) Metabolism of benzoate and the methylbenzoates by Pseudomonas putida (arvilla) mt-2: evidence for the existence of a TOL plasmid. J Bacteriol 120: 416–423.
    • (1974) J Bacteriol , vol.120 , pp. 416-423
    • Williams, P.A.1    Murray, K.2
  • 87
    • 84976908656 scopus 로고    scopus 로고
    • Enhanced annotations and features for comparing thousands of Pseudomonas genomes in the Pseudomonas genome database
    • Winsor, G.L., Griffiths, E.J., Lo, R., Dhillon, B.K., Shay, J.A., and Brinkman, F.S. (2016) Enhanced annotations and features for comparing thousands of Pseudomonas genomes in the Pseudomonas genome database. Nucleic Acids Res 44: D646–D653.
    • (2016) Nucleic Acids Res , vol.44 , pp. D646-D653
    • Winsor, G.L.1    Griffiths, E.J.2    Lo, R.3    Dhillon, B.K.4    Shay, J.A.5    Brinkman, F.S.6


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