메뉴 건너뛰기




Volumn 178, Issue 15, 1996, Pages 4508-4514

Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase

Author keywords

[No Author keywords available]

Indexed keywords

NITROREDUCTASE; OXIDOREDUCTASE; QUERCETIN;

EID: 0029745672     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4508-4514.1996     Document Type: Article
Times cited : (170)

References (31)
  • 1
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 8
    • Bachmann, B. J. 1990. Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev. 54:130-197.
    • (1990) Microbiol. Rev. , vol.54 , pp. 130-197
    • Bachmann, B.J.1
  • 2
    • 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
  • 3
    • 0016631494 scopus 로고
    • Cross-linking of the components of lactose synthetase with dimethylpimelimidate
    • Brew, K., J. H. Shaper, K. W. Olsen, I. P. Trayer, and R. L. Hill. 1975. Cross-linking of the components of lactose synthetase with dimethylpimelimidate. J. Biol. Chem. 250:1434-1444.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1434-1444
    • Brew, K.1    Shaper, J.H.2    Olsen, K.W.3    Trayer, I.P.4    Hill, R.L.5
  • 4
    • 0025892415 scopus 로고
    • Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae
    • Bryant, C., and M. DeLuca. 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
  • 6
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1978. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:25-76.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 25-76
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung, C. T., S. L. Niemela, and R. H. Miller. 1989. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA 86:2172-2175.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 8
    • 0013877705 scopus 로고
    • The aerobic degradation of l-(5-nitrofurrylideneamino)-2-imidazolidinone (NF246) by Escherichia coli
    • Gavin, J. J., F. F. Ebetino, R. Frcedman, and W. E. Waterbury. 1966. The aerobic degradation of l-(5-nitrofurrylideneamino)-2-imidazolidinone (NF246) by Escherichia coli. Arch. Biochem. Biophys. 113:399-404.
    • (1966) Arch. Biochem. Biophys. , vol.113 , pp. 399-404
    • Gavin, J.J.1    Ebetino, F.F.2    Frcedman, R.3    Waterbury, W.E.4
  • 10
  • 11
    • 0017670155 scopus 로고
    • Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi
    • Jablonski, E. and M. DeLuca. 1977. Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry 16:2932-2936.
    • (1977) Biochemistry , vol.16 , pp. 2932-2936
    • Jablonski, E.1    DeLuca, M.2
  • 12
    • 0017813386 scopus 로고
    • Studies of the control of luminescence in Beneckea harveyi: Properties of the NADH and NADPH:FMN oxidoreductases
    • Jablonski, E., and M. DeLuca. 1978. Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry 17:672-678.
    • (1978) Biochemistry , vol.17 , pp. 672-678
    • Jablonski, E.1    DeLuca, M.2
  • 13
    • 0024674214 scopus 로고
    • Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12
    • Rang, W.-K., T. Icho, S. Isono, M. Kitakawa, and K. Isono. 1989. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol. Gen. Genet. 217:281-288.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 281-288
    • Rang, W.-K.1    Icho, T.2    Isono, S.3    Kitakawa, M.4    Isono, K.5
  • 14
    • 0023669069 scopus 로고
    • The physical map of whole. Mli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., K. Akiyama. and K. Isono. 1987. The physical map of whole. mli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 15
    • 0026337725 scopus 로고
    • Molecular cloning, characterization and expression of a nitrofuran reductase gene of Escherichia coli. 3
    • Kumar, A. N., and R. Jayaraman. 1991. Molecular cloning, characterization and expression of a nitrofuran reductase gene of Escherichia coli. 3. Biosci. 16:145-159.
    • (1991) Biosci. , vol.16 , pp. 145-159
    • Kumar, A.N.1    Jayaraman, R.2
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assemhly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assemhly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0028180756 scopus 로고
    • Vibrio harveyi NADPH-flavin oxidoreductase: Cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme
    • Lei, B., M. Liu, S. Huang, and S.-C. Tu. 1994. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. J. Bacteriol. 176: 3552-3558.
    • (1994) J. Bacteriol. , vol.176 , pp. 3552-3558
    • Lei, B.1    Liu, M.2    Huang, S.3    Tu, S.-C.4
  • 19
    • 0017877955 scopus 로고
    • Genetics of nitrofurazone resistance in Escherichia coli. 3
    • McCalla, D. R., C. Kaiser, and M. H. L. Green. 1978. Genetics of nitrofurazone resistance in Escherichia coli. 3. Bacteriol. 133:10-16.
    • (1978) Bacteriol. , vol.133 , pp. 10-16
    • McCalla, D.R.1    Kaiser, C.2    Green, M.H.L.3
  • 20
    • 0020362615 scopus 로고
    • A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments
    • Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269-276.
    • (1982) Gene , vol.19 , pp. 269-276
    • Messing, J.1    Vieira, J.2
  • 22
    • 0018800960 scopus 로고
    • Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes
    • Peterson, F. J., R. P. Mason, J. Hovsepian, and J. L. Holtzruan. 1979. Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes. J. Biol. Chem. 254:4009-4014.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4009-4014
    • Peterson, F.J.1    Mason, R.P.2    Hovsepian, J.3    Holtzruan, J.L.4
  • 23
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg, M., and D. Court. 1979. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet. 13: 319-353.
    • (1979) Annu. Rev. Genet. , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 25
    • 0000228203 scopus 로고
    • Matrices for detecting distant relationships
    • M. O. Dayhoff (ed.), National Biochemical Research Foundation, Washington, D.C
    • Schwartz, R. M., and M. O. Dayhoff. 1978. Matrices for detecting distant relationships, p. 353-358. In M. O. Dayhoff (ed.), Atlas of protein sequence and structure, vol. 5, suppl. 3. National Biochemical Research Foundation, Washington, D.C
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.3 SUPPL. , pp. 353-358
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 26
    • 0016154301 scopus 로고
    • The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and L. Dalgarno. 1974. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 27
    • 0027469780 scopus 로고
    • Cloning of the DNA polymerase gene of Bacillus caldotenax and characterization of the gene product
    • Uemori, T., Y. Ishinn, K. Fujita, K. Asada, and I. Kalo. 1993. Cloning of the DNA polymerase gene of Bacillus caldotenax and characterization of the gene product. J. Biochem. 113:401-410.
    • (1993) J. Biochem. , vol.113 , pp. 401-410
    • Uemori, T.1    Ishinn, Y.2    Fujita, K.3    Asada, K.4    Kalo, I.5
  • 28
    • 0029770130 scopus 로고    scopus 로고
    • Conversion of NfsB, a minor Escherichia coli nitrorcductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischen, by a single amino acid substitution
    • Zenno, S., H. Koike, M. Tanokura, and K. Saigo. 1996. Conversion of NfsB, a minor Escherichia coli nitrorcductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischen, 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
  • 29
    • 85035162804 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 fischen
    • in press
    • Zenno, S., H. Koike, M. Tanokura, and 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 fischen. J. Biochem., in press.
    • J. Biochem.
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4
  • 30
    • 0028206223 scopus 로고
    • Identification of the genes encoding NAD(P)H-flavin oxidoreductases that are similar in sequence to Escherichia coli Fre in four species of luminous bacteria: Photorhabdus luminescent, Vibrio fischen. Vibrio harveyi, and Vibrio orientalis
    • Zenno, S., and K. Saigo. 1994. Identification of the genes encoding NAD(P)H-flavin oxidoreductases that are similar in sequence to Escherichia coli Fre in four species of luminous bacteria: Photorhabdus luminescent, Vibrio fischen. Vibrio harveyi, and Vibrio orientalis. J. Bacteriol. 176:3544-3551.
    • (1994) J. Bacteriol. , vol.176 , pp. 3544-3551
    • Zenno, S.1    Saigo, K.2
  • 31
    • 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., K. Saigo, H. Kanoh, and S. Inouye. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.