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Volumn 6, Issue 1, 2013, Pages

Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes

Author keywords

CAZy database; Evolution of lignocellulose breakdown; Ligninolytic enzymes; Lytic polysaccharide monooxygenases

Indexed keywords

CARBOHYDRATE ESTERASE; CARBOHYDRATE-BINDING MODULES; COMPLEX CARBOHYDRATES; EVOLUTION OF LIGNOCELLULOSE BREAKDOWN; GLYCOSIDE HYDROLASES; LIGNINOLYTIC ENZYMES; LIGNOCELLULOSE CONVERSIONS; MONOOXYGENASES;

EID: 84875193804     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-41     Document Type: Article
Times cited : (944)

References (82)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • 1747104
    • A classification of glycosyl hydrolases based on amino acid sequence similarities. Henrissat B, Biochem J 1991 280 309 316 1747104
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases [1]
    • Updating the sequence-based classification of glycosyl hydrolases. Henrissat B, Bairoch A, Biochem J 1996 316 695 696 8687420 (Pubitemid 26182174)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 3
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • 10.1093/nar/gkn663 18838391
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B, Nucleic Acids Res 2009 37 233 D238 10.1093/nar/gkn663 18838391
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 4
    • 67649799362 scopus 로고    scopus 로고
    • Microbial degradation of lignin: How a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this
    • 10.1111/j.1751-7915.2008.00078.x 21261911
    • Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this. Ruiz-Dueñas FJ, Martínez AT, Microb Biotechnol 2009 2 164 177 10.1111/j.1751-7915.2008.00078.x 21261911
    • (2009) Microb Biotechnol , vol.2 , pp. 164-177
    • Ruiz-Dueñas, F.J.1    Martínez, A.T.2
  • 9
    • 84855912007 scopus 로고    scopus 로고
    • Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
    • 10.1021/ja210657t 22188218
    • Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. Beeson WT, Phillips CM, Cate JH, Marletta MA, J Am Chem Soc 2012 134 890 892 10.1021/ja210657t 22188218
    • (2012) J Am Chem Soc , vol.134 , pp. 890-892
    • Beeson, W.T.1    Phillips, C.M.2    Cate, J.H.3    Marletta, M.A.4
  • 10
    • 84861987031 scopus 로고    scopus 로고
    • Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases
    • 10.1016/j.str.2012.04.002 22578542
    • Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Li X, Beeson WT, Phillips CM, Marletta MA, Cate JHD, Structure 2012 20 1051 1061 10.1016/j.str.2012.04.002 22578542
    • (2012) Structure , vol.20 , pp. 1051-1061
    • Li, X.1    Beeson, W.T.2    Phillips, C.M.3    Marletta, M.A.4    Cate, J.H.D.5
  • 11
    • 84871874790 scopus 로고    scopus 로고
    • Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) fromPodospora anserina
    • 10.1128/AEM.02942-12 23124232
    • Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina. Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC, Appl Environ Microbiol 2013 79 488 496 10.1128/AEM.02942-12 23124232
    • (2013) Appl Environ Microbiol , vol.79 , pp. 488-496
    • Bey, M.1    Zhou, S.2    Poidevin, L.3    Henrissat, B.4    Coutinho, P.M.5    Berrin, J.G.6    Sigoillot, J.C.7
  • 13
    • 84860351767 scopus 로고
    • Cloning, expression, and characterization of a cellobiose dehydrogenase from Thielavia terrestris induced under cellulose growth conditions
    • Cloning, expression, and characterization of a cellobiose dehydrogenase from Thielavia terrestris induced under cellulose growth conditions. Langston JA, Brown K, Xu F, Borch K, Garner A, Sweeney MD, Biochim Biophys Acta 1824 2012 802 812
    • (1824) Biochim Biophys Acta , vol.2012 , pp. 802-812
    • Langston, J.A.1    Brown, K.2    Xu, F.3    Borch, K.4    Garner, A.5    Sweeney, M.D.6
  • 14
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • 10.1021/cb200351y 22004347
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. Phillips CM, Beeson WT, Cate JH, Marletta MA, ACS Chem Biol 2011 6 1399 1406 10.1021/cb200351y 22004347
    • (2011) ACS Chem Biol , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 15
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • DOI 10.1074/jbc.M504468200
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. Vaaje-Kolstad G, Horn SJ, van Aalten DMF, Synstad B, Eijsink VGH, J Biol Chem 2005 280 28492 28497 10.1074/jbc.M504468200 15929981 (Pubitemid 41105749)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Van Aalten, D.M.F.3    Synstad, B.4    Eijsink, V.G.H.5
  • 16
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • 10.1126/science.1192231 20929773
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Vaaje-Kolstad G, Westereng B, Horn SJ, Liu ZL, Zhai H, Sørlie M, Eijsink VGH, Science 2010 330 219 222 10.1126/science.1192231 20929773
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1    Westereng, B.2    Horn, S.J.3    Liu, Z.L.4    Zhai, H.5    Sørlie, M.6    Eijsink, V.G.H.7
  • 18
    • 84856500612 scopus 로고    scopus 로고
    • Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme
    • 10.1016/j.jmb.2011.12.033 22210154
    • Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme. Vaaje-Kolstad G, Bøhle LA, Gåseidnes S, Dalhus B, Bjørås M, Mathiesen G, Eijsink VG, J Mol Biol 2012 416 239 254 10.1016/j.jmb.2011.12.033 22210154
    • (2012) J Mol Biol , vol.416 , pp. 239-254
    • Vaaje-Kolstad, G.1    Bøhle, L.A.2    Gåseidnes, S.3    Dalhus, B.4    Bjørås, M.5    Mathiesen, G.6    Eijsink, V.G.7
  • 19
    • 84869205445 scopus 로고    scopus 로고
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
    • 10.1073/pnas.1208822109 23112164
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Aachmann FL, Sørlie M, Skjåk-Bræk G, Eijsink VG, Vaaje-Kolstad G, Proc Natl Acad Sci U S A 2012 109 18779 18784 10.1073/pnas.1208822109 23112164
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 18779-18784
    • Aachmann, F.L.1    Sørlie, M.2    Skjåk-Bræk, G.3    Eijsink, V.G.4    Vaaje-Kolstad, G.5
  • 20
    • 84857193370 scopus 로고    scopus 로고
    • Genome analyses highlight the different biological roles of cellulases
    • 10.1038/nrmicro2729 22266780
    • Genome analyses highlight the different biological roles of cellulases. Mba Medie F, Davies GJ, Drancourt M, Henrissat B, Nat Rev Microbiol 2012 10 227 234 10.1038/nrmicro2729 22266780
    • (2012) Nat Rev Microbiol , vol.10 , pp. 227-234
    • Mba Medie, F.1    Davies, G.J.2    Drancourt, M.3    Henrissat, B.4
  • 21
    • 0034629232 scopus 로고    scopus 로고
    • A critical review of cellobiose dehydrogenases
    • DOI 10.1016/S0168-1656(00)00206-6, PII S0168165600002066
    • A critical review of cellobiose dehydrogenases. Henriksson G, Johansson G, Pettersson G, J Biotechnol 2000 78 93 113 10.1016/S0168-1656(00)00206-6 10725534 (Pubitemid 30139553)
    • (2000) Journal of Biotechnology , vol.78 , Issue.2 , pp. 93-113
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 22
    • 41649104638 scopus 로고    scopus 로고
    • FOLy: An integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds
    • DOI 10.1016/j.fgb.2008.01.004, PII S1087184508000066
    • FOLy: an integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds. Levasseur A, Piumi F, Coutinho PM, Rancurel C, Asther M, Delattre M, Henrissat B, Pontarotti P, Asther M, Record E, Fungal Genet Biol 2008 45 638 645 10.1016/j.fgb.2008.01.004 18308593 (Pubitemid 351484262)
    • (2008) Fungal Genetics and Biology , vol.45 , Issue.5 , pp. 638-645
    • Levasseur, A.1    Piumi, F.2    Coutinho, P.M.3    Rancurel, C.4    Asther, M.5    Delattre, M.6    Henrissat, B.7    Pontarotti, P.8    Asther, M.9    Record, E.10
  • 23
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases - Occurrence and properties
    • 10.1111/j.1574-4976.2005.00010.x 16472305
    • Fungal laccases-occurrence and properties. Baldrian P, FEMS Microbiol Rev 2006 30 215 242 10.1111/j.1574-4976.2005.00010.x 16472305
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 24
    • 77956961683 scopus 로고    scopus 로고
    • Laccases and their natural mediators: Biotechnological tools for sustainable eco-friendly processes
    • 10.1016/j.biotechadv.2010.05.002 20471466
    • Laccases and their natural mediators: biotechnological tools for sustainable eco-friendly processes. Cañas AI, Camarero S, Biotechnol Adv 2010 28 694 705 10.1016/j.biotechadv.2010.05.002 20471466
    • (2010) Biotechnol Adv , vol.28 , pp. 694-705
    • Cañas, A.I.1    Camarero, S.2
  • 25
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • 10.1016/0092-8674(94)90346-8 8293473
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Askwith C, Eide D, Van Ho A, Bernard PS, Li L, Davis-Kaplan S, Sipe DM, Kaplan J, Cell 1994 76 403 410 10.1016/0092-8674(94) 90346-8 8293473
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Van Ho, A.3    Bernard, P.S.4    Li, L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 26
    • 0037341361 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in fungi
    • DOI 10.1046/j.1365-2958.2003.03368.x
    • Molecular mechanisms of iron uptake in fungi. Kosman DJ, Mol Microbiol 2003 47 1185 1197 10.1046/j.1365-2958.2003.03368.x 12603727 (Pubitemid 36307846)
    • (2003) Molecular Microbiology , vol.47 , Issue.5 , pp. 1185-1197
    • Kosman, D.J.1
  • 27
    • 33845956242 scopus 로고    scopus 로고
    • Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium
    • DOI 10.1016/j.fgb.2006.07.007, PII S1087184506001393
    • Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium. Kersten P, Cullen D, Fungal Genet Biol 2007 44 77 87 10.1016/j.fgb.2006.07.007 16971147 (Pubitemid 46038784)
    • (2007) Fungal Genetics and Biology , vol.44 , Issue.2 , pp. 77-87
    • Kersten, P.1    Cullen, D.2
  • 28
    • 77955777240 scopus 로고    scopus 로고
    • Exploring laccase-like multicopper oxidase genes from the ascomycete Trichoderma reesei: A functional, phylogenetic and evolutionary study
    • 10.1186/1471-2091-11-32 20735824
    • Exploring laccase-like multicopper oxidase genes from the ascomycete Trichoderma reesei: a functional, phylogenetic and evolutionary study. Levasseur A, Saloheimo M, Navarro D, Andberg M, Pontarotti P, Kruus K, Record E, BMC Biochem 2010 11 32 10.1186/1471-2091-11-32 20735824
    • (2010) BMC Biochem , vol.11 , pp. 32
    • Levasseur, A.1    Saloheimo, M.2    Navarro, D.3    Andberg, M.4    Pontarotti, P.5    Kruus, K.6    Record, E.7
  • 29
    • 0041370188 scopus 로고    scopus 로고
    • Extracellular laccases in ascomycetes Trichoderma atroviride and Trichoderma harzianum
    • Extracellular laccases in ascomycetes Trichoderma atroviride and Trichoderma harzianum. Hölker U, Dohse J, Höfer M, Folia Microbiol 2002 47 423 427 10.1007/BF02818702 (Pubitemid 135695745)
    • (2002) Folia Microbiologica , vol.47 , Issue.4 , pp. 423-427
    • Holker, U.1    Dohse, J.2    Hofer, M.3
  • 31
    • 77049096911 scopus 로고    scopus 로고
    • Lignin-modifying enzymes in filamentous basidiomycetes-ecological, functional and phylogenetic review
    • 10.1002/jobm.200900338 20175122
    • Lignin-modifying enzymes in filamentous basidiomycetes-ecological, functional and phylogenetic review. Lundell TK, Mäkelä MR, Hildén K, J Basic Microbiol 2010 50 5 20 10.1002/jobm.200900338 20175122
    • (2010) J Basic Microbiol , vol.50 , pp. 5-20
    • Lundell, T.K.1    Mäkelä, M.R.2    Hildén, K.3
  • 32
    • 77954296079 scopus 로고    scopus 로고
    • New and classic families of secreted fungal heme peroxidases
    • 10.1007/s00253-010-2633-0 20495915
    • New and classic families of secreted fungal heme peroxidases. Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T, Appl Microbiol Biotechnol 2010 87 871 897 10.1007/s00253-010-2633-0 20495915
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 871-897
    • Hofrichter, M.1    Ullrich, R.2    Pecyna, M.J.3    Liers, C.4    Lundell, T.5
  • 33
    • 0026544690 scopus 로고
    • GMC oxidoreductases - A newly defined family of homologous proteins with diverse catalytic activities
    • 10.1016/0022-2836(92)90992-S 1542121
    • GMC oxidoreductases-a newly defined family of homologous proteins with diverse catalytic activities. Cavener DR, J Mol Biol 1992 223 811 814 10.1016/0022-2836(92)90992-S 1542121
    • (1992) J Mol Biol , vol.223 , pp. 811-814
    • Cavener, D.R.1
  • 34
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase - A flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • DOI 10.2174/138920306777452367
    • Cellobiose dehydrogenase- a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Zámocký M, Ludwig R, Peterbauer C, Hallberg BM, Divne C, Nicholls P, Haltrich D, Curr Protein Pept Sci 2006 7 255 280 10.2174/138920306777452367 16787264 (Pubitemid 43881007)
    • (2006) Current Protein and Peptide Science , vol.7 , Issue.3 , pp. 255-280
    • Zamocky, M.1    Ludwig, R.2    Peterbauer, C.3    Hallberg, B.M.4    Divne, C.5    Nicholls, P.6    Haltrich, D.7
  • 35
    • 0026596230 scopus 로고
    • Cellobiose oxidase from Phanerochaete chrysosporium as a source of Fenton's reagent
    • 1327893
    • Cellobiose oxidase from Phanerochaete chrysosporium as a source of Fenton's reagent. Kremer SM, Wood PM, Biochem Soc Trans 1992 20 110S 1327893
    • (1992) Biochem Soc Trans , vol.20
    • Kremer, S.M.1    Wood, P.M.2
  • 36
    • 84878016423 scopus 로고    scopus 로고
    • Heterologous production of cellobiose dehydrogenases from the basidiomycete Coprinopsis cinerea and the ascomycete Podospora anserina and their effect on saccharification of wheat straw
    • In press
    • Heterologous production of cellobiose dehydrogenases from the basidiomycete Coprinopsis cinerea and the ascomycete Podospora anserina and their effect on saccharification of wheat straw. Turbe-Doan A, Arfi Y, Record E, Estrada-Alvarado I, Levasseur A, Appl Microbiol Biotechnol 2012 In press
    • (2012) Appl Microbiol Biotechnol
    • Turbe-Doan, A.1    Arfi, Y.2    Record, E.3    Estrada-Alvarado, I.4    Levasseur, A.5
  • 37
    • 4143089527 scopus 로고    scopus 로고
    • Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi
    • DOI 10.1016/j.gene.2004.04.025, PII S0378111904002495
    • Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi. Zámocký M, Hallberg M, Ludwig R, Divne C, Haltrich D, Gene 2004 338 1 14 10.1016/j.gene.2004.04.025 15302401 (Pubitemid 39092406)
    • (2004) Gene , vol.338 , Issue.1 , pp. 1-14
    • Zamocky, M.1    Hallberg, M.2    Ludwig, R.3    Divne, C.4    Haltrich, D.5
  • 38
    • 84857914934 scopus 로고    scopus 로고
    • Fungal aryl-alcohol oxidase: A peroxide-producing flavoenzyme involved in lignin degradation
    • 10.1007/s00253-011-3836-8 22249717
    • Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation. Hernández-Ortega A, Ferreira P, Martínez AT, Appl Microbiol Biotechnol 2012 93 1395 1410 10.1007/s00253-011-3836-8 22249717
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 1395-1410
    • Hernández-Ortega, A.1    Ferreira, P.2    Martínez, A.T.3
  • 40
    • 0022572161 scopus 로고
    • 2 producing enzyme in Phanerochaete chrysosporium
    • Formation and partial characterization of glucose-2-oxidase, a H§ssub§2§esub§O§ssub§2§esub§ producing enzyme in Phanerochaete chrysosporium. Eriksson KE, Pettersson B, Volc J, Musílek V, Appl Microbiol Biotechnol 1986 23 257 262 (Pubitemid 16150848)
    • (1986) Applied Microbiology and Biotechnology , vol.23 , Issue.3-4 , pp. 257-262
    • Eriksson, K.E.1    Pettersson, B.2    Volc, J.3    Musilek, V.4
  • 41
    • 35148832513 scopus 로고    scopus 로고
    • 2 in brown rot decay of wood
    • DOI 10.1128/AEM.00977-07
    • Characteristics of Gloeophyllum trabeum alcohol oxidase, an extracellular source of H§ssub§2§esub§O§ssub§2§esub§ in brown rot decay of wood. Daniel G, Volc J, Filonova L, Plihal O, Kubátová E, Halada P, Appl Environ Microbiol 2007 73 6241 6253 10.1128/AEM.00977-07 17660304 (Pubitemid 47548035)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.19 , pp. 6241-6253
    • Daniel, G.1    Volc, J.2    Filonova, L.3    Plihal, O.4    Kubatova, E.5    Halada, P.6
  • 42
    • 0034533834 scopus 로고    scopus 로고
    • Fungal pyranose oxidases: Occurrence, properties and biotechnical applications in carbohydrate chemistry
    • DOI 10.1007/s002530000446
    • Fungal pyranose oxidases: occurrence, properties and biotechnical applications in carbohydrate chemistry. Giffhorn F, Appl Microbiol Biotechnol 2000 54 727 740 10.1007/s002530000446 11152063 (Pubitemid 32009732)
    • (2000) Applied Microbiology and Biotechnology , vol.54 , Issue.6 , pp. 727-740
    • Giffhorn, F.1
  • 43
    • 0026665175 scopus 로고
    • Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD
    • 10.1111/j.1432-1033.1992.tb17231.x 1396672
    • Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD. de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA, Eur J Biochem 1992 208 651 657 10.1111/j.1432-1033.1992.tb17231.x 1396672
    • (1992) Eur J Biochem , vol.208 , pp. 651-657
    • De Jong, E.1    Van Berkel, W.J.2    Van Der Zwan, R.P.3    De Bont, J.A.4
  • 45
    • 33746040871 scopus 로고    scopus 로고
    • Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • DOI 10.1128/AEM.00375-06
    • Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium. Vanden Wymelenberg A, Sabat G, Mozuch M, Kersten PJ, Cullen D, Blanchette RA, Appl Environ Microbiol 2006 72 4871 4877 10.1128/AEM.00375-06 16820482 (Pubitemid 44078815)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.7 , pp. 4871-4877
    • Wymelenberg, A.V.1    Sabat, G.2    Mozuch, M.3    Kersten, P.J.4    Cullen, D.5    Blanchette, R.A.6
  • 46
    • 0038604805 scopus 로고    scopus 로고
    • Free radical catalysis by galactose oxidase
    • 10.1021/cr020425z 12797833
    • Free radical catalysis by galactose oxidase. Whittaker JW, Chem Rev 2003 103 2347 2363 10.1021/cr020425z 12797833
    • (2003) Chem Rev , vol.103 , pp. 2347-2363
    • Whittaker, J.W.1
  • 47
    • 0029153403 scopus 로고
    • Purification and characterization of a 1,4-Benzoquinone reductase from the basidiomycete Phanerochaete chrysosporium
    • 16535104
    • Purification and characterization of a 1,4-Benzoquinone reductase from the basidiomycete Phanerochaete chrysosporium. Brock BJ, Rieble S, Gold MH, Appl Environ Microbiol 1995 61 3076 3081 16535104
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3076-3081
    • Brock, B.J.1    Rieble, S.2    Gold, M.H.3
  • 48
    • 34548357017 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular NADH: Quinone reductase from Trametes versicolor
    • Purification and characterization of an intracellular NADH:quinone reductase from Trametes versicolor. Lee SS, Moon DS, Choi HT, Song HG, J Microbiol 2007 45 333 338 17846587 (Pubitemid 47347737)
    • (2007) Journal of Microbiology , vol.45 , Issue.4 , pp. 333-338
    • Lee, S.-S.1    Moon, D.-S.2    Choi, H.T.3    Song, H.-G.4
  • 49
    • 0036269033 scopus 로고    scopus 로고
    • An NADH: Quinone oxidoreductase active during biodegradation by the brown-rot basidiomycete Gloeophyllum trabeum
    • DOI 10.1128/AEM.68.6.2699-2703.2002
    • An NADH:quinone oxidoreductase active during biodegradation by the brown-rot basidiomycete Gloeophyllum trabeum. Jensen K Jr, Ryan Z, Wymelenberg A, Cullen D, Hammel K, Appl Environ Microbiol 2002 68 2699 2703 10.1128/AEM.68.6.2699-2703.2002 12039722 (Pubitemid 34601988)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.6 , pp. 2699-2703
    • Jensen Jr., K.A.1    Ryan, Z.C.2    Wymelenberg, A.V.3    Cullen, D.4    Hammel, K.E.5
  • 50
    • 0034690303 scopus 로고    scopus 로고
    • Characterization of kinetics and thermostability of Acremonium strictum glucooligosaccharide oxidase
    • DOI 10.1002/(SICI)1097-0290(20000420)68:2<231::AID-BIT12>3.0.CO;2-D
    • Characterization of kinetics and thermostability of Acremonium strictum glucooligosaccharide oxidase. Fan Z, Oguntimein GB, Reilly PJ, Biotechnol Bioeng 2000 68 231 237 10.1002/(SICI)1097-0290(20000420)68:2<231::AID-BIT12>3.0. CO;2-D 10712739 (Pubitemid 30194049)
    • (2000) Biotechnology and Bioengineering , vol.68 , Issue.2 , pp. 231-237
    • Fan, Z.1    Oguntimein, G.B.2    Reilly, P.J.3
  • 51
    • 0027324150 scopus 로고
    • Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
    • DOI 10.1016/0005-2728(93)90171-B
    • Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase? Henriksson G, Johansson G, Pettersson G, Biochim Biophys Acta 1993 1144 184 190 10.1016/0005-2728(93)90171-B 8369336 (Pubitemid 23271338)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1144 , Issue.2 , pp. 184-190
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 56
    • 0345161806 scopus 로고    scopus 로고
    • Generation of evolutionary novelty by functional shift
    • Generation of evolutionary novelty by functional shift. Ganfornina MD, Sanchez D, Bioessays 1999 21 432 439 10.1002/(SICI)1521-1878(199905)21:5<432: :AID-BIES10>3.0.CO;2-T 10376014 (Pubitemid 29223315)
    • (1999) BioEssays , vol.21 , Issue.5 , pp. 432-439
    • Ganfornina, M.D.1    Sanchez, D.2
  • 57
    • 0345306751 scopus 로고    scopus 로고
    • The Origins of Genome Complexity
    • DOI 10.1126/science.1089370
    • The origins of genome complexity. Lynch M, Conery JS, Science 2003 302 1401 1404 10.1126/science.1089370 14631042 (Pubitemid 37452183)
    • (2003) Science , vol.302 , Issue.5649 , pp. 1401-1404
    • Lynch, M.1    Conery, J.S.2
  • 58
    • 79951559649 scopus 로고    scopus 로고
    • The role of duplications in the evolution of genomes highlights the need for evolutionary-based approaches in comparative genomics
    • 10.1186/1745-6150-6-11 21333002
    • The role of duplications in the evolution of genomes highlights the need for evolutionary-based approaches in comparative genomics. Levasseur A, Pontarotti P, Biol Direct 2011 6 11 10.1186/1745-6150-6-11 21333002
    • (2011) Biol Direct , vol.6 , pp. 11
    • Levasseur, A.1    Pontarotti, P.2
  • 59
    • 35349010004 scopus 로고    scopus 로고
    • Conceptual bases for quantifying the role of the environment on gene evolution: The participation of positive selection and neutral evolution
    • DOI 10.1111/j.1469-185X.2007.00024.x
    • Conceptual bases for quantifying the role of the environment on gene evolution: the participation of positive selection and neutral evolution. Levasseur A, Orlando L, Bailly X, Milinkovitch MC, Danchin EG, Pontarotti P, Biol Rev Camb Philos Soc 2007 82 551 572 10.1111/j.1469-185X.2007.00024.x 17944617 (Pubitemid 47609919)
    • (2007) Biological Reviews , vol.82 , Issue.4 , pp. 551-572
    • Levasseur, A.1    Orlando, L.2    Bailly, X.3    Milinkovitch, M.C.4    Danchin, E.G.J.5    Pontarotti, P.6
  • 62
    • 0033738805 scopus 로고    scopus 로고
    • Role of horizontal gene transfer in the evolution of fungi
    • 10.1146/annurev.phyto.38.1.325 11701846
    • Role of horizontal gene transfer in the evolution of fungi. Rosewich UL, Kistler HC, Annu Rev Phytopathol 2000 38 325 363 10.1146/annurev.phyto.38.1.325 11701846
    • (2000) Annu Rev Phytopathol , vol.38 , pp. 325-363
    • Rosewich, U.L.1    Kistler, H.C.2
  • 64
    • 0037117789 scopus 로고    scopus 로고
    • Molecular biology and structure-function of lignin-degrading heme peroxidases
    • DOI 10.1016/S0141-0229(01)00521-X, PII S014102290100521X
    • Molecular biology and structure-function of lignin-degrading heme peroxidases. Martinez AT, Enzym Microb Technol 2002 30 425 444 10.1016/S0141-0229(01)00521-X (Pubitemid 34310267)
    • (2002) Enzyme and Microbial Technology , vol.30 , Issue.4 , pp. 425-444
    • Martinez, A.T.1
  • 66
    • 0035252395 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase - An extracellular fungal flavocytochrome
    • DOI 10.1016/S0141-0229(00)00307-0, PII S0141022900003070
    • Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Cameron MD, Aust SD, Enzyme Microb Technol 2001 28 129 138 10.1016/S0141-0229(00)00307- 0 11166803 (Pubitemid 32146630)
    • (2001) Enzyme and Microbial Technology , vol.28 , Issue.2-3 , pp. 129-138
    • Cameron, M.D.1    Aust, S.D.2
  • 68
    • 0034326823 scopus 로고    scopus 로고
    • Production of hydroxyl radical by the synergistic action of fungal laccase and aryl alcohol oxidase
    • 10.1006/abbi.2000.2053 11097187
    • Production of hydroxyl radical by the synergistic action of fungal laccase and aryl alcohol oxidase. Guillén F, Gómez-Toribio V, Martínez MJ, Martínez AT, Arch Biochem Biophys 2000 383 142 147 10.1006/abbi.2000.2053 11097187
    • (2000) Arch Biochem Biophys , vol.383 , pp. 142-147
    • Guillén, F.1    Gómez-Toribio, V.2    Martínez, M.J.3    Martínez, A.T.4
  • 69
    • 44449103132 scopus 로고    scopus 로고
    • Fungal laccase, cellobiose dehydrogenase, and chemical mediators: Combined actions for the decolorization of different classes of textile dyes
    • 10.1016/j.biortech.2008.01.019 18281211
    • Fungal laccase, cellobiose dehydrogenase, and chemical mediators: combined actions for the decolorization of different classes of textile dyes. Ciullini I, Tilli S, Scozzafava A, Briganti F, Bioresour Technol 2008 99 7003 7010 10.1016/j.biortech.2008.01.019 18281211
    • (2008) Bioresour Technol , vol.99 , pp. 7003-7010
    • Ciullini, I.1    Tilli, S.2    Scozzafava, A.3    Briganti, F.4
  • 70
    • 67649766455 scopus 로고    scopus 로고
    • Assessment of the joint effect of laccase and cellobiose dehydrogenase on the decolouration of different synthetic dyes
    • 10.1016/j.jhazmat.2009.03.088 19376643
    • Assessment of the joint effect of laccase and cellobiose dehydrogenase on the decolouration of different synthetic dyes. Enayatzamir K, Tabandeh F, Yakhchali B, Alikhani HA, Rodríguez Couto S, J Hazard Mater 2009 169 176 181 10.1016/j.jhazmat.2009.03.088 19376643
    • (2009) J Hazard Mater , vol.169 , pp. 176-181
    • Enayatzamir, K.1    Tabandeh, F.2    Yakhchali, B.3    Alikhani, H.A.4    Rodríguez Couto, S.5
  • 71
    • 80054695246 scopus 로고    scopus 로고
    • Differential decolorization of textile dyes in mixtures and the joint effect of laccase and cellobiose dehydrogenase activities present in extracellular extracts from Funalia trogii
    • 10.1016/j.enzmictec.2011.08.002 22112619
    • Differential decolorization of textile dyes in mixtures and the joint effect of laccase and cellobiose dehydrogenase activities present in extracellular extracts from Funalia trogii. Tilli S, Ciullini I, Scozzafava A, Briganti F, Enzyme Microb Technol 2011 49 465 471 10.1016/j.enzmictec.2011.08. 002 22112619
    • (2011) Enzyme Microb Technol , vol.49 , pp. 465-471
    • Tilli, S.1    Ciullini, I.2    Scozzafava, A.3    Briganti, F.4
  • 73
    • 0025380342 scopus 로고
    • Degradation of lignin by bacteria
    • Degradation of lignin by bacteria. Zimmermann W, J Biotechnol 1990 13 119 130 10.1016/0168-1656(90)90098-V (Pubitemid 20082671)
    • (1990) Journal of Biotechnology , vol.13 , Issue.2-3 , pp. 119-130
    • Zimmermann, W.1
  • 74
    • 79955761627 scopus 로고    scopus 로고
    • The emerging role for bacteria in lignin degradation and bio-product formation
    • 10.1016/j.copbio.2010.10.009 21071202
    • The emerging role for bacteria in lignin degradation and bio-product formation. Bugg TD, Ahmad M, Hardiman EM, Singh R, Curr Opin Biotechnol 2011 22 394 400 10.1016/j.copbio.2010.10.009 21071202
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 394-400
    • Bugg, T.D.1    Ahmad, M.2    Hardiman, E.M.3    Singh, R.4
  • 75
    • 33846485037 scopus 로고    scopus 로고
    • Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds
    • DOI 10.1271/bbb.60437
    • Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds. Masai E, Katayama Y, Fukuda M, Biosci Biotechnol Biochem 2007 71 1 15 10.1271/bbb.60437 17213657 (Pubitemid 46155140)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.1 , pp. 1-15
    • Masai, E.1    Katayama, Y.2    Fukuda, M.3
  • 76
    • 81355123362 scopus 로고    scopus 로고
    • Pathways for degradation of lignin in bacteria and fungi
    • 10.1039/c1np00042j 21918777
    • Pathways for degradation of lignin in bacteria and fungi. Bugg TD, Ahmad M, Hardiman EM, Rahmanpour R, Nat Prod Rep 2011 28 1883 1896 10.1039/c1np00042j 21918777
    • (2011) Nat Prod Rep , vol.28 , pp. 1883-1896
    • Bugg, T.D.1    Ahmad, M.2    Hardiman, E.M.3    Rahmanpour, R.4
  • 78
    • 26644450247 scopus 로고    scopus 로고
    • A high-throughput screening of genes that encode proteins transported into the endoplasmic reticulum in mammalian cells
    • DOI 10.1093/nar/gni032
    • GenBank. Benson DA, Karsch-Mizrachi I, Lipman DJ, Ostell J, Wheeler DL, Nucleic Acids Res 2005 33 34 D38 10.1093/nar/gni032 15608212 (Pubitemid 41439935)
    • (2005) Nucleic Acids Research , vol.33 , Issue.4 , pp. 1-9
    • Ozawa, T.1    Nishitani, K.2    Sako, Y.3    Umezawa, Y.4
  • 79
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins
    • DOI 10.1093/protein/gzl044
    • Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins. Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B, Protein Eng Des Sel 2006 19 555 562 10.1093/protein/gzl044 17085431 (Pubitemid 44950461)
    • (2006) Protein Engineering, Design and Selection , vol.19 , Issue.12 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.J.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 80
    • 78649868163 scopus 로고    scopus 로고
    • A hierarchical classification of polysaccharide lyases for glycogenomics
    • 10.1042/BJ20101185 20925655
    • A hierarchical classification of polysaccharide lyases for glycogenomics. Lombard V, Bernard T, Rancurel C, Brumer H, Coutinho PM, Henrissat B, Biochem J 2010 432 437 444 10.1042/BJ20101185 20925655
    • (2010) Biochem J , vol.432 , pp. 437-444
    • Lombard, V.1    Bernard, T.2    Rancurel, C.3    Brumer, H.4    Coutinho, P.M.5    Henrissat, B.6
  • 81
    • 84866500048 scopus 로고    scopus 로고
    • Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
    • 10.1186/1471-2148-12-186 22992189
    • Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5). Aspeborg H, Coutinho PM, Wang Y, Brumer H 3rd, Henrissat B, BMC Evol Biol 2012 12 186 10.1186/1471-2148-12-186 22992189
    • (2012) BMC Evol Biol , vol.12 , pp. 186
    • Aspeborg, H.1    Coutinho, P.M.2    Wang, Y.3    Brumer III, H.4    Henrissat, B.5


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