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Volumn 82, Issue 3, 2000, Pages 211-219

Nucleotide sequence analysis, overexpression in Escherichia coli and kinetic characterization of Anacystis nidulans catalase-peroxidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CATALASE; CYANIDE; PEROXIDASE; RECOMBINANT PROTEIN;

EID: 0034115126     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)00204-2     Document Type: Article
Times cited : (20)

References (20)
  • 1
    • 0018367454 scopus 로고
    • Purification of the o-dianisidine peroxidase from Escherichia coli B
    • Clairborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. J. Biol. Chem. 245:1979;4245-4252.
    • (1979) J. Biol. Chem. , vol.245 , pp. 4245-4252
    • Clairborne, A.1    Fridovich, I.2
  • 2
    • 0029996846 scopus 로고    scopus 로고
    • The catalase-peroxidase of Synechococcus PCC 7942: Purification, nucleotide sequence analysis and expression in Escherichia coli
    • Mutsuda M., Ishikawa T., Takeda T., Shigeoka S. The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli. Biochem. J. 316:1996;251-257.
    • (1996) Biochem. J. , vol.316 , pp. 251-257
    • Mutsuda, M.1    Ishikawa, T.2    Takeda, T.3    Shigeoka, S.4
  • 3
    • 0031587989 scopus 로고    scopus 로고
    • Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans
    • Obinger C., Regelsberger G., Strasser G., Burner U., Peschek G.A. Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans. Biochem. Biophys. Res. Commun. 235:1997;545-552.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 545-552
    • Obinger, C.1    Regelsberger, G.2    Strasser, G.3    Burner, U.4    Peschek, G.A.5
  • 4
    • 0032923152 scopus 로고    scopus 로고
    • Purification and characterization of a hydroperoxidase from the cyanobacterium Synechocystis PCC 6803: Identification of its gene by peptide mass mapping using matrix assisted laser desorption ionization time-of-flight mass spectrometry
    • Regelsberger G., Obinger C., Zoder R., Altmann F., Peschek G.A. Purification and characterization of a hydroperoxidase from the cyanobacterium Synechocystis PCC 6803: identification of its gene by peptide mass mapping using matrix assisted laser desorption ionization time-of-flight mass spectrometry. FEMS Microbiol. Lett. 170:1999;1-12.
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 1-12
    • Regelsberger, G.1    Obinger, C.2    Zoder, R.3    Altmann, F.4    Peschek, G.A.5
  • 6
    • 0033543171 scopus 로고    scopus 로고
    • Spectral and kinetic studies of the oxidation of monosubstituted phenols and anilines by recombinant Synechocystis catalase-peroxidase compound I
    • Regelsberger G., Jakopitsch C., Engleder M., Rüker F., Peschek G.A., Obinger C. Spectral and kinetic studies of the oxidation of monosubstituted phenols and anilines by recombinant Synechocystis catalase-peroxidase compound I. Biochemistry. 38:1999;10480-10488.
    • (1999) Biochemistry , vol.38 , pp. 10480-10488
    • Regelsberger, G.1    Jakopitsch, C.2    Engleder, M.3    Rüker, F.4    Peschek, G.A.5    Obinger, C.6
  • 7
    • 0345426301 scopus 로고    scopus 로고
    • Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: Cloning, overexpression in Escherichia coli, and kinetic characterization
    • Jakopitsch C., Rüker F., Regelsberger G., Dockal M., Peschek G.A., Obinger C. Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization. J. Biol. Chem. 380:1999;1087-1096.
    • (1999) J. Biol. Chem. , vol.380 , pp. 1087-1096
    • Jakopitsch, C.1    Rüker, F.2    Regelsberger, G.3    Dockal, M.4    Peschek, G.A.5    Obinger, C.6
  • 8
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2:1992;388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 9
    • 0025995263 scopus 로고
    • Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
    • Welinder K.G. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta. 1080:1991;215-220.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 215-220
    • Welinder, K.G.1
  • 10
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1. 7-Å resolution
    • Finzel B.C., Poulos T.L., Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1. 7-Å resolution. J. Biol. Chem. 259:1984;13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 11
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson W.R., Poulos T.L. Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry. 34:1995;4331-4341.
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 12
    • 0000854931 scopus 로고
    • Characterization of cytochrome-c oxidase in isolated and purified plasma and thylakoid membranes from cyanobacteria
    • Peschek G.A., Molitor V., Trnka M., Wastyn M., Erber W. Characterization of cytochrome-c oxidase in isolated and purified plasma and thylakoid membranes from cyanobacteria. Methods Enzymol. 167:1988;437-449.
    • (1988) Methods Enzymol. , vol.167 , pp. 437-449
    • Peschek, G.A.1    Molitor, V.2    Trnka, M.3    Wastyn, M.4    Erber, W.5
  • 13
    • 0011140369 scopus 로고
    • Molecular cloning: A laboratory manual
    • Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory Press
    • Sambrook R., Fritsch E., Maniatis T. Molecular cloning: a laboratory manual. 2nd edn :1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1989) 2nd Edn
    • Sambrook, R.1    Fritsch, E.2    Maniatis, T.3
  • 14
    • 0024338720 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA)
    • Loprasert S., Negoro S., Okada H. Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA). J. Bacteriol. 171:1989;4871-4875.
    • (1989) J. Bacteriol. , vol.171 , pp. 4871-4875
    • Loprasert, S.1    Negoro, S.2    Okada, H.3
  • 16
    • 0027248433 scopus 로고
    • Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis
    • Heym B., Zhang Y., Poulet S., Young D., Cole S.T. Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J. Bacteriol. 175:1993;4255-4259.
    • (1993) J. Bacteriol. , vol.175 , pp. 4255-4259
    • Heym, B.1    Zhang, Y.2    Poulet, S.3    Young, D.4    Cole, S.T.5
  • 17
    • 0023106193 scopus 로고
    • Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I
    • Fishel L.A., Villafranca J.E., Mauro J.M., Kraut J. Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I. Biochemistry. 26:1987;351-360.
    • (1987) Biochemistry , vol.26 , pp. 351-360
    • Fishel, L.A.1    Villafranca, J.E.2    Mauro, J.M.3    Kraut, J.4
  • 18
    • 0021164456 scopus 로고
    • Genetic relationships among cyanobacterial strains originally designated as 'Anacystis nidulans' and some other Synechococcus strains
    • Wilmotte A.M.R., Stam W.T. Genetic relationships among cyanobacterial strains originally designated as 'Anacystis nidulans' and some other Synechococcus strains. J. Gen. Microbiol. 130:1984;2737-2740.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2737-2740
    • Wilmotte, A.M.R.1    Stam, W.T.2
  • 19
    • 0031907590 scopus 로고    scopus 로고
    • Mechanisms involved in the intrinsic isoniazid resistance of Mycobacterium avium
    • Mdluli K., Swanson J., Fischer E., Lee R.E., Barry C.E. Mechanisms involved in the intrinsic isoniazid resistance of Mycobacterium avium. Mol. Microbiol. 27:1998;1223-1233.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1223-1233
    • Mdluli, K.1    Swanson, J.2    Fischer, E.3    Lee, R.E.4    Barry, C.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.