메뉴 건너뛰기




Volumn 75, Issue 9, 2009, Pages 2750-2757

Cellobiose dehydrogenase from the ligninolytic basidiomycete Ceriporiopsis subvermispora

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; CARBOHYDRATE CONTENT; CATALYTIC EFFICIENCIES; CELLOBIOSE; CELLOBIOSE DEHYDROGENASE; CERIPORIOPSIS SUBVERMISPORA; ELECTRON ACCEPTOR; ELECTRON TRANSFER; EXTRACELLULAR; EXTRACELLULAR PROTEINS; FLAVOCYTOCHROME; GENOMIC DNA; GLUCOSE CONVERSION; GLYCOFORMS; HIGHER TEMPERATURES; INTER-DOMAIN; ISO-ELECTRIC POINTS; LIQUID MEDIUM; PEPTIDE LINKERS; PROTEIN SEQUENCES; WHITE ROT FUNGI; YEAST EXTRACTS;

EID: 65549083766     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02320-08     Document Type: Article
Times cited : (46)

References (50)
  • 1
    • 0033563869 scopus 로고    scopus 로고
    • Oxalate oxidase from Ceriporiopsis subvermispora: Biochemical and cytochemical studies
    • Aguilar, C., U. Urzúa, C. Koenig, and R. Vicuña. 1999. Oxalate oxidase from Ceriporiopsis subvermispora: biochemical and cytochemical studies. Arch. Biochem. Biophys. 366:275-282.
    • (1999) Arch. Biochem. Biophys , vol.366 , pp. 275-282
    • Aguilar, C.1    Urzúa, U.2    Koenig, C.3    Vicuña, R.4
  • 3
    • 0028266020 scopus 로고
    • The cellobiose-oxidizing enzymes CBQ and CbO as related to lignin and cellulose degradation: A review
    • Ander, P. 1994. The cellobiose-oxidizing enzymes CBQ and CbO as related to lignin and cellulose degradation: a review. FEMS Microbiol. Rev. 13:297-311.
    • (1994) FEMS Microbiol. Rev , vol.13 , pp. 297-311
    • Ander, P.1
  • 4
    • 0022067755 scopus 로고
    • Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate
    • Ansorge, W. 1985. Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate. J. Biochem. Biophys. Methods 11:13-20.
    • (1985) J. Biochem. Biophys. Methods , vol.11 , pp. 13-20
    • Ansorge, W.1
  • 6
    • 0035318377 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii
    • Baminger, U., S. S. Subramaniam, V. Renganathan, and D. Haltrich. 2001. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl. Environ. Microbiol. 67:1766-1774.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 1766-1774
    • Baminger, U.1    Subramaniam, S.S.2    Renganathan, V.3    Haltrich, D.4
  • 7
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J., H. Nielsen, G. von Heijne, and S. Brunak. 2004. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340:783-795.
    • (2004) J. Mol. Biol , vol.340 , pp. 783-795
    • Bendtsen, J.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 8
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom, N., T. Sicheritz-Pontén, R. Gupta, S. Gammeltoft, and S. Brunak. 2004. Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4:1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Pontén, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bind- ing
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bind- ing. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0035252395 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase: An extra- cellular fungal flavocytochrome
    • Cameron, M. D., and S. D. Aust. 2001. Cellobiose dehydrogenase: an extra- cellular fungal flavocytochrome. Enzyme Microb. Technol. 28:129-138.
    • (2001) Enzyme Microb. Technol , vol.28 , pp. 129-138
    • Cameron, M.D.1    Aust, S.D.2
  • 11
    • 0025865802 scopus 로고
    • Cellobiose dehydrogenase of Sporotrichum (Chrysosporium) thermophile
    • Canevascini, G., P. Borer, and J.-L. Dreyer. 1991. Cellobiose dehydrogenase of Sporotrichum (Chrysosporium) thermophile. Eur. J. Biochem. 198:43-52.
    • (1991) Eur. J. Biochem , vol.198 , pp. 43-52
    • Canevascini, G.1    Borer, P.2    Dreyer, J.-L.3
  • 12
    • 0442276359 scopus 로고    scopus 로고
    • Extraction and determination of enzymes produced by Ceriporiopsis subvermispora dur- ing biopulping of Pinus taeda wood chips
    • De Souza-Cruz, P. B., J. Freer, M. Siika-Aho, and A. Ferraz. 2004. Extraction and determination of enzymes produced by Ceriporiopsis subvermispora dur- ing biopulping of Pinus taeda wood chips. Enzyme Microb. Technol. 34:228-234.
    • (2004) Enzyme Microb. Technol , vol.34 , pp. 228-234
    • De Souza-Cruz, P.B.1    Freer, J.2    Siika-Aho, M.3    Ferraz, A.4
  • 13
    • 0035813522 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase is essential for wood invasion and nones- sential for kraft pulp delignification by Trametes versicolor
    • Dumonceaux, T., K. Bartholomew, L. Valeanu, T. Charles, and F. Archibald. 2001. Cellobiose dehydrogenase is essential for wood invasion and nones- sential for kraft pulp delignification by Trametes versicolor. Enzyme Microb. Technol. 29:478-489.
    • (2001) Enzyme Microb. Technol , vol.29 , pp. 478-489
    • Dumonceaux, T.1    Bartholomew, K.2    Valeanu, L.3    Charles, T.4    Archibald, F.5
  • 14
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., H. Nielsen, S. Brunak, and G. von Heijne. 2000. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300:1005-1016.
    • (2000) J. Mol. Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 17
    • 0037413379 scopus 로고    scopus 로고
    • Wood biodegradation and enzyme production by Ceriporiopsis subvermispora during solid-state fermen- tation of Eucalyptus grandis
    • Ferraz, A., A. M. Cordova, and A. Machuca. 2003. Wood biodegradation and enzyme production by Ceriporiopsis subvermispora during solid-state fermen- tation of Eucalyptus grandis. Enzyme Microb. Technol. 32:59-65.
    • (2003) Enzyme Microb. Technol , vol.32 , pp. 59-65
    • Ferraz, A.1    Cordova, A.M.2    Machuca, A.3
  • 18
    • 0027580147 scopus 로고
    • ITS primers with enhanced specificity for basidiomycetes: Application to the identification of mycorrhizae and rusts
    • Gardes, M., and T. D. Bruns. 1993. ITS primers with enhanced specificity for basidiomycetes: application to the identification of mycorrhizae and rusts. Mol. Ecol. 2:113-118.
    • (1993) Mol. Ecol , vol.2 , pp. 113-118
    • Gardes, M.1    Bruns, T.D.2
  • 19
    • 0038411275 scopus 로고    scopus 로고
    • Molecular weight distribution of wood components extracted from Pinus taeda biotreated by Ceriporiopsis subvermispora
    • Guerra, A., R. Mendonca, and A. Ferraz. 2003. Molecular weight distribution of wood components extracted from Pinus taeda biotreated by Ceriporiopsis subvermispora. Enzyme Microb. Technol. 33:12-18.
    • (2003) Enzyme Microb. Technol , vol.33 , pp. 12-18
    • Guerra, A.1    Mendonca, R.2    Ferraz, A.3
  • 20
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg, M. B., G. Henriksson, G. Pettersson, and C. Divne. 2002. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J. Mol. Biol. 315:421-434.
    • (2002) J. Mol. Biol , vol.315 , pp. 421-434
    • Hallberg, M.B.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 21
    • 43849099090 scopus 로고    scopus 로고
    • Role of fungal peroxidases in biological ligninolysis
    • Hammel, K. E., and D. Cullen. 2008. Role of fungal peroxidases in biological ligninolysis. Curr. Opin. Plant Biol. 11:1-7.
    • (2008) Curr. Opin. Plant Biol , vol.11 , pp. 1-7
    • Hammel, K.E.1    Cullen, D.2
  • 22
    • 0028347666 scopus 로고
    • Lignin-modifying enzymes from selected white-rot fungi: Production and role in lignin degradation
    • Hatakka, A. 1994. Lignin-modifying enzymes from selected white-rot fungi: production and role in lignin degradation. FEMS Microbiol. Rev. 13:125-135.
    • (1994) FEMS Microbiol. Rev , vol.13 , pp. 125-135
    • Hatakka, A.1
  • 23
    • 28844490102 scopus 로고    scopus 로고
    • Characterization of hemicellulases and cellulases produced by Ceriporiopsis subvermispora grown on wood under biopulping conditions
    • Heidorne, F. O., P. O. Magalhaes, A. L. Ferraz, and A. M. F. Milagres. 2006. Characterization of hemicellulases and cellulases produced by Ceriporiopsis subvermispora grown on wood under biopulping conditions. Enzyme Microb. Technol. 38:436-442.
    • (2006) Enzyme Microb. Technol , vol.38 , pp. 436-442
    • Heidorne, F.O.1    Magalhaes, P.O.2    Ferraz, A.L.3    Milagres, A.M.F.4
  • 24
  • 25
  • 27
    • 0010612802 scopus 로고
    • Characterization and regulation of cellobiose dehydrogenase in Fomes annosus
    • Hüttermann, A., and A. Noelle. 1982. Characterization and regulation of cellobiose dehydrogenase in Fomes annosus. Holzforschung 36:283-286.
    • (1982) Holzforschung , vol.36 , pp. 283-286
    • Hüttermann, A.1    Noelle, A.2
  • 28
    • 0031032498 scopus 로고    scopus 로고
    • A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hy- phae
    • Hyde, S. M., and P. M. Wood. 1997. A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hy- phae. Microbiology 143:259-266.
    • (1997) Microbiology , vol.143 , pp. 259-266
    • Hyde, S.M.1    Wood, P.M.2
  • 29
    • 0033525202 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase (CDH) from the fungi Phanerochaete chrysosporium and Humicola insolens: The flavohemo- protein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor
    • Igarashii, K., M. F. J. M. Verhagen, M. Samejima, M. Schülein, K. E. Eriksson, and T. Nishino. 1999. Cellobiose dehydrogenase (CDH) from the fungi Phanerochaete chrysosporium and Humicola insolens: the flavohemo- protein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor. J. Biol. Chem. 274:3338-3344.
    • (1999) J. Biol. Chem , vol.274 , pp. 3338-3344
    • Igarashii, K.1    Verhagen, M.F.J.M.2    Samejima, M.3    Schülein, M.4    Eriksson, K.E.5    Nishino, T.6
  • 30
    • 28444457376 scopus 로고    scopus 로고
    • Properties of neutral cellobiose dehydro- genase from the ascomycete Chaetomium sp. INBI 2-26 and comparison with basidiomycetous cellobiose dehydrogenase
    • Karapetyan, K. N., T. V. Fedorova, L. G. Vasil'chenko, R. Ludwig, D. Hal- trich, and M. L. Rabinovich. 2006. Properties of neutral cellobiose dehydro- genase from the ascomycete Chaetomium sp. INBI 2-26 and comparison with basidiomycetous cellobiose dehydrogenase. J. Biotechnol. 121:34-48.
    • (2006) J. Biotechnol , vol.121 , pp. 34-48
    • Karapetyan, K.N.1    Fedorova, T.V.2    Vasil'chenko, L.G.3    Ludwig, R.4    Hal- trich, D.5    Rabinovich, M.L.6
  • 31
    • 0026674531 scopus 로고
    • Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium
    • Kremer, S. M., and P. M. Wood. 1992. Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium. Eur. J. Biochem. 208:807-814.
    • (1992) Eur. J. Biochem , vol.208 , pp. 807-814
    • Kremer, S.M.1    Wood, P.M.2
  • 32
    • 4444364240 scopus 로고    scopus 로고
    • Characteriza- tion of a multicopper oxidase gene cluster in Phanerochaete chrysosporium and evidence of altered splicing of the mco transcripts
    • Larrondo, L. F., B. Gonzalez, D. Cullen, and R. Vicuña. 2004. Characteriza- tion of a multicopper oxidase gene cluster in Phanerochaete chrysosporium and evidence of altered splicing of the mco transcripts. Microbiology 150: 2775-2783.
    • (2004) Microbiology , vol.150 , pp. 2775-2783
    • Larrondo, L.F.1    Gonzalez, B.2    Cullen, D.3    Vicuña, R.4
  • 33
    • 0142040829 scopus 로고    scopus 로고
    • A novel extracellular multicopper oxidase from Phanerochaete chrasosporium with ferroxidase activity
    • Larrondo, L. F., L. Salas, F. Melo, R. Vicuna, and D. Cullen. 2003. A novel extracellular multicopper oxidase from Phanerochaete chrasosporium with ferroxidase activity. Appl. Environ. Microbiol. 69:6257-6263.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 6257-6263
    • Larrondo, L.F.1    Salas, L.2    Melo, F.3    Vicuna, R.4    Cullen, D.5
  • 36
    • 0348049808 scopus 로고    scopus 로고
    • Rotting by radicals: The role of cellobiose oxidoreductase?
    • Mason, M. G., P. Nicholls, and M. T. Wilson. 2003. Rotting by radicals: the role of cellobiose oxidoreductase? Biochem. Soc. Trans. 31:1335-1336.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1335-1336
    • Mason, M.G.1    Nicholls, P.2    Wilson, M.T.3
  • 37
    • 0037042218 scopus 로고    scopus 로고
    • Oxygen reduc- tion by cellobiose oxidoreductase: The role of the haem group
    • Mason, M. G., M. T. Wilson, A. Ball, and P. Nicholls. 2002. Oxygen reduc- tion by cellobiose oxidoreductase: the role of the haem group. FEBS Lett. 518:29-32.
    • (2002) FEBS Lett , vol.518 , pp. 29-32
    • Mason, M.G.1    Wilson, M.T.2    Ball, A.3    Nicholls, P.4
  • 38
    • 0028329762 scopus 로고
    • Biopulping: An overview on develop- ments in an environmentally save paper-making technology
    • Messner, K., and E. Srebotnik. 1994. Biopulping: an overview on develop- ments in an environmentally save paper-making technology. FEMS Micro- biol. Rev. 13:351-364.
    • (1994) FEMS Micro- biol. Rev , vol.13 , pp. 351-364
    • Messner, K.1    Srebotnik, E.2
  • 39
    • 0030614959 scopus 로고    scopus 로고
    • Identifica- tion of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identifica- tion of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. Des. Sel. 10:1-6.
    • (1997) Protein Eng. Des. Sel , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 40
    • 25844478457 scopus 로고    scopus 로고
    • Ceriporic acid B, an extracellular metabolite of Ceriporiopsis subvermispora, suppresses the depolymerization of cellulose by the Fenton reaction
    • Rahmawati, N., Y. Ohashi, T. Watanabe, Y. Honda, and T. Watanabe. 2005. Ceriporic acid B, an extracellular metabolite of Ceriporiopsis subvermispora, suppresses the depolymerization of cellulose by the Fenton reaction. Bio- macromolecules 6:2851-2856.
    • (2005) Bio- macromolecules , vol.6 , pp. 2851-2856
    • Rahmawati, N.1    Ohashi, Y.2    Watanabe, T.3    Honda, Y.4    Watanabe, T.5
  • 41
    • 0029860128 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenase from the white rot fungus Trametes versicolor
    • Roy, B. P., T. Dumonceaux, A. A. Koukoulas, and F. S. Archibald. 1996. Purification and characterization of cellobiose dehydrogenase from the white rot fungus Trametes versicolor. Appl. Environ. Microbiol. 62:4417-4427.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 4417-4427
    • Roy, B.P.1    Dumonceaux, T.2    Koukoulas, A.A.3    Archibald, F.S.4
  • 42
    • 0000758534 scopus 로고    scopus 로고
    • Production of hemicellulose- and cellulose-degrading enzymes by various strains of Sclerotium rolfsii
    • Sachslehner, A., D. Haltrich, B. Nidetzky, and K. D. Kulbe. 1997. Production of hemicellulose- and cellulose-degrading enzymes by various strains of Sclerotium rolfsii. Appl. Biochem. Biotechnol. 63-65:189-201.
    • (1997) Appl. Biochem. Biotechnol , vol.63-65 , pp. 189-201
    • Sachslehner, A.1    Haltrich, D.2    Nidetzky, B.3    Kulbe, K.D.4
  • 44
    • 0029025395 scopus 로고
    • Synthetic lignin mineralization by Ceripori- opsis subvermispora is inhibited by an increase in the pH of the cultures resulting from fungal growth
    • Tapia, J., and R. Vicun. 1995. Synthetic lignin mineralization by Ceripori- opsis subvermispora is inhibited by an increase in the pH of the cultures resulting from fungal growth. Appl. Environ. Microbiol. 61:2476-2481.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 2476-2481
    • Tapia, J.1    Vicun, R.2
  • 45
    • 0032975171 scopus 로고    scopus 로고
    • Novel interaction between laccase and cel- lobiose dehydrogenase during pigment synthesis in the white rot fungus Pycnoporus cinnabarinus
    • Temp, U., and C. Eggert. 1999. Novel interaction between laccase and cel- lobiose dehydrogenase during pigment synthesis in the white rot fungus Pycnoporus cinnabarinus. Appl. Environ. Microbiol. 65:389-395.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 389-395
    • Temp, U.1    Eggert, C.2
  • 46
    • 0035498333 scopus 로고    scopus 로고
    • Oxidative mechanisms involved in lignin degradation by white-rot fungi
    • ten Have, R., and P. J. M. Teunissen. 2001. Oxidative mechanisms involved in lignin degradation by white-rot fungi. Chem. Rev. 101:3397-3413.
    • (2001) Chem. Rev , vol.101 , pp. 3397-3413
    • ten Have, R.1    Teunissen, P.J.M.2
  • 47
    • 0031985659 scopus 로고    scopus 로고
    • Manganese peroxidase- dependent oxidation of glyoxylic and oxalic acid synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide
    • Urzúa, U., P. J. Kersten, and R. Vicuna. 1998. Manganese peroxidase- dependent oxidation of glyoxylic and oxalic acid synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide. Appl. Environ. Mi- crobiol. 64:68-73.
    • (1998) Appl. Environ. Mi- crobiol , vol.64 , pp. 68-73
    • Urzúa, U.1    Kersten, P.J.2    Vicuna, R.3
  • 49
    • 4143089527 scopus 로고    scopus 로고
    • Ancestral gene fusion in cellobiose dehydrogenase reflects a specific evolu- tion of GMC oxidoreductases in fungi
    • Zámocký, M., M. Hallberg, R. Ludwig, C. Divne, and D. Haltrich. 2004. Ancestral gene fusion in cellobiose dehydrogenase reflects a specific evolu- tion of GMC oxidoreductases in fungi. Gene 338:1-14.
    • (2004) Gene , vol.338 , pp. 1-14
    • Zámocký, M.1    Hallberg, M.2    Ludwig, R.3    Divne, C.4    Haltrich, D.5
  • 50
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase: A flavocytochrome from wood-degrading, phytopathogenic and saprotrophic fungi. Curr. Pro- tein
    • Zámocký, M., R. Ludwig, C. Peterbauer, B. M. Hallberg, C. Divne, P. Ni- cholls, and D. Haltrich. 2006. Cellobiose dehydrogenase: a flavocytochrome from wood-degrading, phytopathogenic and saprotrophic fungi. Curr. Pro- tein Pept. Sci. 7:255-280.
    • (2006) Pept. Sci , vol.7 , pp. 255-280
    • Zámocký, M.1    Ludwig, R.2    Peterbauer, C.3    Hallberg, B.M.4    Divne, C.5    Ni- cholls, P.6    Haltrich, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.