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Volumn 11, Issue , 2009, Pages 59-66

Purification and identification of an FMN-dependent NAD(P)H azoreductase from Enterococcus faecalis

Author keywords

[No Author keywords available]

Indexed keywords

AZO REDUCTASE; METHYL RED; POLYACRYLAMIDE GEL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; FLAVINE MONONUCLEOTIDE;

EID: 54849415265     PISSN: 14673037     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (47)

References (24)
  • 1
    • 54849420486 scopus 로고    scopus 로고
    • Abraham KJ, J., G. (2007). Development of a Classification Scheme using a Secondary and Tertiary Amino Acid Analysis of Azoreductase Gene. Journal of Medical and Biological Sciences 1, 1-5.
    • Abraham KJ, J., G. (2007). Development of a Classification Scheme using a Secondary and Tertiary Amino Acid Analysis of Azoreductase Gene. Journal of Medical and Biological Sciences 1, 1-5.
  • 2
    • 33947203976 scopus 로고    scopus 로고
    • Decolorization of textile azo dyes by newly isolated halophilic and halotolerant bacteria
    • Asad, S., Amoozegar, M. A., Pourbabaee, A. A., Sarbolouki, M. N., and Dastgheib, S. M. (2007). Decolorization of textile azo dyes by newly isolated halophilic and halotolerant bacteria. Bioresour Technol 98, 2082-2088.
    • (2007) Bioresour Technol , vol.98 , pp. 2082-2088
    • Asad, S.1    Amoozegar, M.A.2    Pourbabaee, A.A.3    Sarbolouki, M.N.4    Dastgheib, S.M.5
  • 3
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • Blumel, S., Knackmuss, H. J., and Stolz, A. (2002). Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl Environ Microbiol 68, 3948-3955.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3948-3955
    • Blumel, S.1    Knackmuss, H.J.2    Stolz, A.3
  • 4
    • 0043164772 scopus 로고    scopus 로고
    • Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24
    • Blumel, S., and Stolz,A. (2003). Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl Microbiol Biotechnol 62, 186-190.
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 186-190
    • Blumel, S.1    Stolz, A.2
  • 5
    • 33646181980 scopus 로고    scopus 로고
    • Recent advances in azo dye degrading enzyme research
    • Chen, H. (2006). Recent advances in azo dye degrading enzyme research. Curr Protein Pept Sci 7, 101-111.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 101-111
    • Chen, H.1
  • 6
    • 19044389145 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein
    • Chen, H., Hopper, S. L., and Cerniglia, C. E. (2005). Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151, 1433-1441.
    • (2005) Microbiology , vol.151 , pp. 1433-1441
    • Chen, H.1    Hopper, S.L.2    Cerniglia, C.E.3
  • 7
    • 1642354143 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
    • Chen, H., Wang, R. F., and Cerniglia, C. E. (2004). Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Expr Purif 34, 302-310.
    • (2004) Protein Expr Purif , vol.34 , pp. 302-310
    • Chen, H.1    Wang, R.F.2    Cerniglia, C.E.3
  • 8
    • 0026529951 scopus 로고
    • The reduction of azo dyes by the intestinal microflora
    • Chung, K. T., Stevens, S. E., Jr., and Cerniglia, C. E. (1992). The reduction of azo dyes by the intestinal microflora. Crit Rev Microbiol 18, 175-190.
    • (1992) Crit Rev Microbiol , vol.18 , pp. 175-190
    • Chung, K.T.1    Stevens Jr., S.E.2    Cerniglia, C.E.3
  • 9
    • 0141955057 scopus 로고    scopus 로고
    • A method for reducing the time required to match protein sequences with tandem mass spectra
    • Craig, R., and Beavis, R. C. (2003). A method for reducing the time required to match protein sequences with tandem mass spectra. Rapid Commun Mass Spectrom 17, 2310-2316.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 2310-2316
    • Craig, R.1    Beavis, R.C.2
  • 10
    • 0034724218 scopus 로고    scopus 로고
    • Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: Species comparison and structural changes with substrate binding and release
    • Faig, M., Bianchet, M. A., Talalay, P., Chen, S., Winski, S., Ross, D., and Amzel, L. M. (2000). Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci U S A 97, 3177-3182.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3177-3182
    • Faig, M.1    Bianchet, M.A.2    Talalay, P.3    Chen, S.4    Winski, S.5    Ross, D.6    Amzel, L.M.7
  • 11
    • 0026457805 scopus 로고
    • Purification and partial characterization of two azoreductases from Shigella dysenteriae type 1
    • Ghosh, D. K., Mandal, A., and Chaudhuri, J. (1992). Purification and partial characterization of two azoreductases from Shigella dysenteriae type 1. FEMS Microbiol Lett 77, 229-233.
    • (1992) FEMS Microbiol Lett , vol.77 , pp. 229-233
    • Ghosh, D.K.1    Mandal, A.2    Chaudhuri, J.3
  • 12
    • 33746029411 scopus 로고    scopus 로고
    • Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms
    • Ito, K., Nakanishi, M., Lee, W. C., Sasaki, H., Zenno, S., Saigo, K., Kitade, Y, and Tanokura, M. (2006). Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms. J Biol Chem 281, 20567-20576.
    • (2006) J Biol Chem , vol.281 , pp. 20567-20576
    • Ito, K.1    Nakanishi, M.2    Lee, W.C.3    Sasaki, H.4    Zenno, S.5    Saigo, K.6    Kitade, Y.7    Tanokura, M.8
  • 13
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002). Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74, 5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P) H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li, R., Bianchet, M. A., Talalay, P., and Amzel, L. M. (1995). The three-dimensional structure of NAD(P) H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci U S A 92, 8846-8850.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 17
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi, M., Yatome, C., Ishida, N., and Kitade, Y. (2001). Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem 276, 46394-46399.
    • (2001) J Biol Chem , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 18
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., olker E., and Aebersold, R. (2003). A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75, 4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    olker, E.3    Aebersold, R.4
  • 19
    • 53149098243 scopus 로고    scopus 로고
    • Punj, S., and John, G. H. (2008). Physiological Characterization of Azo Dye Reduction in Enterococcus faecalis. Microbial Ecology in Health and Disease. iFirst, 1-9. DOI: 10.1080/08910600802169630
    • Punj, S., and John, G. H. (2008). Physiological Characterization of Azo Dye Reduction in Enterococcus faecalis. Microbial Ecology in Health and Disease. iFirst, 1-9. DOI: 10.1080/08910600802169630
  • 20
    • 0026654586 scopus 로고
    • Azoreductase activity by purified rabbit liver aldehyde oxidase
    • Stoddart, A. M., and Levine, W. G. (1992). Azoreductase activity by purified rabbit liver aldehyde oxidase. Biochem Pharmacol 43, 2227-2235.
    • (1992) Biochem Pharmacol , vol.43 , pp. 2227-2235
    • Stoddart, A.M.1    Levine, W.G.2
  • 21
    • 0034921274 scopus 로고    scopus 로고
    • Basic and applied aspects in the microbial degradation of azo dyes
    • Stolz, A. (2001). Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56, 69-80.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 69-80
    • Stolz, A.1
  • 22
    • 0015061210 scopus 로고
    • Mechanisms of azo reduction by Streptococcus faecalis. I. Optimization of assay conditions
    • Walker, R., Gingell, R., and Murrells, D. F. (1971). Mechanisms of azo reduction by Streptococcus faecalis. I. Optimization of assay conditions. Xenobiotica 1, 221-229.
    • (1971) Xenobiotica , vol.1 , pp. 221-229
    • Walker, R.1    Gingell, R.2    Murrells, D.F.3
  • 23
    • 35148864753 scopus 로고    scopus 로고
    • Molecular cloning, characterisation and ligandbound structure of an azoreductase from Pseudomonas aeruginosa
    • Wang, C. J., Hagemeier, C., Rahman, N., Lowe, E., Noble, M., Coughtrie, M., Sim, E., and Westwood, I. (2007). Molecular cloning, characterisation and ligandbound structure of an azoreductase from Pseudomonas aeruginosa. J Mol Biol 373, 1213-1228.
    • (2007) J Mol Biol , vol.373 , pp. 1213-1228
    • Wang, C.J.1    Hagemeier, C.2    Rahman, N.3    Lowe, E.4    Noble, M.5    Coughtrie, M.6    Sim, E.7    Westwood, I.8
  • 24
    • 0025686034 scopus 로고
    • Characteristics of two classes of azo dye reductase activity associated with rat liver microsomal cytochrome P450
    • Zbaida, S., and Levine, W. G. (1990). Characteristics of two classes of azo dye reductase activity associated with rat liver microsomal cytochrome P450. Biochem Pharmacol 40, 2415-2423.
    • (1990) Biochem Pharmacol , vol.40 , pp. 2415-2423
    • Zbaida, S.1    Levine, W.G.2


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