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Volumn 46, Issue 3-4, 2010, Pages 217-222

Characterization of a new Cu/Zn-superoxide dismutase from Beauveria bassiana and two site-directed mutations crucial to its antioxidation activity without chaperon

Author keywords

Antioxidation activity enhancement; Beauveria bassiana; Copper chaperon; Site directed mutation; Superoxide dismutase

Indexed keywords

ANTIOXIDATION ACTIVITIES; BEAUVERIA BASSIANA; CRUDE EXTRACT; CU/ZN-SOD; CU/ZN-SUPEROXIDE DISMUTASE; E. COLI; FUNCTION ANALYSIS; GENE CLONING; HETEROGENEOUS EXPRESSIONS; LURIA-BERTANI MEDIUMS; SEQUENCE IDENTITY; SITE-DIRECTED MUTATION; SUPER OXIDE DISMUTASE;

EID: 74149090314     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.09.005     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 0020644952 scopus 로고
    • Superoxide radical: an endogenous toxicant
    • Fridovich I. Superoxide radical: an endogenous toxicant. Annu Rev Pharmacol Toxicol 23 (1983) 239-257
    • (1983) Annu Rev Pharmacol Toxicol , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 2
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem 64 (1995) 97-112
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 3
    • 56649123322 scopus 로고    scopus 로고
    • Manganese superoxide dismutase expressed in silkworm larvae, Bombyx mori L enhances the NK activity and splenocyte proliferation against Sarcoma 180 tumor cells in vivo
    • Yue W.F., Yao M.L., Liu J.M., Li G.L., Li X.H., Wu X.F., et al. Manganese superoxide dismutase expressed in silkworm larvae, Bombyx mori L enhances the NK activity and splenocyte proliferation against Sarcoma 180 tumor cells in vivo. Mol Biol Rep 36 (2009) 187-192
    • (2009) Mol Biol Rep , vol.36 , pp. 187-192
    • Yue, W.F.1    Yao, M.L.2    Liu, J.M.3    Li, G.L.4    Li, X.H.5    Wu, X.F.6
  • 4
    • 44449089083 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan
    • Gao F., Koenitzer J.R., Tobolewski J.M., Jiang D.H., Liang J.R., Noble P.W., et al. Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan. J Biol Chem 283 (2008) 6058-6066
    • (2008) J Biol Chem , vol.283 , pp. 6058-6066
    • Gao, F.1    Koenitzer, J.R.2    Tobolewski, J.M.3    Jiang, D.H.4    Liang, J.R.5    Noble, P.W.6
  • 5
    • 41049108634 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase protects the heart against oxidative stress and hypertrophy after myocardial infarction
    • van Deel E.D., Lu Z.B., Xu X., Zhu G.S., Hu X.L., Oury T.D., et al. Extracellular superoxide dismutase protects the heart against oxidative stress and hypertrophy after myocardial infarction. Free Rad Biol Med 44 (2008) 1305-1313
    • (2008) Free Rad Biol Med , vol.44 , pp. 1305-1313
    • van Deel, E.D.1    Lu, Z.B.2    Xu, X.3    Zhu, G.S.4    Hu, X.L.5    Oury, T.D.6
  • 7
    • 74149092116 scopus 로고    scopus 로고
    • Novel purified isozyme of autoclavable superoxide dismutase extracted from the plant Potentilla atrosanguinea Lodd. var. argyrophylla, useful in cosmetic, pharmaceutical and food compositions
    • US Patent 6485950-B1 2003
    • Kumar S, Sahoo R, Ahuja PS. Novel purified isozyme of autoclavable superoxide dismutase extracted from the plant Potentilla atrosanguinea Lodd. var. argyrophylla, useful in cosmetic, pharmaceutical and food compositions. US Patent 6485950-B1 (2003).
    • Kumar, S.1    Sahoo, R.2    Ahuja, P.S.3
  • 8
    • 74149084822 scopus 로고    scopus 로고
    • Bhardwaj PK, Sahoo R, Kumar S, Ahuja PS, Bhardwaj P, Ahuja P. New superoxide dismutase (SOD) obtained from Potentilla atrosanguinea, useful in pharmaceuticals and medical fields, and in cosmetic and food industry. World Patent 2007113615-A1 2007
    • Bhardwaj PK, Sahoo R, Kumar S, Ahuja PS, Bhardwaj P, Ahuja P. New superoxide dismutase (SOD) obtained from Potentilla atrosanguinea, useful in pharmaceuticals and medical fields, and in cosmetic and food industry. World Patent 2007113615-A1 (2007).
  • 9
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • Casareno R.L.B., Waggoner D., and Gitlin J.D. The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J Biol Chem 273 (1998) 23625-23628
    • (1998) J Biol Chem , vol.273 , pp. 23625-23628
    • Casareno, R.L.B.1    Waggoner, D.2    Gitlin, J.D.3
  • 10
    • 0034721928 scopus 로고    scopus 로고
    • Copper activation of superoxide dismutase 1 (SOD1) in vivo: role for protein-protein interactions with the copper chaperone for SOD1
    • Schmidt P.J., Kunst C., and Culotta V.C. Copper activation of superoxide dismutase 1 (SOD1) in vivo: role for protein-protein interactions with the copper chaperone for SOD1. J Biol Chem 275 (2000) 33771-33776
    • (2000) J Biol Chem , vol.275 , pp. 33771-33776
    • Schmidt, P.J.1    Kunst, C.2    Culotta, V.C.3
  • 11
    • 3543029884 scopus 로고    scopus 로고
    • Oxygen induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS
    • Furukawa Y., Torres A.S., and Halloran T.V. Oxygen induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J 23 (2004) 2872-2881
    • (2004) EMBO J , vol.23 , pp. 2872-2881
    • Furukawa, Y.1    Torres, A.S.2    Halloran, T.V.3
  • 12
    • 0029161726 scopus 로고
    • Cloning and characterization of the Saccharomyces cerevisiae lys7 gene - evidence for function outside of lysine biosynthesis
    • Horecka J., Kinsey P.T., and Sprague G.F. Cloning and characterization of the Saccharomyces cerevisiae lys7 gene - evidence for function outside of lysine biosynthesis. Gene 162 (1995) 87-92
    • (1995) Gene , vol.162 , pp. 87-92
    • Horecka, J.1    Kinsey, P.T.2    Sprague, G.F.3
  • 14
    • 0036669912 scopus 로고    scopus 로고
    • Plant copper chaperones
    • Wintz H., and Vulpe C. Plant copper chaperones. Biochem Soc Trans 30 (2002) 732-735
    • (2002) Biochem Soc Trans , vol.30 , pp. 732-735
    • Wintz, H.1    Vulpe, C.2
  • 15
    • 0034726678 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a copper chaperone for copper/zinc superoxide dismutase from the rat
    • Hiromura M., Chino H., Sonoda T., and Sakurai H. Molecular cloning and characterization of a copper chaperone for copper/zinc superoxide dismutase from the rat. Biochem Biophys Res Commun 275 (2000) 394-400
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 394-400
    • Hiromura, M.1    Chino, H.2    Sonoda, T.3    Sakurai, H.4
  • 16
    • 0034065650 scopus 로고    scopus 로고
    • Cloning and mapping of murine CCS and mapping of the human orthology
    • Moore S.D., Chen M.M., and Cox D.W. Cloning and mapping of murine CCS and mapping of the human orthology. Cytogenet Cell Genet 88 (2000) 35-37
    • (2000) Cytogenet Cell Genet , vol.88 , pp. 35-37
    • Moore, S.D.1    Chen, M.M.2    Cox, D.W.3
  • 18
    • 0037111137 scopus 로고    scopus 로고
    • CCS knockout mice establish an alternative source for copper for SOD in ALS
    • Beckman J.S., Estvez A.G., Barbeito L., and Crow J.P. CCS knockout mice establish an alternative source for copper for SOD in ALS. Free Rad Biol Med 33 (2002) 1433-1435
    • (2002) Free Rad Biol Med , vol.33 , pp. 1433-1435
    • Beckman, J.S.1    Estvez, A.G.2    Barbeito, L.3    Crow, J.P.4
  • 19
    • 29244480623 scopus 로고    scopus 로고
    • Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS
    • Jensen L.T., and Culotta V.C. Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS. J Biol Chem 280 (2005) 41373-41379
    • (2005) J Biol Chem , vol.280 , pp. 41373-41379
    • Jensen, L.T.1    Culotta, V.C.2
  • 20
    • 35548970780 scopus 로고    scopus 로고
    • Mycoinsecticides and mycoacaricides: a comprehensive list with worldwide coverage and international classification of formulation types
    • De Faria M.R., and Wraight S.P. Mycoinsecticides and mycoacaricides: a comprehensive list with worldwide coverage and international classification of formulation types. Biol Control 43 (2007) 237-256
    • (2007) Biol Control , vol.43 , pp. 237-256
    • De Faria, M.R.1    Wraight, S.P.2
  • 21
    • 70149108159 scopus 로고    scopus 로고
    • Comparative tolerances of various Beauveria bassiana isolates to UV-B irradiation with a description of a modeling method to assess lethal dose
    • Huang B.F., and Feng M.G. Comparative tolerances of various Beauveria bassiana isolates to UV-B irradiation with a description of a modeling method to assess lethal dose. Mycopathol 168 (2009) 145-215
    • (2009) Mycopathol , vol.168 , pp. 145-215
    • Huang, B.F.1    Feng, M.G.2
  • 22
    • 0031825295 scopus 로고    scopus 로고
    • Molecular and cellular effects of ultraviolet light-induced genotoxicity
    • Griffiths H.R., Mistry P., Herbert K.E., and Lunec J. Molecular and cellular effects of ultraviolet light-induced genotoxicity. Crit Rev Clin Lab Sci 35 (1998) 189-237
    • (1998) Crit Rev Clin Lab Sci , vol.35 , pp. 189-237
    • Griffiths, H.R.1    Mistry, P.2    Herbert, K.E.3    Lunec, J.4
  • 23
    • 0022206304 scopus 로고
    • Rapid preparation of DNA from filamentous fungi
    • Reader U., and Broda P. Rapid preparation of DNA from filamentous fungi. Lett Appl Microbiol 1 (1985) 17-20
    • (1985) Lett Appl Microbiol , vol.1 , pp. 17-20
    • Reader, U.1    Broda, P.2
  • 24
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S., Nei M., Dudley J., and Tamura K. MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinform 9 (2008) 299-306
    • (2008) Brief Bioinform , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 25
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S., and Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47 (1974) 248-254
    • (1974) Eur J Biochem , vol.47 , pp. 248-254
    • Marklund, S.1    Marklund, G.2
  • 26
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount S.M. A catalogue of splice junction sequences. Nucleic Acids Res 10 (1982) 459-472
    • (1982) Nucleic Acids Res , vol.10 , pp. 459-472
    • Mount, S.M.1
  • 28
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu,Zn superoxide dismutase family
    • Bordo D., Djinovic K., and Bolognesi M. Conserved patterns in the Cu,Zn superoxide dismutase family. J Mol Biol 238 (1994) 366-386
    • (1994) J Mol Biol , vol.238 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 29
    • 0022384062 scopus 로고
    • Essentially of the active site arginine residue for the normal catalytic activity of Cu,Zn superoxide dismutase
    • Borders C.J., Saunders J.E., Blech D.M., and Fridovich I. Essentially of the active site arginine residue for the normal catalytic activity of Cu,Zn superoxide dismutase. Biochem J 230 (1985) 771-776
    • (1985) Biochem J , vol.230 , pp. 771-776
    • Borders, C.J.1    Saunders, J.E.2    Blech, D.M.3    Fridovich, I.4
  • 31
    • 0034969183 scopus 로고    scopus 로고
    • A novel glycosylated Cu/Zn-containing superoxide dismutase: production and potential therapeutic effect
    • Angelova M., Dolashka-Angelova P., Ivanova E., Serkedjieva J., Slokoska L., Pashova S., et al. A novel glycosylated Cu/Zn-containing superoxide dismutase: production and potential therapeutic effect. Microbiol-SGM 147 (2001) 1641-1650
    • (2001) Microbiol-SGM , vol.147 , pp. 1641-1650
    • Angelova, M.1    Dolashka-Angelova, P.2    Ivanova, E.3    Serkedjieva, J.4    Slokoska, L.5    Pashova, S.6
  • 32
    • 0012023519 scopus 로고    scopus 로고
    • Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli
    • Seo H.S., Koo Y.J., Lim J.Y., Song J.T., Kim C.H., Kim J.K., et al. Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli. Appl Environ Microbiol 66 (2000) 2484-2490
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2484-2490
    • Seo, H.S.1    Koo, Y.J.2    Lim, J.Y.3    Song, J.T.4    Kim, C.H.5    Kim, J.K.6
  • 33
    • 0035664509 scopus 로고    scopus 로고
    • Optimized linker sequences for the expression of monomeric and dimeric bispecific single-chain diabodies
    • Volkel T., Korn T., Bach M., Muller R., and Kontermann R.E. Optimized linker sequences for the expression of monomeric and dimeric bispecific single-chain diabodies. Protein Eng 14 (2001) 815-823
    • (2001) Protein Eng , vol.14 , pp. 815-823
    • Volkel, T.1    Korn, T.2    Bach, M.3    Muller, R.4    Kontermann, R.E.5
  • 34
    • 0028880549 scopus 로고
    • Effect of glucose on the superoxide dismutase production in fungal strain Humicola lutea
    • Angelova M., Genova L., Slokoska L., and Pashova S. Effect of glucose on the superoxide dismutase production in fungal strain Humicola lutea. Can J Microbiol 41 (1995) 978-983
    • (1995) Can J Microbiol , vol.41 , pp. 978-983
    • Angelova, M.1    Genova, L.2    Slokoska, L.3    Pashova, S.4
  • 35
    • 0030471370 scopus 로고    scopus 로고
    • Effect of cultural conditions on the synthesis of superoxide dismutase by Humicola lutea 110
    • Angelova M., Genova L., Pashova S., Slokoska L., and Dolashka P. Effect of cultural conditions on the synthesis of superoxide dismutase by Humicola lutea 110. J Ferment Bioeng 82 (1996) 464-468
    • (1996) J Ferment Bioeng , vol.82 , pp. 464-468
    • Angelova, M.1    Genova, L.2    Pashova, S.3    Slokoska, L.4    Dolashka, P.5
  • 36
    • 33847268142 scopus 로고    scopus 로고
    • Improved production by fed-batch cultivation and some properties of Cu/Zn-superoxide dismutase from the fungal strain Humicola lutea 103
    • Krumova E., Dolashka-Angelova P., Pashova S., Stefanova L., Van Beeumen J., Vassilev S., et al. Improved production by fed-batch cultivation and some properties of Cu/Zn-superoxide dismutase from the fungal strain Humicola lutea 103. Enzyme Micro Technol 40 (2007) 524-532
    • (2007) Enzyme Micro Technol , vol.40 , pp. 524-532
    • Krumova, E.1    Dolashka-Angelova, P.2    Pashova, S.3    Stefanova, L.4    Van Beeumen, J.5    Vassilev, S.6
  • 37
    • 31344476584 scopus 로고    scopus 로고
    • Effect of nutrition factors on the synthesis of superoxide dismutase, catalase, and membrane lipid peroxide levels in Cordyceps militaris mycelium
    • Wang Z.S., Gu Y.X., and Yuan Q.S. Effect of nutrition factors on the synthesis of superoxide dismutase, catalase, and membrane lipid peroxide levels in Cordyceps militaris mycelium. Curr Microbiol 52 (2006) 74-79
    • (2006) Curr Microbiol , vol.52 , pp. 74-79
    • Wang, Z.S.1    Gu, Y.X.2    Yuan, Q.S.3
  • 38
    • 38049174883 scopus 로고    scopus 로고
    • Characterization of the superoxide dismutase SOD1 gene of Kluyveromyces marxianus L3 and improved production of SOD activity
    • Raimondi S., Uccelletti D., Matteuzzi D., Pagnoni U.M., Rossi M., and Palleschi C. Characterization of the superoxide dismutase SOD1 gene of Kluyveromyces marxianus L3 and improved production of SOD activity. Appl Microbiol Biotechnol 77 (2008) 1269-1277
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1269-1277
    • Raimondi, S.1    Uccelletti, D.2    Matteuzzi, D.3    Pagnoni, U.M.4    Rossi, M.5    Palleschi, C.6


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