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Volumn 34, Issue 2, 2004, Pages 302-310

Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis

Author keywords

Aerobic azoreductase; Azo dye; Enterococcus faecalis; Human intestinal microflora

Indexed keywords

AMARANTHUS CAUDATUS; ENTEROCOCCUS; ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI; POSIBACTERIA;

EID: 1642354143     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.12.016     Document Type: Article
Times cited : (161)

References (36)
  • 2
    • 0034921274 scopus 로고    scopus 로고
    • Basic and applied aspects in the microbial degradation of azo dyes
    • A. Stolz, Basic and applied aspects in the microbial degradation of azo dyes, Appl. Microbiol. Biotechnol. 56 (2001) 69-80.
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 69-80
    • Stolz, A.1
  • 3
    • 0015058826 scopus 로고
    • Mechanisms of azo reduction by Streptococcus faecalis. II. The role of soluble flavins
    • R. Gingell, R. Walker, Mechanisms of azo reduction by Streptococcus faecalis. II. The role of soluble flavins, Xenobiotica 1 (1971) 231-239.
    • (1971) Xenobiotica , vol.1 , pp. 231-239
    • Gingell, R.1    Walker, R.2
  • 4
    • 0034071030 scopus 로고    scopus 로고
    • The function of cytoplasmic flavin reductases in the reduction of azo dyes by bacteria
    • R. Russ, J. Rau, A. Stolz, The function of cytoplasmic flavin reductases in the reduction of azo dyes by bacteria, Appl. Environ. Microbiol. 66 (2000) 1429-1434.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1429-1434
    • Russ, R.1    Rau, J.2    Stolz, A.3
  • 5
    • 0021259033 scopus 로고
    • Comparison of two bacterial azoreductases acquired during adaptation to growth on azo dyes
    • T. Zimmermann, F. Gasser, H.G. Kulla, T. Leisinger, Comparison of two bacterial azoreductases acquired during adaptation to growth on azo dyes, Arch. Microbiol. 138 (1984) 37-43.
    • (1984) Arch. Microbiol. , vol.138 , pp. 37-43
    • Zimmermann, T.1    Gasser, F.2    Kulla, H.G.3    Leisinger, T.4
  • 6
    • 0020410057 scopus 로고
    • Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46
    • T. Zimmermann, H.G. Kulla, T. Leisinger, Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46, Eur. J. Biochem. 129 (1982) 197-203.
    • (1982) Eur. J. Biochem. , vol.129 , pp. 197-203
    • Zimmermann, T.1    Kulla, H.G.2    Leisinger, T.3
  • 7
    • 0035937804 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-1 isolated from soil
    • Y. Suzuki, T. Yoda, A. Ruhul, W. Sugiura, Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-1 isolated from soil, J. Biol. Chem. 276 (2001) 9059-9065.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9059-9065
    • Suzuki, Y.1    Yoda, T.2    Ruhul, A.3    Sugiura, W.4
  • 9
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • M. Nakanishi, C. Yatome, N. Ishida, Y. Kitade, Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase, J. Biol. Chem. 276 (2001) 46394-46399.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 10
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • S. Blumel, H.-J. Knackmuss, A. Stolz, Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F, Appl. Environ. Microbiol. 68 (2002) 3948-3955.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3948-3955
    • Blumel, S.1    Knackmuss, H.-J.2    Stolz, A.3
  • 11
    • 0043164772 scopus 로고    scopus 로고
    • Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24
    • S. Blumel, A. Stolz, Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24, Appl. Microbiol. Biotech. 62 (2003) 186-190.
    • (2003) Appl. Microbiol. Biotech. , vol.62 , pp. 186-190
    • Blumel, S.1    Stolz, A.2
  • 12
    • 0020418488 scopus 로고
    • Metabolism of benzidine and benzidine-congener based dyes by human, monkey and rat intestinal bacteria
    • C.E. Cerniglia, J.P. Freeman, W. Franklin, L.D. Pack, Metabolism of benzidine and benzidine-congener based dyes by human, monkey and rat intestinal bacteria, Biochem. Biophys. Res. Commun. 107 (1982) 1224-1229.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1224-1229
    • Cerniglia, C.E.1    Freeman, J.P.2    Franklin, W.3    Pack, L.D.4
  • 13
    • 0020441138 scopus 로고
    • Metabolism of azo dyes derived from benzidine, 3,3′-dimethyl- benzidine and 3,3′-dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria
    • C.E. Cerniglia, J.P. Freeman, W. Franklin, L.D. Pack, Metabolism of azo dyes derived from benzidine, 3,3′-dimethyl-benzidine and 3,3′-dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria, Carcinogenesis 3 (1982) 1255-1260.
    • (1982) Carcinogenesis , vol.3 , pp. 1255-1260
    • Cerniglia, C.E.1    Freeman, J.P.2    Franklin, W.3    Pack, L.D.4
  • 14
    • 0021867082 scopus 로고
    • Metabolism of the benzidine-based azo dye Direct Black 38 by human intestinal microbiota
    • B.W. Manning, C.E. Cerniglia, W.W. Federle, Metabolism of the benzidine-based azo dye Direct Black 38 by human intestinal microbiota, Appl. Environ. Microbiol. 50 (1985) 10-15.
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 10-15
    • Manning, B.W.1    Cerniglia, C.E.2    Federle, W.W.3
  • 15
    • 0022975291 scopus 로고
    • Mutagenic activation of the benzidine-based dye direct black 38 by human intestinal microflora
    • C.E. Cerniglia, Z. Zhou, B.W. Manning, T.W. Federle, R.H. Heflich, Mutagenic activation of the benzidine-based dye direct black 38 by human intestinal microflora, Mutat. Res. 175 (1986) 11-16.
    • (1986) Mutat. Res. , vol.175 , pp. 11-16
    • Cerniglia, C.E.1    Zhou, Z.2    Manning, B.W.3    Federle, T.W.4    Heflich, R.H.5
  • 16
    • 0032861116 scopus 로고    scopus 로고
    • Formation of a carcinogenic aromatic amine from an azo dye by human skin bacteria
    • T. Platzek, C. Lang, G. Grohmann, U.-S. Gi, W. Baltes, Formation of a carcinogenic aromatic amine from an azo dye by human skin bacteria, Hum. Exp.Toxicol. 18 (1999) 552-559.
    • (1999) Hum. Exp.Toxicol. , vol.18 , pp. 552-559
    • Platzek, T.1    Lang, C.2    Grohmann, G.3    Gi, U.-S.4    Baltes, W.5
  • 17
    • 0027304570 scopus 로고
    • The normal intestinal microflora: Ecology, variability and stability
    • R.J. Carman, R.L. Van Tassell, T.D. Wilkins, The normal intestinal microflora: ecology, variability and stability, Vet. Hum. Toxicol. 35 (Suppl. 1) (1993) 11-14.
    • (1993) Vet. Hum. Toxicol. , vol.35 , Issue.1 SUPPL. , pp. 11-14
    • Carman, R.J.1    Van Tassell, R.L.2    Wilkins, T.D.3
  • 18
    • 0032996673 scopus 로고    scopus 로고
    • Evaluation of veterinary drug residues in food for their potential to affect human intestinal microflora
    • C.E. Cerniglia, S. Kotarski, Evaluation of veterinary drug residues in food for their potential to affect human intestinal microflora, Regul. Toxicol. Pharmacol. 29 (1999) 238-261.
    • (1999) Regul. Toxicol. Pharmacol. , vol.29 , pp. 238-261
    • Cerniglia, C.E.1    Kotarski, S.2
  • 19
    • 0031422026 scopus 로고    scopus 로고
    • Classification and overview of the genera Streptococcus and Enterococcus
    • J.M. Hardie, R.A. Whiley, Classification and overview of the genera Streptococcus and Enterococcus, Soc. Appl. Bacteriol. Symp. Ser. 26 (1997) 1S-11S.
    • (1997) Soc. Appl. Bacteriol. Symp. Ser. , vol.26
    • Hardie, J.M.1    Whiley, R.A.2
  • 20
    • 0036940379 scopus 로고    scopus 로고
    • Isolation of Enterococcus species from infectious skin lesions
    • S. Higaki, M. Morohashi, T. Yamagishi, Isolation of Enterococcus species from infectious skin lesions, Drugs Exptl. Clin. Res. 28 (2002) 91-93.
    • (2002) Drugs Exptl. Clin. Res. , vol.28 , pp. 91-93
    • Higaki, S.1    Morohashi, M.2    Yamagishi, T.3
  • 21
    • 0028587626 scopus 로고
    • Urinary tract infection with an Enterococcus faecalis isolate that requires vancomycin for growth
    • H.S. Fraimow, D.L. Jungkind, D.W. Lander, D.R. Delso, J.L. Dean, Urinary tract infection with an Enterococcus faecalis isolate that requires vancomycin for growth, Ann. Intern. Med. 121 (1994) 22-26.
    • (1994) Ann. Intern. Med. , vol.121 , pp. 22-26
    • Fraimow, H.S.1    Jungkind, D.L.2    Lander, D.W.3    Delso, D.R.4    Dean, J.L.5
  • 22
    • 0035238260 scopus 로고    scopus 로고
    • Enterococci. Habitats, infections, virulence factors, resistances to antibiotics, transfer of resistance determinants
    • I. Klare, G. Werner, W. Witte, Enterococci. Habitats, infections, virulence factors, resistances to antibiotics, transfer of resistance determinants, Contrib. Microbiol. 8 (2001) 108-122.
    • (2001) Contrib. Microbiol. , vol.8 , pp. 108-122
    • Klare, I.1    Werner, G.2    Witte, W.3
  • 23
    • 0034058528 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococcal infections
    • B.E. Murray, Vancomycin-resistant enterococcal infections, N. Engl. J. Med. 342 (2000) 710-721.
    • (2000) N. Engl. J. Med. , vol.342 , pp. 710-721
    • Murray, B.E.1
  • 24
    • 0026755890 scopus 로고
    • Enterococcal endocarditis
    • D.W. Megran, Enterococcal endocarditis, Clin. Infect. Dis. 15 (1992) 63-71.
    • (1992) Clin. Infect. Dis. , vol.15 , pp. 63-71
    • Megran, D.W.1
  • 25
    • 0015061210 scopus 로고
    • Mechanisms of azo reduction by Streptococcus faecalis. I. Optimization of assay conditions
    • R. Walker, R. Gingell, D.F. Murrells, Mechanisms of azo reduction by Streptococcus faecalis. I. Optimization of assay conditions, Xenobiotica 1 (1971) 221-229.
    • (1971) Xenobiotica , vol.1 , pp. 221-229
    • Walker, R.1    Gingell, R.2    Murrells, D.F.3
  • 26
    • 0036812495 scopus 로고    scopus 로고
    • Development of a membrane-array method for the detection of human intestinal bacteria in fecal samples
    • R.F. Wang, S.-J. Kim, L.H. Robertson, C.E. Cerniglia, Development of a membrane-array method for the detection of human intestinal bacteria in fecal samples, Mol. Cell. Probes. 16 (2002) 341-350.
    • (2002) Mol. Cell. Probes. , vol.16 , pp. 341-350
    • Wang, R.F.1    Kim, S.-J.2    Robertson, L.H.3    Cerniglia, C.E.4
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 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 harveyi flavin oxidoreductase
    • S. Zenno, H. Koike, A.N. Kumar, R. Jayaraman, M. Tanokura, K. Saigo, Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase, J. Bacteriol. 178 (1996) 4508-4514.
    • (1996) J. Bacteriol. , vol.178 , pp. 4508-4514
    • Zenno, S.1    Koike, H.2    Kumar, A.N.3    Jayaraman, R.4    Tanokura, M.5    Saigo, K.6
  • 29
    • 0020042161 scopus 로고
    • A review of the genotoxicity of food drug and cosmatic colors and other azo, triphenylmethane and xanthene dyes
    • R.D. Combes, R.B. Haveland-Smith, A review of the genotoxicity of food drug and cosmatic colors and other azo, triphenylmethane and xanthene dyes, Mutat. Res. 98 (1982) 101-248.
    • (1982) Mutat. Res. , vol.98 , pp. 101-248
    • Combes, R.D.1    Haveland-Smith, R.B.2
  • 30
    • 0020566002 scopus 로고
    • The significance of azo-reduction in the mutagenesis and carcinogenesis of azo dyes
    • K.-T. Chung, The significance of azo-reduction in the mutagenesis and carcinogenesis of azo dyes, Mutat. Res. 114 (1983) 269-281.
    • (1983) Mutat. Res. , vol.114 , pp. 269-281
    • Chung, K.-T.1
  • 31
    • 0034525487 scopus 로고    scopus 로고
    • Culture-based knowledge on biodiversity, development and stability of human gastrointestinal microflora
    • B. Kleessen, E. Bezirtzoglou, J. Matto, Culture-based knowledge on biodiversity, development and stability of human gastrointestinal microflora, Microb. Ecol. Health Dis. 2 (2000) 53-63.
    • (2000) Microb. Ecol. Health Dis. , vol.2 , pp. 53-63
    • Kleessen, B.1    Bezirtzoglou, E.2    Matto, J.3
  • 33
    • 0029827889 scopus 로고    scopus 로고
    • Taxonomical changes in intestinal (faecal) enterococci and streptococci: Consequences on their use as indicators of faecal contamination in drinking water
    • H. Leclerc, M.T. Devriese, D.A.A. Mossel, Taxonomical changes in intestinal (faecal) enterococci and streptococci: consequences on their use as indicators of faecal contamination in drinking water, Appl. Bacteriol. 81 (1996) 459-466.
    • (1996) Appl. Bacteriol. , vol.81 , pp. 459-466
    • Leclerc, H.1    Devriese, M.T.2    Mossel, D.A.A.3
  • 34
    • 0023135722 scopus 로고
    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • A. Ben-Bassat, K. Bauer, S.Y. Chang, K. Myambo, A. Boosman, S. Chang, Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure, J. Bacteriol. 169 (1987) 751-757.
    • (1987) J. Bacteriol. , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 35
    • 0036451269 scopus 로고    scopus 로고
    • A flavoprotein encoded in Selenomonas ruminantium is characterized after expression in Escherichia coli
    • P.J. Anderson, L.J. Cole, D.B. Mckay, B. Entsch, A flavoprotein encoded in Selenomonas ruminantium is characterized after expression in Escherichia coli, Protein Expr. Purif. 24 (2002) 429-438.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 429-438
    • Anderson, P.J.1    Cole, L.J.2    Mckay, D.B.3    Entsch, B.4
  • 36
    • 0029808844 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri
    • S. Zenno, H. Koike, M. Tanokura, K. Saigo, Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, J. Biochem. 120 (1996) 736-744.
    • (1996) J. Biochem. , vol.120 , pp. 736-744
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4


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