메뉴 건너뛰기




Volumn 2, Issue 2 SPEC. ISS., 2009, Pages 287-294

Microbial responses to xenobiotic compounds. Identification of genes that allow Pseudomonas putida KT2440 to cope with 2,4,6-trinitrotoluene

Author keywords

[No Author keywords available]

Indexed keywords

1 AMINO 1,3 CYCLOPENTANEDICARBOXYLIC ACID; AROMATIC NITRO COMPOUND; DNA; ENZYME; GLUCOSE; ISOQUINOLINE; NITROREDUCTASE; OXIDOREDUCTASE; PNRA ENZYME; TRINITROTOLUENE; UNCLASSIFIED DRUG; XEND ENZYME; XENOBIOTIC AGENT;

EID: 70350708933     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2009.00085.x     Document Type: Article
Times cited : (54)

References (53)
  • 1
    • 34447540214 scopus 로고    scopus 로고
    • Acid-shock responses in staphylococcus aureus investigated by global gene expression analysis
    • Bore, E., Langsrud, S., Langsrud, Ø., Rode, T.M., and Holck, A. (2007) Acid-shock responses in staphylococcus aureus investigated by global gene expression analysis. Microbiology 153: 289-303.
    • (2007) Microbiology , vol.153 , pp. 289-303
    • Bore, E.1    Langsrud, S.2    Langsrud, Ø.3    Rode, T.M.4    Holck, A.5
  • 2
    • 34247099407 scopus 로고    scopus 로고
    • Quantification of changing Pseudomonas aeruginosa sodA, htpX and mt gene abundance in response to trace metal toxicity: A potential in situ biomarker of environmental health
    • Bouskill, N.J., Barnhart, E.P., Galloway, T.S., Handy, R.D., and Ford, T.E. (2007) Quantification of changing Pseudomonas aeruginosa sodA, htpX and mt gene abundance in response to trace metal toxicity: a potential in situ biomarker of environmental health. FEMS Microbiol Ecol 60: 276-286.
    • (2007) FEMS Microbiol Ecol , vol.60 , pp. 276-286
    • Bouskill, N.J.1    Barnhart, E.P.2    Galloway, T.S.3    Handy, R.D.4    Ford, T.E.5
  • 3
    • 0025892415 scopus 로고
    • Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae
    • Bryant, C., and DeLuca, M. (1991) Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae. J Biol Chem 266: 4119-4125.
    • (1991) J Biol Chem , vol.266 , pp. 4119-4125
    • Bryant, C.1    DeLuca, M.2
  • 4
    • 20444364023 scopus 로고    scopus 로고
    • PnrA, a new nitroreductase-family enzyme in the TNT-degrading strain Pseudomonas putida JLR11
    • Caballero, A., Lázaro, J.J., Ramos, J.L., and Esteve-Nuñez, A. (2005) PnrA, a new nitroreductase-family enzyme in the TNT-degrading strain Pseudomonas putida JLR11. Environ Microbiol 7: 1211-1219.
    • (2005) Environ Microbiol , vol.7 , pp. 1211-1219
    • Caballero, A.1    Lázaro, J.J.2    Ramos, J.L.3    Esteve-Nuñez, A.4
  • 8
    • 55049133449 scopus 로고    scopus 로고
    • Subfunctionalization of hydride transferases of the Old Yellow Enzyme family of flavoproteins of Pseudomonas putida
    • van Dillewijn, P., Wittich, R.M., Caballero, A., and Ramos, J.L. (2008a) Subfunctionalization of hydride transferases of the Old Yellow Enzyme family of flavoproteins of Pseudomonas putida. Appl Environ Microbiol 74: 6703-6708.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6703-6708
    • Van Dillewijn, P.1    Wittich, R.M.2    Caballero, A.3    Ramos, J.L.4
  • 9
    • 55049102309 scopus 로고    scopus 로고
    • Type II hydride transferases from different microorganisms yield nitrite and diarylamines from polynitroaromatic compounds
    • van Dillewijn, P., Wittich, R.M., Caballero, A., and Ramos, J.L. (2008b) Type II hydride transferases from different microorganisms yield nitrite and diarylamines from polynitroaromatic compounds. Appl Environ Microbiol 74: 6820-6823.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6820-6823
    • Van Dillewijn, P.1    Wittich, R.M.2    Caballero, A.3    Ramos, J.L.4
  • 11
    • 0038820069 scopus 로고    scopus 로고
    • Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response
    • Fitzpatrick, T.B., Amrhein, N., and Macheroux, P. (2003) Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response. J Biol Chem 278: 19891-19897.
    • (2003) J Biol Chem , vol.278 , pp. 19891-19897
    • Fitzpatrick, T.B.1    Amrhein, N.2    Macheroux, P.3
  • 12
    • 33744991789 scopus 로고    scopus 로고
    • A glutathione S-transferase catalyzes the dehalogenation of inhibitory metabolites of polychlorinated biphenyls
    • Fortin, P.D., Horsman, G.P., Yang, H.M., and Eltis, L.D. (2006) A glutathione S-transferase catalyzes the dehalogenation of inhibitory metabolites of polychlorinated biphenyls. J Bacteriol 188: 4424-4430.
    • (2006) J Bacteriol , vol.188 , pp. 4424-4430
    • Fortin, P.D.1    Horsman, G.P.2    Yang, H.M.3    Eltis, L.D.4
  • 13
    • 34547192667 scopus 로고    scopus 로고
    • Transcriptome analysis reveals that multidrug efflux genes are upregulated to protect Pseudomonas aeruginosa from pentachlorophenol stress
    • Fraga-Muller, J., Stevens, A.M., Craig, J., and Love, N.G. (2007) Transcriptome analysis reveals that multidrug efflux genes are upregulated to protect Pseudomonas aeruginosa from pentachlorophenol stress. Appl Environ Microbiol 73: 4550-4558.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4550-4558
    • Fraga-Muller, J.1    Stevens, A.M.2    Craig, J.3    Love, N.G.4
  • 14
    • 53149116351 scopus 로고    scopus 로고
    • Tracing explosives in soil with transcriptional regulators of Pseudomonas putida evolved for responding to nitrotoluenes
    • Garmendia, J., de las Heras, A., Calcagno Galvão, T., and de Lorenzo, V. (2008) Tracing explosives in soil with transcriptional regulators of Pseudomonas putida evolved for responding to nitrotoluenes. Microb Biotechnol 1: 236-246.
    • (2008) Microb Biotechnol , vol.1 , pp. 236-246
    • Garmendia, J.1    De Las Heras, A.2    Calcagno Galvão, T.3    De Lorenzo, V.4
  • 16
    • 34248590170 scopus 로고    scopus 로고
    • Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth
    • González-Pérez, M.M., van Dillewijn, P., Wittich, R.M., and Ramos, J.L. (2007) Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth. Environ Microbiol 9: 1535-1540.
    • (2007) Environ Microbiol , vol.9 , pp. 1535-1540
    • González-Pérez, M.M.1    Van Dillewijn, P.2    Wittich, R.M.3    Ramos, J.L.4
  • 18
    • 8644260716 scopus 로고    scopus 로고
    • Analysis of TNT (2,4,6-trinitrotoluene) inducible cellular responses and stress shock proteome in Stenotrophomonas sp. O.K-5
    • Ho, E.M., Chang, H.W., Kim, S.I., Kahng, H.Y., and Oh, K.H. (2004) Analysis of TNT (2,4,6-trinitrotoluene) inducible cellular responses and stress shock proteome in Stenotrophomonas sp. O.K-5. Curr Microbiol 49: 346-352.
    • (2004) Curr Microbiol , vol.49 , pp. 346-352
    • Ho, E.M.1    Chang, H.W.2    Kim, S.I.3    Kahng, H.Y.4    Oh, K.H.5
  • 19
    • 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
  • 20
    • 0037192150 scopus 로고    scopus 로고
    • Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase
    • Kiefer, P.M., Jr. and Copley, S.D. (2002) Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase. Biochemistry 41: 1315-1322.
    • (2002) Biochemistry , vol.41 , pp. 1315-1322
    • Kiefer Jr., P.M.1    Copley, S.D.2
  • 21
    • 0025896449 scopus 로고
    • Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX
    • Kornitzer, D., Teff, D., Altuvia, S., and Oppenheim, A.B. (1991) Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX. J Bacteriol 173: 2944-2953.
    • (1991) J Bacteriol , vol.173 , pp. 2944-2953
    • Kornitzer, D.1    Teff, D.2    Altuvia, S.3    Oppenheim, A.B.4
  • 22
    • 27744503862 scopus 로고    scopus 로고
    • Biochemical characterization of nitrotoluene transforming oxygen-insensitive nitroreductases from Clostridium acetobutylicum ATCC 824
    • Kutty, R., and Bennett, G.N. (2005) Biochemical characterization of nitrotoluene transforming oxygen-insensitive nitroreductases from Clostridium acetobutylicum ATCC 824. Arch Microbiol 184: 158-167.
    • (2005) Arch Microbiol , vol.184 , pp. 158-167
    • Kutty, R.1    Bennett, G.N.2
  • 23
    • 0031016991 scopus 로고    scopus 로고
    • Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa
    • Köhler, T., Michéa-Hamzehpour, M., Henze, U., Gotoh, N., Curty, L.K., and Pechère, J.C. (1997) Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa. Mol Microbiol 23: 345-354.
    • (1997) Mol Microbiol , vol.23 , pp. 345-354
    • Köhler, T.1    Michéa-Hamzehpour, M.2    Henze, U.3    Gotoh, N.4    Curty, L.K.5    Pechère, J.C.6
  • 24
    • 1842483586 scopus 로고    scopus 로고
    • Bioremediation of soils contaminated with explosives
    • Lewis, A.T., Newcombe, D.A., and Crawford, R.L. (2004) Bioremediation of soils contaminated with explosives. J Environ Manage 70: 291-307.
    • (2004) J Environ Manage , vol.70 , pp. 291-307
    • Lewis, A.T.1    Newcombe, D.A.2    Crawford, R.L.3
  • 25
    • 0032455186 scopus 로고    scopus 로고
    • Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance
    • Li, X.Z., Zhang, L., and Poole, K. (1998) Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance. J Bacteriol 180: 2987-2991.
    • (1998) J Bacteriol , vol.180 , pp. 2987-2991
    • Li, X.Z.1    Zhang, L.2    Poole, K.3
  • 26
    • 34648830900 scopus 로고    scopus 로고
    • Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
    • Liu, G., Zhou, J., Lv, H., Xiang, X., Wang, J., Zhou, M., and Qv, Y. (2007) Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase. Appl Microbiol Biotechnol 76: 1271-1279.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1271-1279
    • Liu, G.1    Zhou, J.2    Lv, H.3    Xiang, X.4    Wang, J.5    Zhou, M.6    Qv, Y.7
  • 27
    • 0345698706 scopus 로고    scopus 로고
    • pTn5cat: A Tn5-derived genetic element to facilitate insertion mutagenesis, promoter probing, physical mapping, cloning, and marker exchange in phytopathogenic and other gram-negative bacteria
    • Marsch-Moreno, R., Hernández-Guzmán, G., and Alvarez- Morales, A. (1998) pTn5cat: a Tn5-derived genetic element to facilitate insertion mutagenesis, promoter probing, physical mapping, cloning, and marker exchange in phytopathogenic and other gram-negative bacteria. Plasmid 39: 205-214.
    • (1998) Plasmid , vol.39 , pp. 205-214
    • Marsch-Moreno, R.1    Hernández-Guzmán, G.2    Alvarez- Morales, A.3
  • 28
    • 0036437005 scopus 로고    scopus 로고
    • A novel assembly process of the multicomponent xenobiotic efflux pump in Pseudomonas aeruginosa
    • Maseda, H., Kitao, M., Eda, S., Yoshihara, E., and Nakae, T. (2002) A novel assembly process of the multicomponent xenobiotic efflux pump in Pseudomonas aeruginosa. Mol Microbiol 43: 677-686.
    • (2002) Mol Microbiol , vol.43 , pp. 677-686
    • Maseda, H.1    Kitao, M.2    Eda, S.3    Yoshihara, E.4    Nakae, T.5
  • 29
    • 0031021921 scopus 로고    scopus 로고
    • Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli
    • Miura, K., Tomioka, Y., Suzuki, H., Yonezawa, M., Hishinuma, T., and Mizugaki, M. (1997) Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli. Biol Pharm Bull 20: 110-112.
    • (1997) Biol Pharm Bull , vol.20 , pp. 110-112
    • Miura, K.1    Tomioka, Y.2    Suzuki, H.3    Yonezawa, M.4    Hishinuma, T.5    Mizugaki, M.6
  • 30
    • 0034089814 scopus 로고    scopus 로고
    • Survival of Pseudomonas putida KT2440 in soil and in the rhizosphere of plants under greenhouse and environmental conditions
    • Molina, L., Ramos, C., Duque, E., Ronchel, M.C., Garcia, J.M., Wyke, L., and Ramos, J.L. (2000) Survival of Pseudomonas putida KT2440 in soil and in the rhizosphere of plants under greenhouse and environmental conditions. Soil Biol Biochem 32: 315-321.
    • (2000) Soil Biol Biochem , vol.32 , pp. 315-321
    • Molina, L.1    Ramos, C.2    Duque, E.3    Ronchel, M.C.4    Garcia, J.M.5    Wyke, L.6    Ramos, J.L.7
  • 31
    • 0036933705 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440
    • Nelson, K.E., Weinel, C., Paulsen, I.T., Dodson, R.J., Hilbert, H. Martins dos Santos, V.A., et al. (2002) Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440. Env Microbiol 4: 799-808.
    • (2002) Env Microbiol , vol.4 , pp. 799-808
    • Nelson, K.E.1    Weinel, C.2    Paulsen, I.T.3    Dodson, R.J.4    Hilbert, H.5    Martins Dos Santos, V.A.6
  • 32
    • 0037206601 scopus 로고    scopus 로고
    • Identification and characterization of SnrA, an inducible oxygen-insensitive nitroreductase in Salmonella enterica serovar Typhimurium TA1535
    • Nokhbeh, M.R., Boroumandi, S., Pokorny, N., Koziarz, P., Paterson, E.S., and Lambert, I.B. (2002) Identification and characterization of SnrA, an inducible oxygen-insensitive nitroreductase in Salmonella enterica serovar Typhimurium TA1535. Mutant Res 508: 59-70.
    • (2002) Mutant Res , vol.508 , pp. 59-70
    • Nokhbeh, M.R.1    Boroumandi, S.2    Pokorny, N.3    Koziarz, P.4    Paterson, E.S.5    Lambert, I.B.6
  • 33
    • 0033754165 scopus 로고    scopus 로고
    • Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C
    • Pak, J.W., Knoke, K.L., Noguera, D.R., Fox, B.G., and Chambliss, G.H. (2000) Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C. Appl Environ Microbiol 66: 4742-4750.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4742-4750
    • Pak, J.W.1    Knoke, K.L.2    Noguera, D.R.3    Fox, B.G.4    Chambliss, G.H.5
  • 34
    • 0033966167 scopus 로고    scopus 로고
    • Identification and characterization of the nitrobenzene catabolic plasmid pNB1 and pNB2 in Pseuomonas putida HS12
    • Park, H.S., and Kim, H.S. (2000) Identification and characterization of the nitrobenzene catabolic plasmid pNB1 and pNB2 in Pseuomonas putida HS12. J Bacteriol 182: 573-580.
    • (2000) J Bacteriol , vol.182 , pp. 573-580
    • Park, H.S.1    Kim, H.S.2
  • 35
    • 4143114718 scopus 로고    scopus 로고
    • Differential gene expression of Chlamydomonas reinhardtii in response to 2,4,6- Trinitrotoluene (TNT) using microarray analysis
    • Patel, N., Cardoza, V., Christensen, E., Rekapalli, B., Ayalew, M., and Stewart, C.N., Jr (2004) Differential gene expression of Chlamydomonas reinhardtii in response to 2,4,6- trinitrotoluene (TNT) using microarray analysis. Plant Sci 167: 1109-1122.
    • (2004) Plant Sci , vol.167 , pp. 1109-1122
    • Patel, N.1    Cardoza, V.2    Christensen, E.3    Rekapalli, B.4    Ayalew, M.5    Stewart Jr., C.N.6
  • 36
    • 40549124911 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in the response to acidic pH and stomach transit
    • Reid, A.N., Pandey, R., Palyada, K., Naikare, H., and Stintzi, A. (2008) Identification of Campylobacter jejuni genes involved in the response to acidic pH and stomach transit. Appl Environ Microbiol 74: 1583-1597.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1583-1597
    • Reid, A.N.1    Pandey, R.2    Palyada, K.3    Naikare, H.4    Stintzi, A.5
  • 38
    • 0036205616 scopus 로고    scopus 로고
    • NAD(P)H:flavin mononucleotide oxidoreductase inactivation during 2,4,6- trinitrotoluene reduction
    • Riefler, R.G., and Smets, B.F. (2002) NAD(P)H:flavin mononucleotide oxidoreductase inactivation during 2,4,6- trinitrotoluene reduction. Appl Environ Microbiol 68: 1690-1696.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 1690-1696
    • Riefler, R.G.1    Smets, B.F.2
  • 39
    • 59649117138 scopus 로고    scopus 로고
    • Physiological responses of Pseudomonas putida to formaldehyde during detoxification
    • Roca, A. Rodríguez-Herva, J.J., Duque, E., and Ramos, J.L. (2008) Physiological responses of Pseudomonas putida to formaldehyde during detoxification. Microbial Biotechnol 1: 158-169.
    • (2008) Microbial Biotechnol , vol.1 , pp. 158-169
    • Roca, A.1    Rodríguez-Herva, J.J.2    Duque, E.3    Ramos, J.L.4
  • 40
    • 1942539970 scopus 로고    scopus 로고
    • Metabolic pathway engineering to enhance aerobic degradation of chlorinated ethenes and to reduce their toxicity by cloning a novel glutathione S-transferase, an evolved toluene o-monooxygease, and γ-glutamylcysteine synthetase
    • Rui, L., Kwon, Y.M., Reardon, K.F., and Wood, T.K. (2004) Metabolic pathway engineering to enhance aerobic degradation of chlorinated ethenes and to reduce their toxicity by cloning a novel glutathione S-transferase, an evolved toluene o-monooxygease, and γ-glutamylcysteine synthetase. Environ Microbiol 4: 491-500.
    • (2004) Environ Microbiol , vol.4 , pp. 491-500
    • Rui, L.1    Kwon, Y.M.2    Reardon, K.F.3    Wood, T.K.4
  • 41
    • 25844456936 scopus 로고    scopus 로고
    • Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli
    • Sakoh, M., Ito, K., and Akiyama, Y. (2005) Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli. J Biol Chem 280: 33305-33310.
    • (2005) J Biol Chem , vol.280 , pp. 33305-33310
    • Sakoh, M.1    Ito, K.2    Akiyama, Y.3
  • 42
    • 24344489015 scopus 로고    scopus 로고
    • Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene
    • Segura, A., Godoy, P., van Dillewijn, P., Hurtado, A., Arroyo, N., Santacruz, S., and Ramos, J.L. (2005) Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene. J Bacteriol 187: 5937-5945.
    • (2005) J Bacteriol , vol.187 , pp. 5937-5945
    • Segura, A.1    Godoy, P.2    Van Dillewijn, P.3    Hurtado, A.4    Arroyo, N.5    Santacruz, S.6    Ramos, J.L.7
  • 43
    • 34247562745 scopus 로고    scopus 로고
    • Expression and purification of HtpX-like small heat shock integral membrane protease of an unknown organism related to Methylobacillus flagellatus
    • Siddiqui, A.A., Jalah, R., and Sharma, Y.D. (2007) Expression and purification of HtpX-like small heat shock integral membrane protease of an unknown organism related to Methylobacillus flagellatus. J Biochem Biophys Methods 70: 539-546.
    • (2007) J Biochem Biophys Methods , vol.70 , pp. 539-546
    • Siddiqui, A.A.1    Jalah, R.2    Sharma, Y.D.3
  • 44
    • 34547117597 scopus 로고    scopus 로고
    • TNT biotransformation: When chemistry confronts mineralization
    • Smets, B.F., Yin, H., and Esteve-Nuñez, A. (2007) TNT biotransformation: when chemistry confronts mineralization. Appl Microbiol Biotechnol 76: 267-277.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 267-277
    • Smets, B.F.1    Yin, H.2    Esteve-Nuñez, A.3
  • 45
    • 0036937672 scopus 로고    scopus 로고
    • Pseudomonas putida: A cosmopolitan opportunist par excellence
    • Timmis, K.N. (2002) Pseudomonas putida: a cosmopolitan opportunist par excellence. Environ Microbiol 4: 779-781.
    • (2002) Environ Microbiol , vol.4 , pp. 779-781
    • Timmis, K.N.1
  • 46
    • 0036158688 scopus 로고    scopus 로고
    • The elusive roles of bacterial glutathione S-transferases: New lessons from genomes
    • Vuilleumier, S., and Pagni, M. (2002) The elusive roles of bacterial glutathione S-transferases: new lessons from genomes. Appl Microbiol Biotechnol 58: 138-146.
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 138-146
    • Vuilleumier, S.1    Pagni, M.2
  • 47
    • 2942563803 scopus 로고    scopus 로고
    • Biotransformation of explosives by the Old Yellow Enzyme family of flavoproteins
    • Williams, R.E., Rathbone, D.A., Scrutton, N.S., and Bruce, N.C. (2004) Biotransformation of explosives by the Old Yellow Enzyme family of flavoproteins. Appl Environ Microbiol 7: 3566-3574.
    • (2004) Appl Environ Microbiol , vol.7 , pp. 3566-3574
    • Williams, R.E.1    Rathbone, D.A.2    Scrutton, N.S.3    Bruce, N.C.4
  • 48
    • 0035987236 scopus 로고    scopus 로고
    • 'New uses for an old enzyme' - The Old Yellow Enzyme family of flavoenzymes
    • Williams, R.E., and Bruce, N.C. (2002) 'New uses for an old enzyme' - the Old Yellow Enzyme family of flavoenzymes. Microbiology 148: 1607-1614.
    • (2002) Microbiology , vol.148 , pp. 1607-1614
    • Williams, R.E.1    Bruce, N.C.2
  • 49
    • 38949213661 scopus 로고    scopus 로고
    • OYE Flavoprotein reductases initiate the condensation of TNT-derived intemediates to secondary diarylamines and nitrite
    • Wittich, R.-M., Haïdour, A., van Dillewijn, P., and Ramos, J.L. (2008) OYE Flavoprotein reductases initiate the condensation of TNT-derived intemediates to secondary diarylamines and nitrite. Environ Sci Technol 42: 734-739.
    • (2008) Environ Sci Technol , vol.42 , pp. 734-739
    • Wittich, R.-M.1    Haïdour, A.2    Van Dillewijn, P.3    Ramos, J.L.4
  • 51
    • 0028340512 scopus 로고
    • Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744
    • Zenno, S., Saigo, K., Kanoh, H., and Inouye, S. (1994) Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744. J Bacteriol 176: 3536-3543.
    • (1994) J Bacteriol , vol.176 , pp. 3536-3543
    • Zenno, S.1    Saigo, K.2    Kanoh, H.3    Inouye, S.4
  • 52
    • 0029770130 scopus 로고    scopus 로고
    • Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution
    • Zenno, S., Koike, H., Tanokura, M., and Saigo, K. (1996a) Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution. J Bacteriol 178: 4731-4733.
    • (1996) J Bacteriol , vol.178 , pp. 4731-4733
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4
  • 53
    • 0029745672 scopus 로고    scopus 로고
    • Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harvey flavin oxidoreductase
    • Zenno, S., Koike, H., Kumar, A., Jayaraman, R., Tanokura, M., and Saigo, K. (1996b) Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harvey flavin oxidoreductase. J Bacteriol 178: 4508-4514.
    • (1996) J Bacteriol , vol.178 , pp. 4508-4514
    • Zenno, S.1    Koike, H.2    Kumar, A.3    Jayaraman, R.4    Tanokura, M.5    Saigo, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.