메뉴 건너뛰기




Volumn 380, Issue 9, 1999, Pages 1087-1096

Catalase-peroxidase from the cyanobacterium synechocystis PCC 6803: Cloning, overexpression in Escherichia coli, and kinetic characterization

Author keywords

Compound I; Compound II; KatG; Transient state kinetics

Indexed keywords

ASCORBIC ACID; CYTOCHROME C; DIANISIDINE; GLUTATHIONE; GUAIACOL; HEMIN; METAL CHELATE; PEROXIDASE; PYROGALLOL; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0345426301     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.135     Document Type: Article
Times cited : (42)

References (45)
  • 1
    • 0023653379 scopus 로고
    • Astopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides
    • Balny, C., Anni, H., and Yonetani, T. (1987). Astopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides. FEBS Lett. 221, 349-354.
    • (1987) FEBS Lett. , vol.221 , pp. 349-354
    • Balny, C.1    Anni, H.2    Yonetani, T.3
  • 2
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R.F., and Sizer, I.W. (1952). A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-137.
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-137
    • Beers, R.F.1    Sizer, I.W.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micro quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976). A rapid and sensitive method for the quantitation of micro 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.1
  • 4
    • 0018367454 scopus 로고
    • Purification of the o-dianisidine peroxidase from Escherichia coli B
    • Claiborne, A., and Fridovich, I. (1979). Purification of the o-dianisidine peroxidase from Escherichia coli B. J. Biol. Chem. 254, 4245-4252.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4245-4252
    • Claiborne, A.1    Fridovich, I.2
  • 5
    • 0014819568 scopus 로고
    • Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role
    • Deisseroth, A., and Dounce, A.L. (1970). Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role. Physiological Reviews 50, 319-375.
    • (1970) Physiological Reviews , vol.50 , pp. 319-375
    • Deisseroth, A.1    Dounce, A.L.2
  • 6
    • 0016750834 scopus 로고
    • The purification and properties of peroxidase in Mycobacterium tuberculosis H37Rv and its possible role in the mechanism of action of isonicotinic acid hydrazide
    • Devi, B.G., Shaila, M.S., Ramakrishnan, T., and Gopinathan, K.P. (1975). The purification and properties of peroxidase in Mycobacterium tuberculosis H37Rv and its possible role in the mechanism of action of isonicotinic acid hydrazide. Biochem. J. 149, 187-197.
    • (1975) Biochem. J. , vol.149 , pp. 187-197
    • Devi, B.G.1    Shaila, M.S.2    Ramakrishnan, T.3    Gopinathan, K.P.4
  • 7
    • 0016251335 scopus 로고
    • Isolation and characterization of catalase produced by Mycobacterium tuberculosis
    • Diaz, G.A., and Wayne, L.G. (1974). Isolation and characterization of catalase produced by Mycobacterium tuberculosis. Am. Rev. Respir. Dis. 110, 312-319.
    • (1974) Am. Rev. Respir. Dis. , vol.110 , pp. 312-319
    • Diaz, G.A.1    Wayne, L.G.2
  • 8
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • J. Everse, K.E. Everse and M.B. Grisham, eds. (Boca Raton, Florida, USA: CRC Press)
    • Dunford, H.B. (1991). Horseradish peroxidase: structure and kinetic properties. In: Peroxidases in chemistry and biology, J. Everse, K.E. Everse and M.B. Grisham, eds. (Boca Raton, Florida, USA: CRC Press) pp. 2-24.
    • (1991) Peroxidases in Chemistry and Biology , pp. 2-24
    • Dunford, H.B.1
  • 9
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution
    • Finzel, B.C., Poulos, T.L., and Kraut, J. (1984). Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. J. Biol. Chem. 259, 13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 10
    • 0027215430 scopus 로고
    • Molecular cloning, sequence analysis and expression of the gene for catalase-peroxidase (cpeA) from the photosynthetic bacterium Rhodobacter capsulatus B10
    • Forkl, H., Vandekerckhove, J., Drews, G., and Tadros, M.H. (1993). Molecular cloning, sequence analysis and expression of the gene for catalase-peroxidase (cpeA) from the photosynthetic bacterium Rhodobacter capsulatus B10. Eur. J. Biochem. 214, 251-258.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 251-258
    • Forkl, H.1    Vandekerckhove, J.2    Drews, G.3    Tadros, M.H.4
  • 11
    • 0022341246 scopus 로고
    • Purification and properties of a peroxidase from Halobacterium halobium L-33
    • Fukumori, Y., Fujiwara, T., Okada-Takahashi, Y., Mukohata, Y., and Yamanaka, T. (1985). Purification and properties of a peroxidase from Halobacterium halobium L-33. J. Biochem. 98, 1055-1061.
    • (1985) J. Biochem. , vol.98 , pp. 1055-1061
    • Fukumori, Y.1    Fujiwara, T.2    Okada-Takahashi, Y.3    Mukohata, Y.4    Yamanaka, T.5
  • 12
    • 0015976238 scopus 로고
    • Visualization of catalase on acrylamide gels
    • Gregory, E.M., and Fridovich, I. (1974). Visualization of catalase on acrylamide gels. Anal. Biochem. 58, 57-62.
    • (1974) Anal. Biochem. , vol.58 , pp. 57-62
    • Gregory, E.M.1    Fridovich, I.2
  • 13
    • 85052778791 scopus 로고
    • Glutathione peroxidase
    • R.A. Greenwald, ed. (Boca Raton, Florida, USA: CRC Press)
    • Günzler, W.A., and Flohé, L. (1985). Glutathione peroxidase. In: CRC Handbook of Methods for Oxygen Radical Research, R.A. Greenwald, ed. (Boca Raton, Florida, USA: CRC Press), pp. 285-290.
    • (1985) CRC Handbook of Methods for Oxygen Radical Research , pp. 285-290
    • Günzler, W.A.1    Flohé, L.2
  • 14
    • 0000510324 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • R. Eisenthal and M.J. Danson, eds. (Oxford, UK: IRL Press)
    • Henderson, P.J.F. (1992). Statistical analysis of enzyme kinetic data. In: Enzyme Assays - A Practical Approach, R. Eisenthal and M.J. Danson, eds. (Oxford, UK: IRL Press) pp. 277-316.
    • (1992) Enzyme Assays - A Practical Approach , pp. 277-316
    • Henderson, P.J.F.1
  • 15
    • 0023654802 scopus 로고
    • Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata
    • Hochman, A., and Shemesh, A. (1987). Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata. J. Biol. Chem. 262, 6871-6876.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6871-6876
    • Hochman, A.1    Shemesh, A.2
  • 16
    • 0025780541 scopus 로고
    • Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae
    • Hochman, A., and Goldberg, I. (1991). Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae. Biochim. Biophys. Acta 1077, 299-307.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 299-307
    • Hochman, A.1    Goldberg, I.2
  • 17
    • 0008130352 scopus 로고
    • The diversity of bacterial hydroperoxidases
    • K.G. Welinder, S.K. Rasmussen, C. Penel and H. Greppin, eds. (Geneva, Switzerland: University of Geneva Press)
    • Hochman, A. (1993). The diversity of bacterial hydroperoxidases. In: Plant Peroxidases: Biochemistry and Physiology, K.G. Welinder, S.K. Rasmussen, C. Penel and H. Greppin, eds. (Geneva, Switzerland: University of Geneva Press), pp. 102-112.
    • (1993) Plant Peroxidases: Biochemistry and Physiology , pp. 102-112
    • Hochman, A.1
  • 19
    • 0344677635 scopus 로고
    • Heme-containing oxygen carriers
    • S. Otsuka and T. Yamanaka, eds. (Amsterdam, NL: Elsevier Science Publishers)
    • Imai, K. (1988). Heme-containing oxygen carriers. In: Metalloproteins: Chemical Properties and Biological Effects, S. Otsuka and T. Yamanaka, eds. (Amsterdam, NL: Elsevier Science Publishers), pp. 115-126.
    • (1988) Metalloproteins: Chemical Properties and Biological Effects , pp. 115-126
    • Imai, K.1
  • 20
    • 0031029149 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the catalase-peroxidase katG from Mycobacterium tuberculosis
    • Johnsson, K., Froland, W.A., and Schultz, P.G. (1997). Overexpression, purification, and characterization of the catalase-peroxidase katG from Mycobacterium tuberculosis. J. Biol. Chem. 272, 2834-2840.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2834-2840
    • Johnsson, K.1    Froland, W.A.2    Schultz, P.G.3
  • 22
    • 0031194670 scopus 로고    scopus 로고
    • Single-chain Fv fusion proteins suitable as coating and detecting reagents in a double antibody sandwich enzyme-linked immunosorbent assay
    • Kerschbaumer, R.J., Hirschl, S., Kaufmann, A., Ibl, M., Koenig, R., and Himmler, G. (1997). Single-chain Fv fusion proteins suitable as coating and detecting reagents in a double antibody sandwich enzyme-linked immunosorbent assay. Anal. Biochem. 249, 219-227.
    • (1997) Anal. Biochem. , vol.249 , pp. 219-227
    • Kerschbaumer, R.J.1    Hirschl, S.2    Kaufmann, A.3    Ibl, M.4    Koenig, R.5    Himmler, G.6
  • 23
    • 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
  • 24
    • 0023758686 scopus 로고
    • Thermostable peroxidase from Bacillus stearothermophilus
    • Loprasert, S., Negoro, S., and Okada, H. (1988). Thermostable peroxidase from Bacillus stearothermophilus. J. Gen. Microbiol. 134, 1971-1976.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1971-1976
    • Loprasert, S.1    Negoro, S.2    Okada, H.3
  • 25
    • 0024338720 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of the the Bacillus stearothermophilus peroxidase gene (perA)
    • Loprasert, S., Negoro, S., and Okada, H. (1989). Cloning, nucleotide sequence, and expression in Escherichia coli of the the Bacillus stearothermophilus peroxidase gene (perA). J. Bacteriol. 171, 4871-4875.
    • (1989) J. Bacteriol. , vol.171 , pp. 4871-4875
    • Loprasert, S.1    Negoro, S.2    Okada, H.3
  • 26
    • 0029153735 scopus 로고
    • Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation
    • Marcinkeviciene, J.A., Magliozzo, R.S., and Blanchard, J.S. (1995). Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation. J. Biol. Chem. 270, 22290-22295.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22290-22295
    • Marcinkeviciene, J.A.1    Magliozzo, R.S.2    Blanchard, J.S.3
  • 27
    • 0030200341 scopus 로고    scopus 로고
    • Kinetic ans spectral properties of pea cytosolic ascorbate peroxidase
    • Marquez, L.A., Quitoriano, M., Zilinskas, B.A., and Dunford, H.B. (1996). Kinetic ans spectral properties of pea cytosolic ascorbate peroxidase. FEBS Lett. 389, 153-156.
    • (1996) FEBS Lett. , vol.389 , pp. 153-156
    • Marquez, L.A.1    Quitoriano, M.2    Zilinskas, B.A.3    Dunford, H.B.4
  • 28
    • 0001073890 scopus 로고
    • Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts
    • Miyake, C., Cao, W.-H., and Asada, K. (1993). Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol. 34, 881-889.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 881-889
    • Miyake, C.1    Cao, W.-H.2    Asada, K.3
  • 29
    • 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., and Shigeoka, S. (1996). The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli. Biochem. J. 316, 251-257.
    • (1996) Biochem. J. , vol.316 , pp. 251-257
    • Mutsuda, M.1    Ishikawa, T.2    Takeda, T.3    Shigeoka, S.4
  • 31
    • 0031467299 scopus 로고    scopus 로고
    • Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis
    • Nagy, J.M., Cass, A.E.G., and Brown, K.A. (1997). Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis. J. Biol. Chem. 272, 31265-31271.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31265-31271
    • Nagy, J.M.1    Cass, A.E.G.2    Brown, K.A.3
  • 32
    • 77957183372 scopus 로고
    • Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical
    • Nakano, Y., and Asada, K. (1987). Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical. Plant Cell Physiol. 28, 131-140.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 34
    • 0001408791 scopus 로고
    • Catalases
    • P.D. Boyer and H. Lardy, eds. (San Diego, USA: Academic Press)
    • Nicholls, P., and Schonbaum, G.R. (1963). Catalases. In: The Enzymes, P.D. Boyer and H. Lardy, eds. (San Diego, USA: Academic Press) pp. 147-225.
    • (1963) The Enzymes , pp. 147-225
    • Nicholls, P.1    Schonbaum, G.R.2
  • 35
    • 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., and Peschek, G.A. (1997). Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans. Biochem. Biophys. Res. Commun. 235, 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
  • 36
    • 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. (1999). 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, 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
  • 37
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson, W.R., and Poulos, T.L. (1995). Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34, 4331-4341.
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 39
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue-green algae (order Chroococcales)
    • Stanier, R.Y., Kunisawa, R., Mandel, M., and Cohen-Bazire, G. (1971). Purification and properties of unicellular blue-green algae (order Chroococcales). Bacteriol. Rev. 35, 171-205.
    • (1971) Bacteriol. Rev. , vol.35 , pp. 171-205
    • Stanier, R.Y.1    Kunisawa, R.2    Mandel, M.3    Cohen-Bazire, G.4
  • 40
    • 0025255092 scopus 로고
    • Buffers: Principles and practice
    • Stoll, V.S., and Blanchard, J.S. (1990). Buffers: principles and practice. Methods Enzymol. 182, 24-38.
    • (1990) Methods Enzymol. , vol.182 , pp. 24-38
    • Stoll, V.S.1    Blanchard, J.S.2
  • 42
    • 0025995263 scopus 로고
    • Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
    • Welinder, K.G. (1991). Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080, 215-220.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 215-220
    • Welinder, K.G.1
  • 43
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder, K.G. (1992). Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2, 388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 44
    • 77957024978 scopus 로고
    • Construction of specific mutations in photosystem II photosynthetic reaction center by genetic engineering methods in Synechocystis 6803
    • Williams, J.G.K. (1988). Construction of specific mutations in photosystem II photosynthetic reaction center by genetic engineering methods in Synechocystis 6803. Methods Enzymol. 167, 766-778.
    • (1988) Methods Enzymol. , vol.167 , pp. 766-778
    • Williams, J.G.K.1
  • 45
    • 0029070056 scopus 로고
    • Spectral characterization and chemical modification of catalase-peroxidase from Streptomyces sp.
    • Youn, H.-D., Yim, Y.-I., Kim, K., Hah, Y.C., and Kang, S.-O. (1995). Spectral characterization and chemical modification of catalase-peroxidase from Streptomyces sp. J. Biol. Chem. 270, 13740-13747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13740-13747
    • Youn, H.-D.1    Yim, Y.-I.2    Kim, K.3    Hah, Y.C.4    Kang, S.-O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.