메뉴 건너뛰기




Volumn 77, Issue 5, 2011, Pages 1804-1815

Catalytic properties and classification of cellobiose dehydrogenases from ascomycetes

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PH; BIOCHEMICAL DATA; CARBOHYDRATE-BINDING MODULES; CATALYTIC PROPERTIES; CELLOBIOSE; CELLOBIOSE DEHYDROGENASE; CLASS II; ENCODING GENES; EXTRACELLULAR; FLAVOCYTOCHROME; GENOME SEQUENCING PROJECTS; INTRA-MOLECULAR ELECTRON TRANSFER; LIGNOCELLULOSE DEGRADATION; MATURE PROTEINS; NEUROSPORA CRASSA; PH OPTIMA; PH-DEPENDENT; SUBSTRATE SPECIFICITY; THERMOPHILUS; WHITE ROT;

EID: 79953182351     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02052-10     Document Type: Article
Times cited : (120)

References (46)
  • 1
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • Baldrian, P., and V. Valaskova. 2008. Degradation of cellulose by basidiomycetous fungi. FEMS Microbiol. Rev. 32:501-521.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 501-521
    • Baldrian, P.1    Valaskova, V.2
  • 2
    • 0033003063 scopus 로고    scopus 로고
    • A simple assay for measuring cellobiose dehydrogenase activity in the presence of laccase
    • Baminger, U., B. Nidetzky, K. D. Kulbe, and D. Haltrich. 1999. A simple assay for measuring cellobiose dehydrogenase activity in the presence of laccase. J. Microbiol. Methods 35:253-259.
    • (1999) J. Microbiol. Methods , vol.35 , pp. 253-259
    • Baminger, U.1    Nidetzky, B.2    Kulbe, K.D.3    Haltrich, D.4
  • 3
    • 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
  • 4
    • 0025865802 scopus 로고
    • Cellobiose dehydrogenases of Sporotrichum (Chrysosporium) thermophile
    • Canevascini, G., P. Borer, and J. L. Dreyer. 1991. Cellobiose dehydrogenases 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
  • 5
    • 0020119009 scopus 로고
    • Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile
    • Coudray, M. R., G. Canevascini, and H. Meier. 1982. Characterization of a cellobiose dehydrogenase in the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile. Biochem. J. 203:277-284.
    • (1982) Biochem. J. , vol.203 , pp. 277-284
    • Coudray, M.R.1    Canevascini, G.2    Meier, H.3
  • 6
    • 20244366844 scopus 로고    scopus 로고
    • The genome sequence of the rice blast fungus Magnaporthe grisea
    • Dean, R. A., et al. 2005. The genome sequence of the rice blast fungus Magnaporthe grisea. Nature 434:980-986.
    • (2005) Nature , vol.434 , pp. 980-986
    • Dean, R.A.1
  • 7
    • 0019254299 scopus 로고
    • Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia
    • Dekker, R. F. H. 1980. Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia. J. Gen. Microbiol. 120:309-316.
    • (1980) J. Gen. Microbiol. , vol.120 , pp. 309-316
    • Dekker, R.F.H.1
  • 8
    • 77952240274 scopus 로고    scopus 로고
    • Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli
    • Desriani, S. Ferri, and K. Sode. 2010. Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli. Biotechnol. Lett. 32:855-859.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 855-859
    • Desriani, S.F.1    Sode, K.2
  • 9
    • 64549104846 scopus 로고    scopus 로고
    • The effect of temperature on the proteome of recombinant Pichia pastoris
    • Dragosits, M., et al. 2009. The effect of temperature on the proteome of recombinant Pichia pastoris. J. Proteome Res. 8:1380-1392.
    • (2009) J. Proteome Res. , vol.8 , pp. 1380-1392
    • Dragosits, M.1
  • 10
    • 48949118871 scopus 로고    scopus 로고
    • The genome sequence of the model ascomycete fungus Podospora anserina
    • Espagne, E., et al. 2008. The genome sequence of the model ascomycete fungus Podospora anserina. Genome Biol. 9:R77.
    • (2008) Genome Biol. , vol.9
    • Espagne, E.1
  • 11
    • 0342910926 scopus 로고
    • Conversion of cellulose to sugars and cellobionic acid by the extracellular enzyme system of Chaetomium cellulolyticum
    • Fähnrich, P., and K. Irrgang. 1982. Conversion of cellulose to sugars and cellobionic acid by the extracellular enzyme system of Chaetomium cellulolyticum. Biotechnol. Lett. 4:775-780.
    • (1982) Biotechnol. Lett. , vol.4 , pp. 775-780
    • Fähnrich, P.1    Irrgang, K.2
  • 12
    • 0030953976 scopus 로고    scopus 로고
    • Wide distribution of cellobiose-oxidizing enzymes in wood-rot fungus indicates a physiological importance in lignocellulosics degradation
    • Fang, J., Y. Qu, and P. Gao. 1997. Wide distribution of cellobiose-oxidizing enzymes in wood-rot fungus indicates a physiological importance in lignocellulosics degradation. Biotechnol. Tech. 11:195-197.
    • (1997) Biotechnol. Tech. , vol.11 , pp. 195-197
    • Fang, J.1    Qu, Y.2    Gao, P.3
  • 13
    • 0037464589 scopus 로고    scopus 로고
    • The genome sequence of the filamentous fungus Neurospora crassa
    • Galagan, J. E., et al. 2003. The genome sequence of the filamentous fungus Neurospora crassa. Nature 422:859-868.
    • (2003) Nature , vol.422 , pp. 859-868
    • Galagan, J.E.1
  • 14
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg, B. M., 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, B.M.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 15
    • 34547587876 scopus 로고    scopus 로고
    • Investigation of graphite electrodes modified with cellobiose dehydrogenase from the ascomycete Myriococcum thermophilum
    • Harreither, W., V. Coman, R. Ludwig, D. Haltrich, and L. Gorton. 2007. Investigation of graphite electrodes modified with cellobiose dehydrogenase from the ascomycete Myriococcum thermophilum. Electroanalysis 19:172- 180.
    • (2007) Electroanalysis , vol.19 , pp. 172-180
    • Harreither, W.1    Coman, V.2    Ludwig, R.3    Haltrich, D.4    Gorton, L.5
  • 16
    • 0030852180 scopus 로고    scopus 로고
    • Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1
    • Henriksson, G., A. Salumets, C. Divne, and G. Petersson. 1997. Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1. Biochem. J. 324:833-838.
    • (1997) Biochem. J. , vol.324 , pp. 833-838
    • Henriksson, G.1    Salumets, A.2    Divne, C.3    Petersson, G.4
  • 17
    • 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 hyphae
    • 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 hyphae. Microbiology 143:259-266.
    • (1997) Microbiology , vol.143 , pp. 259-266
    • Hyde, S.M.1    Wood, P.M.2
  • 18
    • 28444457376 scopus 로고    scopus 로고
    • Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26(-) and comparison with basidiomycetous cellobiose dehydrogenases
    • Karapetyan, K. N., et al. 2006. Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26(-) and comparison with basidiomycetous cellobiose dehydrogenases. J. Biotechnol. 121:34-48.
    • (2006) J. Biotechnol. , vol.121 , pp. 34-48
    • Karapetyan, K.N.1
  • 19
    • 77956207198 scopus 로고    scopus 로고
    • Fungi unearthed: transcripts encoding lignocellulolytic and chitinolytic enzymes in forest soil
    • Kellner, H., and M. Vandenbol. 2010. Fungi unearthed: transcripts encoding lignocellulolytic and chitinolytic enzymes in forest soil. PLoS One 5:e10971.
    • (2010) PLoS One , vol.5
    • Kellner, H.1    Vandenbol, M.2
  • 20
    • 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
  • 21
    • 29244469442 scopus 로고    scopus 로고
    • 14C-labelled synthetic lignin and extracellular enzyme activities of the wood-colonizing ascomycetes Xylaria hypoxylon and Xylaria polymorpha
    • 14C-labelled synthetic lignin and extracellular enzyme activities of the wood-colonizing ascomycetes Xylaria hypoxylon and Xylaria polymorpha. Appl. Microbiol. Biotechnol. 69:573-579.
    • (2006) Appl. Microbiol. Biotechnol. , vol.69 , pp. 573-579
    • Liers, C.1    Ullrich, R.2    Steffen, K.T.3    Hatakka, A.4    Hofrichter, M.5
  • 23
    • 0037364882 scopus 로고    scopus 로고
    • Optimisation of cellobiose dehydrogenase production by the fungus Sclerotium (Athelia) rolfsii
    • Ludwig, R., and D. Haltrich. 2003. Optimisation of cellobiose dehydrogenase production by the fungus Sclerotium (Athelia) rolfsii. Appl. Microbiol. Biotechnol. 61:32-39.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 32-39
    • Ludwig, R.1    Haltrich, D.2
  • 24
    • 77956791837 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase: a versatile catalyst for electrochemical applications
    • Ludwig, R., W. Harreither, F. Tasca, and L. Gorton. 2010. Cellobiose dehydrogenase: a versatile catalyst for electrochemical applications. ChemPhys-Chem 11:2674-2697.
    • (2010) ChemPhys-Chem , vol.11 , pp. 2674-2697
    • Ludwig, R.1    Harreither, W.2    Tasca, F.3    Gorton, L.4
  • 25
    • 2342432133 scopus 로고    scopus 로고
    • Characterisation of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa
    • Ludwig, R., et al. 2004. Characterisation of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa. Appl. Microbiol. Biotechnol. 64:213-222.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 213-222
    • Ludwig, R.1
  • 26
    • 0030812766 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase, an active agent in cellulose depolymerization
    • Mansfield, S. D., E. De Jong, and J. N. Saddler. 1997. Cellobiose dehydrogenase, an active agent in cellulose depolymerization. Appl. Environ. Microbiol. 63:3804-3809.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3804-3809
    • Mansfield, S.D.1    De Jong, E.2    Saddler, J.N.3
  • 27
    • 0037042218 scopus 로고    scopus 로고
    • Oxygen reduction by cellobiose oxidoreductase: the role of the haem group
    • Mason, M. G., M. T. Wilson, A. Ball, and P. Nicholls. 2002. Oxygen reduction 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
  • 28
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine, T. C. 1921. A buffer solution for colorimetric comparison. J. Biol. Chem. 49:183-186.
    • (1921) J. Biol. Chem. , vol.49 , pp. 183-186
    • McIlvaine, T.C.1
  • 29
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: when are closer mutations better?
    • Morley, K. L., and R. J. Kazlauskas. 2005. Improving enzyme properties: when are closer mutations better? Trends Biotechnol. 23:231-237.
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 30
    • 77952337288 scopus 로고    scopus 로고
    • De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis
    • Nowrousian, M., et al. 2010. De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis. PLoS Genet. 6:e1000891.
    • (2010) PLoS Genet , vol.6
    • Nowrousian, M.1
  • 31
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum evolution trees
    • Rzhetsky, A., and M. Nei. 1992. A simple method for estimating and testing minimum evolution trees. Mol. Biol. Evol. 9:945-967.
    • (1992) Mol. Biol. Evol. , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 32
    • 0000758534 scopus 로고    scopus 로고
    • Production of hemicellulose- and cellulose-degrading enzymes by various strains of Sclerotium rolfsii
    • Sachslehner, A. 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
  • 33
    • 0032519528 scopus 로고    scopus 로고
    • Characterization of a cellobiose dehydrogenase from Humicola insolens
    • Schou, C., M. H. Christensen, and M. Schülein. 1998. Characterization of a cellobiose dehydrogenase from Humicola insolens. Biochem. J. 330:565-571.
    • (1998) Biochem. J. , vol.330 , pp. 565-571
    • Schou, C.1    Christensen, M.H.2    Schülein, M.3
  • 34
    • 35448975285 scopus 로고    scopus 로고
    • New insights into the ligninolytic capability of a wood decay ascomycete
    • Shary, S., S. A. Ralph, and K. E. Hammel. 2007. New insights into the ligninolytic capability of a wood decay ascomycete. Appl. Environ. Microbiol. 73:6691-6694.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6691-6694
    • Shary, S.1    Ralph, S.A.2    Hammel, K.E.3
  • 35
    • 0033562157 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile
    • Subramaniam, S. S., S. R. Nagalla, and V. Renganathan. 1999. Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile. Arch. Biochem. Biophys. 365:223-230.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 223-230
    • Subramaniam, S.S.1    Nagalla, S.R.2    Renganathan, V.3
  • 36
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 37
    • 76049107428 scopus 로고    scopus 로고
    • Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa
    • Tian, C., et al. 2009. Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa. Proc. Natl. Acad. Sci. U. S. A. 106:22157-22162.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22157-22162
    • Tian, C.1
  • 38
    • 0034174658 scopus 로고    scopus 로고
    • Biodegradation of lignin in a compost environment: a review
    • Tuomela, M., M. Vikman, A. Hatakka, and M. Itävaara. 2000. Biodegradation of lignin in a compost environment: a review. Biores. Technol. 72:169- 183.
    • (2000) Biores. Technol. , vol.72 , pp. 169-183
    • Tuomela, M.1    Vikman, M.2    Hatakka, A.3    Itävaara, M.4
  • 40
    • 0030899633 scopus 로고    scopus 로고
    • Comparison of wood decay among diverse lignicolous fungi
    • Worrall, J. J., S. E. Anagnost, and R. A. Zabel. 1997. Comparison of wood decay among diverse lignicolous fungi. Mycologia 89:199-219.
    • (1997) Mycologia , vol.89 , pp. 199-219
    • Worrall, J.J.1    Anagnost, S.E.2    Zabel, R.A.3
  • 41
    • 0035822013 scopus 로고    scopus 로고
    • Humicola insolens cellobiose dehydrogenase: cloning, redox chemistry, and "logic gate"-like dual functionality
    • Xu, F., et al. 2001. Humicola insolens cellobiose dehydrogenase: cloning, redox chemistry, and "logic gate"-like dual functionality. Enzyme Microb. Technol. 28:744-753.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 744-753
    • Xu, F.1
  • 42
    • 23744497140 scopus 로고    scopus 로고
    • Characterization of carbohydrate-binding cytochrome b-562 from the white-rot fungus Phanerochaete chrysosporium
    • Yoshida, M., et al. 2005. Characterization of carbohydrate-binding cytochrome b-562 from the white-rot fungus Phanerochaete chrysosporium. Appl. Environ. Microbiol. 71:4548-4555.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4548-4555
    • Yoshida, M.1
  • 43
    • 4143089527 scopus 로고    scopus 로고
    • Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi
    • Zamocky, M., B. M. Hallberg, R. Ludwig, C. Divne, and D. Haltrich. 2004. Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi. Gene 338:1-14.
    • (2004) Gene , vol.338 , pp. 1-14
    • Zamocky, M.1    Hallberg, B.M.2    Ludwig, R.3    Divne, C.4    Haltrich, D.5
  • 44
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase-a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • Zamocky, M., et al. 2006. Cellobiose dehydrogenase-a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Curr. Protoc. Pept. Sci. 7:255-280.
    • (2006) Curr. Protoc. Pept. Sci. , vol.7 , pp. 255-280
    • Zamocky, M.1
  • 45
    • 42749094404 scopus 로고    scopus 로고
    • Cloning, sequence analysis and heterologous expression in Pichia pastoris of a gene encoding a thermostable cellobiose dehydrogenase from Myriococcum thermophilum
    • Zamocky, M., et al. 2008. Cloning, sequence analysis and heterologous expression in Pichia pastoris of a gene encoding a thermostable cellobiose dehydrogenase from Myriococcum thermophilum. Prot. Expr. Purif. 59:258- 265.
    • (2008) Prot. Expr. Purif. , vol.59 , pp. 258-265
    • Zamocky, M.1
  • 46
    • 34247575628 scopus 로고    scopus 로고
    • An overview of the systematics of the Sordariomycetes based on a four-gene phylogeny
    • Zhang, N., et al. 2006. An overview of the systematics of the Sordariomycetes based on a four-gene phylogeny. Mycologia 98:1076-1087.
    • (2006) Mycologia , vol.98 , pp. 1076-1087
    • Zhang, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.