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Volumn 274, Issue 3, 2007, Pages 879-894

Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma

Author keywords

Covalent flavinylation; Lignocellulose degradation; Litter degrading fungi; Pyranose dehydrogenase

Indexed keywords

AMINO ACID; AMMONIUM SULFATE; BENZOQUINONE; CARBOHYDRATE; CASPASE; CATION; GALACTOSE; GLUCOSE; GLUCOSE OXIDASE; GLUCOSIDE; GLYCOPROTEIN; HISTIDINE DERIVATIVE; ISOMERASE; LIGNOCELLULOSE; METAL ION; MONOMER; MONOSACCHARIDE; OLIGOSACCHARIDE; OXIDOREDUCTASE; POLYPEPTIDE; PYRANOSE DEHYDROGENASE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33846425319     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05634.x     Document Type: Article
Times cited : (38)

References (51)
  • 2
    • 0032519818 scopus 로고    scopus 로고
    • Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases
    • Kiess M, Hecht HJ & Kalisz HM (1998) Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases. Eur J Biochem 252, 90-99.
    • (1998) Eur J Biochem , vol.252 , pp. 90-99
    • Kiess, M.1    Hecht, H.J.2    Kalisz, H.M.3
  • 3
    • 0030937674 scopus 로고    scopus 로고
    • Characterization of hexose oxidase from the red seaweed Chondrus crispus
    • Groen BW, De Vries S & Duine JA (1997) Characterization of hexose oxidase from the red seaweed Chondrus crispus. Eur J Biochem 244, 858-861.
    • (1997) Eur J Biochem , vol.244 , pp. 858-861
    • Groen, B.W.1    De Vries, S.2    Duine, J.A.3
  • 5
    • 33644689024 scopus 로고    scopus 로고
    • Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: A novel flavinylation of 6-S-cysteinyl, 8α-N1-histidyl FAD
    • Huang CH, Lai WL, Lee MH, Chen CJ, Vasella A, Tsai YC & Liaw SH (2005) Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8α-N1-histidyl FAD. J Biol Chem 280, 38831-38838.
    • (2005) J Biol Chem , vol.280 , pp. 38831-38838
    • Huang, C.H.1    Lai, W.L.2    Lee, M.H.3    Chen, C.J.4    Vasella, A.5    Tsai, Y.C.6    Liaw, S.H.7
  • 6
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg BM, Henriksson G, Pettersson G & Divne C (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
  • 8
    • 0035430520 scopus 로고    scopus 로고
    • Purification and characterization of pyranose oxidase from the white-rot fungus Trametes multicolor
    • Leitner C, Volc J & Haltrich D (2001) Purification and characterization of pyranose oxidase from the white-rot fungus Trametes multicolor. Appl Environ Microbiol 67, 3636-3644.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3636-3644
    • Leitner, C.1    Volc, J.2    Haltrich, D.3
  • 9
    • 4344582358 scopus 로고    scopus 로고
    • Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase
    • Hallberg BM, Leitner C, Haltrich D & Divne C (2004) Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase. J Mol Biol 341, 781-796.
    • (2004) J Mol Biol , vol.341 , pp. 781-796
    • Hallberg, B.M.1    Leitner, C.2    Haltrich, D.3    Divne, C.4
  • 10
    • 33846442623 scopus 로고    scopus 로고
    • Amperometric biosensors for detection of sugars based on the electrical wiring of different pyranose oxidases and pyranose dehydrogenases with osmium redox polymers on graphite electrodes
    • in press
    • Tasca F, Timur S, Ludwig R, Kittl R, Haltrich D, Volc J, Antiochia R & Gorton L (2007) Amperometric biosensors for detection of sugars based on the electrical wiring of different pyranose oxidases and pyranose dehydrogenases with osmium redox polymers on graphite electrodes. Electroanalysis, in press.
    • (2007) Electroanalysis
    • Tasca, F.1    Timur, S.2    Ludwig, R.3    Kittl, R.4    Haltrich, D.5    Volc, J.6    Antiochia, R.7    Gorton, L.8
  • 11
    • 0034533834 scopus 로고    scopus 로고
    • Fungal pyranose oxidases: Occurrence, properties and biotechnical applications in carbohydrate chemistry
    • Giffhorn F (2000) Fungal pyranose oxidases: occurrence, properties and biotechnical applications in carbohydrate chemistry. Appl Microbiol Biotechnol 54, 727-740.
    • (2000) Appl Microbiol Biotechnol , vol.54 , pp. 727-740
    • Giffhorn, F.1
  • 12
    • 0030979941 scopus 로고    scopus 로고
    • Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus
    • Volc J, Kubátová E, Wood DA & Daniel G (1997) Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus. Arch Microbiol 167, 119-125.
    • (1997) Arch Microbiol , vol.167 , pp. 119-125
    • Volc, J.1    Kubátová, E.2    Wood, D.A.3    Daniel, G.4
  • 13
    • 0034890010 scopus 로고    scopus 로고
    • Screening of basidiomycete fungi for the quinone dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase and properties of the enzyme from Macrolepiota rhacodes
    • Volc J, Kubátová E, Daniel G, Sedmera P & Haltrich D (2001) Screening of basidiomycete fungi for the quinone dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase and properties of the enzyme from Macrolepiota rhacodes. Arch Microbiol 176, 178-186.
    • (2001) Arch Microbiol , vol.176 , pp. 178-186
    • Volc, J.1    Kubátová, E.2    Daniel, G.3    Sedmera, P.4    Haltrich, D.5
  • 14
    • 3042836537 scopus 로고    scopus 로고
    • Conversion of lactose to β-D-galactopyranosyl- (1→4)-D-arabino-hexos-2-ulose (2-dehydrolactose) and lactobiono-1,5-lactone by fungal pyranose dehydrogenase
    • Volc J, Sedmera P, Kujawa M, Halada P, Kubátová E & Haltrich D (2004) Conversion of lactose to β-D-galactopyranosyl- (1→4)-D-arabino-hexos-2-ulose (2-dehydrolactose) and lactobiono-1,5-lactone by fungal pyranose dehydrogenase. J Mol Catal B 30, 177-184.
    • (2004) J Mol Catal B , vol.30 , pp. 177-184
    • Volc, J.1    Sedmera, P.2    Kujawa, M.3    Halada, P.4    Kubátová, E.5    Haltrich, D.6
  • 15
    • 7044235562 scopus 로고    scopus 로고
    • A new enzyme catalysis: 3,4-dioxidation of some aryl β-D-glycopyranosides by fungal pyranose dehydrogenase
    • Sedmera P, Halada P, Peterbauer C & Volc J (2004) A new enzyme catalysis: 3,4-dioxidation of some aryl β-D-glycopyranosides by fungal pyranose dehydrogenase. Tetrahedron Lett 45, 8677-8680.
    • (2004) Tetrahedron Lett , vol.45 , pp. 8677-8680
    • Sedmera, P.1    Halada, P.2    Peterbauer, C.3    Volc, J.4
  • 16
    • 33745154878 scopus 로고    scopus 로고
    • New biotransformation of some reducing sugars to the corresponding (di) dehydro (glycosyl) aldoses or alduronic acids using fungal pyranose dehydrogenase
    • Sedmera P, Halada P, Kubátová E, Haltrich D, Prikrylová V & Volc J (2006) New biotransformation of some reducing sugars to the corresponding (di) dehydro (glycosyl) aldoses or alduronic acids using fungal pyranose dehydrogenase. J Mol Catal B 41, 32-42.
    • (2006) J Mol Catal B , vol.41 , pp. 32-42
    • Sedmera, P.1    Halada, P.2    Kubátová, E.3    Haltrich, D.4    Prikrylová, V.5    Volc, J.6
  • 17
    • 12244253706 scopus 로고    scopus 로고
    • Identification of the covalent flavin adenine dinucleotide-binding region in pyranose 2-oxidase from Trametes multicolor
    • Halada P, Leitner C, Sedmera P, Haltrich D & Volc J (2003) Identification of the covalent flavin adenine dinucleotide-binding region in pyranose 2-oxidase from Trametes multicolor. Anal Biochem 314, 235-242.
    • (2003) Anal Biochem , vol.314 , pp. 235-242
    • Halada, P.1    Leitner, C.2    Sedmera, P.3    Haltrich, D.4    Volc, J.5
  • 18
    • 0032900941 scopus 로고    scopus 로고
    • Characterization of a glucose 3-dehydrogenase from the cultivated mushroom (Agaricus bisporus)
    • Morrison SC, Wood DA & Wood PM (1999) Characterization of a glucose 3-dehydrogenase from the cultivated mushroom (Agaricus bisporus). Appl Microbiol Biotechnol 51, 58-64.
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 58-64
    • Morrison, S.C.1    Wood, D.A.2    Wood, P.M.3
  • 19
    • 0031006631 scopus 로고    scopus 로고
    • Pyranose 2-oxidase from Phanerochaete chrysosporium: Further biochemical characterisation
    • Artolozaga MJ, Kubátová E, Volc J & Kalisz HM (1997) Pyranose 2-oxidase from Phanerochaete chrysosporium: further biochemical characterisation. Appl Microbiol Biotechnol 47, 508-514.
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 508-514
    • Artolozaga, M.J.1    Kubátová, E.2    Volc, J.3    Kalisz, H.M.4
  • 20
    • 0031742179 scopus 로고    scopus 로고
    • Rare keto-aldoses from enzymatic oxidation: Substrates and oxidation products of pyranose 2-oxidase
    • Freimund S, Huwig A, Giffhorn F & Köpper S (1998) Rare keto-aldoses from enzymatic oxidation: substrates and oxidation products of pyranose 2-oxidase. Chem Eur J 4, 2442-2455.
    • (1998) Chem Eur J , vol.4 , pp. 2442-2455
    • Freimund, S.1    Huwig, A.2    Giffhorn, F.3    Köpper, S.4
  • 21
    • 0037171621 scopus 로고    scopus 로고
    • C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: Spectral characterization
    • Volc J, Sedmera P, Halada P, Daniel G, Prikrylová V & Haltrich D (2002) C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization. J Mol Catal B 17, 91-100.
    • (2002) J Mol Catal B , vol.17 , pp. 91-100
    • Volc, J.1    Sedmera, P.2    Halada, P.3    Daniel, G.4    Prikrylová, V.5    Haltrich, D.6
  • 22
    • 84972808957 scopus 로고
    • The isomeric composition of D-ribo-hexos-3-ulose (3-keto-D-glucose) in aqueous solution
    • Morris PEJ, Hope KD & Kiely EE (1989) The isomeric composition of D-ribo-hexos-3-ulose (3-keto-D-glucose) in aqueous solution. J Carbohydr Chem 8, 515-530.
    • (1989) J Carbohydr Chem , vol.8 , pp. 515-530
    • Morris, P.E.J.1    Hope, K.D.2    Kiely, E.E.3
  • 23
    • 0037184280 scopus 로고    scopus 로고
    • Enzymatic synthesis of D-glucosone 6-phosphate (D-arabino-hexos-2-ulose 6-(dihydrogen phosphate) and NMR analysis of its isomeric forms
    • Freimund S, Baldes L, Huwig A & Giffhorn F (2002) Enzymatic synthesis of D-glucosone 6-phosphate (D-arabino-hexos-2-ulose 6-(dihydrogen phosphate) and NMR analysis of its isomeric forms. Carbohydr Res 337, 1585-1587.
    • (2002) Carbohydr Res , vol.337 , pp. 1585-1587
    • Freimund, S.1    Baldes, L.2    Huwig, A.3    Giffhorn, F.4
  • 24
    • 0031044867 scopus 로고    scopus 로고
    • Structural analysis of crystalline D-erythro-hexos-2,3-diulose (2,3-diketo-D-glucose) prepared enzymatically from D-glucose
    • Sedmera P, Volc J, Havlícek V, Pakhomova S & Jegorov A (1997) Structural analysis of crystalline D-erythro-hexos-2,3-diulose (2,3-diketo-D-glucose) prepared enzymatically from D-glucose. Carbohydr Res 297, 375-378.
    • (1997) Carbohydr Res , vol.297 , pp. 375-378
    • Sedmera, P.1    Volc, J.2    Havlícek, V.3    Pakhomova, S.4    Jegorov, A.5
  • 25
    • 0037254394 scopus 로고    scopus 로고
    • The composition of keto aldoses in aqueous solution as determined by NMR spectroscopy
    • Köpper S & Freimund S (2003) The composition of keto aldoses in aqueous solution as determined by NMR spectroscopy. Helv Chim Acta 86, 827-843.
    • (2003) Helv Chim Acta , vol.86 , pp. 827-843
    • Köpper, S.1    Freimund, S.2
  • 28
    • 0030921453 scopus 로고    scopus 로고
    • Involvement of a flavin iminoquinone methide in the formation of 6-hydroxyflavin mononucleotide in trimethylamine dehydrogenase: A rationale for the existence of 8α-methyl and C6-linked covalent flavoproteins
    • Mewies M, Basran J, Packman LC, Hille R & Scrutton NS (1997) Involvement of a flavin iminoquinone methide in the formation of 6-hydroxyflavin mononucleotide in trimethylamine dehydrogenase: a rationale for the existence of 8α-methyl and C6-linked covalent flavoproteins. Biochemistry 36, 7162-7168.
    • (1997) Biochemistry , vol.36 , pp. 7162-7168
    • Mewies, M.1    Basran, J.2    Packman, L.C.3    Hille, R.4    Scrutton, N.S.5
  • 29
    • 0034655736 scopus 로고    scopus 로고
    • Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of β-D-glucose
    • Witt S, Wohlfahrt G, Schomburg D, Hecht HJ & Kalisz HM (2000) Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of β-D-glucose. Biochem J 347, 553-559.
    • (2000) Biochem J , vol.347 , pp. 553-559
    • Witt, S.1    Wohlfahrt, G.2    Schomburg, D.3    Hecht, H.J.4    Kalisz, H.M.5
  • 30
    • 0031663962 scopus 로고    scopus 로고
    • C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus
    • Volc J, Sedmera P, Halada P, Prikrylová V & Daniel G (1998) C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus. Carbohydr Res 310, 151-156.
    • (1998) Carbohydr Res , vol.310 , pp. 151-156
    • Volc, J.1    Sedmera, P.2    Halada, P.3    Prikrylová, V.4    Daniel, G.5
  • 31
    • 0031941120 scopus 로고    scopus 로고
    • Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
    • Mewies M, McIntire WS & Scrutton NS (1998) Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. Protein Sci 7, 7-20.
    • (1998) Protein Sci , vol.7 , pp. 7-20
    • Mewies, M.1    McIntire, W.S.2    Scrutton, N.S.3
  • 32
    • 33745229673 scopus 로고    scopus 로고
    • Characterization of the flavin association in hexose oxidase from Chondrus crispus
    • Rand T, Qvist KB, Walter CP & Poulsen CH (2006) Characterization of the flavin association in hexose oxidase from Chondrus crispus. FEBS J 273, 2693-2703.
    • (2006) FEBS J , vol.273 , pp. 2693-2703
    • Rand, T.1    Qvist, K.B.2    Walter, C.P.3    Poulsen, C.H.4
  • 33
    • 33746325823 scopus 로고    scopus 로고
    • Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor
    • Winkler A, Hartner F, Kutchan TM, Glieder A & Macheroux P (2006) Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor. J Biol Chem 281, 21276-21285.
    • (2006) J Biol Chem , vol.281 , pp. 21276-21285
    • Winkler, A.1    Hartner, F.2    Kutchan, T.M.3    Glieder, A.4    Macheroux, P.5
  • 34
    • 0033544926 scopus 로고    scopus 로고
    • Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase
    • Fraaije MW, van den Heuvel RH, van Berkel WJ & Mattevi A (1999) Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase. J Biol Chem 274, 35514-55520.
    • (1999) J Biol Chem , vol.274 , pp. 35514-55520
    • Fraaije, M.W.1    van den Heuvel, R.H.2    van Berkel, W.J.3    Mattevi, A.4
  • 35
    • 0035916226 scopus 로고    scopus 로고
    • Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase
    • Efimov I, Cronin CN & McIntire WS (2001) Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase. Biochemistry 40, 2155-2166.
    • (2001) Biochemistry , vol.40 , pp. 2155-2166
    • Efimov, I.1    Cronin, C.N.2    McIntire, W.S.3
  • 36
    • 0035947649 scopus 로고    scopus 로고
    • Cholesterol oxidase from Brevibacterium sterolicum. The relationship between covalent flavinylation and redox properties
    • Motteran L, Pilone MS, Molla G, Ghisla S & Pollegioni L (2001) Cholesterol oxidase from Brevibacterium sterolicum. The relationship between covalent flavinylation and redox properties. J Biol Chem 276, 18024-18030.
    • (2001) J Biol Chem , vol.276 , pp. 18024-18030
    • Motteran, L.1    Pilone, M.S.2    Molla, G.3    Ghisla, S.4    Pollegioni, L.5
  • 37
    • 33747095429 scopus 로고    scopus 로고
    • Role of the covalent flavin linkage in monomeric sarcosine oxidase
    • Hassan-Abdallah A, Zhao G & Jorns MS (2006) Role of the covalent flavin linkage in monomeric sarcosine oxidase. Biochemistry 45, 9454-9462.
    • (2006) Biochemistry , vol.45 , pp. 9454-9462
    • Hassan-Abdallah, A.1    Zhao, G.2    Jorns, M.S.3
  • 38
  • 39
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga RK, Terpstra P & Hol WG (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 187, 101-107.
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 40
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym O & Eisenberg D (2001) Sequence-structure analysis of FAD-containing proteins. Protein Sci 10, 1712-1728.
    • (2001) Protein Sci , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 41
    • 0026544690 scopus 로고
    • GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities
    • Cavener DR (1992) GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities. J Mol Biol 223, 811-814.
    • (1992) J Mol Biol , vol.223 , pp. 811-814
    • Cavener, D.R.1
  • 42
    • 4143089527 scopus 로고    scopus 로고
    • Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi
    • Zamocky M, Hallberg M, Ludwig R, Divne C & Haltrich D (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, M.2    Ludwig, R.3    Divne, C.4    Haltrich, D.5
  • 43
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution
    • Vrielink A, Lloyd LF & Blow DM (1991) Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution. J Mol Biol 219, 533-554.
    • (1991) J Mol Biol , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 45
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxgen reactivity of flavoenzymes
    • Mattevi A (2006) To be or not to be an oxidase: challenging the oxgen reactivity of flavoenzymes. Trends Biochem Sci 31, 276-283.
    • (2006) Trends Biochem Sci , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 46
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 47
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 48
    • 0003180169 scopus 로고    scopus 로고
    • Gradient-enhanced one-dimensional proton chemical-shift correlation with full sensitivity
    • Uhrín D & Barlow P (1997) Gradient-enhanced one-dimensional proton chemical-shift correlation with full sensitivity. J Magn Reson 126, 248-255.
    • (1997) J Magn Reson , vol.126 , pp. 248-255
    • Uhrín, D.1    Barlow, P.2
  • 49
    • 0028340896 scopus 로고
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida. Appl Environ Microbiol 60, 2524-2532.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2524-2532
    • Daniel, G.1    Volc, J.2    Kubátová, E.3
  • 50
    • 0026443134 scopus 로고
    • 2-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions
    • 2-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions. Appl Environ Microbiol 58, 3667-3676.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3667-3676
    • Daniel, G.1    Volc, J.2    Kubátová, E.3    Nilsson, T.4
  • 51
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW & Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr Sect A 47, 110-119.
    • (1991) Acta Crystallogr Sect A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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