메뉴 건너뛰기




Volumn 71, Issue 6, 2006, Pages 898-906

Hydrolysis of β-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-β-glucanase from the basidiomycete Phanerochaete chrysosporium

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CATALYSIS; DNA; HYDROLYSIS; POLYSACCHARIDES; PROTEINS;

EID: 33746720134     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-005-0214-4     Document Type: Article
Times cited : (52)

References (43)
  • 1
    • 0036617995 scopus 로고    scopus 로고
    • Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic β-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165
    • Asano T, Taki J, Yamamoto M, Aono R (2002) Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic β-1,3-glucan- hydrolase BglM of Bacillus circulans IAM1165. Biosci Biotechnol Biochem 66:1246-1255
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1246-1255
    • Asano, T.1    Taki, J.2    Yamamoto, M.3    Aono, R.4
  • 2
    • 0028895388 scopus 로고
    • Isolation of extracellular 28- and 42-kilodalton β-1,3-glucanases and comparison of three β-1,3-glucanases produced by Bacillus circulans IAM1165
    • Aono R, Hammura M, Yamamoto M, Asano T (1995) Isolation of extracellular 28- and 42-kilodalton β-1,3-glucanases and comparison of three β-1,3-glucanases produced by Bacillus circulans IAM1165. Appl Environ Microbiol 61:122-129
    • (1995) Appl Environ Microbiol , vol.61 , pp. 122-129
    • Aono, R.1    Hammura, M.2    Yamamoto, M.3    Asano, T.4
  • 3
    • 0033026416 scopus 로고    scopus 로고
    • Cloning and characterization of an endo-β-1,3(4) glucanase and an aspartic protease from Phaffia rhodozyma CBS 6938
    • Bang ML, Villadsen I, Sandal T (1999) Cloning and characterization of an endo-β-1,3(4) glucanase and an aspartic protease from Phaffia rhodozyma CBS 6938. Appl Microbiol Biotechnol 51:215-222
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 215-222
    • Bang, M.L.1    Villadsen, I.2    Sandal, T.3
  • 4
    • 0031901635 scopus 로고    scopus 로고
    • The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases
    • Barbeyron T, Gerard A, Potin P, Henrissat B, Kloareg B (1998) The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases. Mol Biol Evol 15:528-537
    • (1998) Mol Biol Evol , vol.15 , pp. 528-537
    • Barbeyron, T.1    Gerard, A.2    Potin, P.3    Henrissat, B.4    Kloareg, B.5
  • 5
    • 0001492547 scopus 로고
    • Synthesis, structure, and enzymatic degradation of an extracellular glucan produced in nitrogen-starved cultures of the white rot fungus Phanerochaete chrysosporium
    • Bes B, Pettersson B, Lennholm H, Iversen T, Eriksson K-E (1987) Synthesis, structure, and enzymatic degradation of an extracellular glucan produced in nitrogen-starved cultures of the white rot fungus Phanerochaete chrysosporium. Biotechnol Appl Biochem 9:310-318
    • (1987) Biotechnol Appl Biochem , vol.9 , pp. 310-318
    • Bes, B.1    Pettersson, B.2    Lennholm, H.3    Iversen, T.4    Eriksson, K.-E.5
  • 6
    • 0013990139 scopus 로고
    • The biochemistry of laminarin and the nature of laminarinase
    • Bull AT, Chesters CG (1966) The biochemistry of laminarin and the nature of laminarinase. Adv Enzymol Relat Areas Mol Biol 28:325-364
    • (1966) Adv Enzymol Relat Areas Mol Biol , vol.28 , pp. 325-364
    • Bull, A.T.1    Chesters, C.G.2
  • 7
    • 0028173885 scopus 로고
    • A Phanerochaete chrysosporium β-D-glucosidase/β-D-xylosidase with specificity for (1->3)-β-D-glucan linkages
    • Copa-Patio JL, Broda P (1994) A Phanerochaete chrysosporium β-D-glucosidase/β-D-xylosidase with specificity for (1->3)-β-D-glucan linkages. Carbohydr Res 253:265-275
    • (1994) Carbohydr Res , vol.253 , pp. 265-275
    • Copa-Patio, J.L.1    Broda, P.2
  • 8
    • 0024846974 scopus 로고
    • Purification and properties of a 1,3-β-glucanase from Penicillium oxalicum autolysates
    • Copa-Patio JL, Reyes F, Perez-Leblic MI (1989) Purification and properties of a 1,3-β-glucanase from Penicillium oxalicum autolysates. FEMS Microbiol Lett 65:285-292
    • (1989) FEMS Microbiol Lett , vol.65 , pp. 285-292
    • Copa-Patio, J.L.1    Reyes, F.2    Perez-Leblic, M.I.3
  • 9
    • 0031038378 scopus 로고    scopus 로고
    • Purification and characterization of an endo-1,3-β-glucanase from Aspergillus fumigatus
    • Fontaine T, Hartland RP, Beauvais A, Diaquin M, Latge J-P (1997a) Purification and characterization of an endo-1,3-β-glucanase from Aspergillus fumigatus. Eur J Biochem 243:315-321
    • (1997) Eur J Biochem , vol.243 , pp. 315-321
    • Fontaine, T.1    Hartland, R.P.2    Beauvais, A.3    Diaquin, M.4    Latge, J.-P.5
  • 10
    • 0030910922 scopus 로고    scopus 로고
    • Differential patterns of activity displayed by two exo-β-1, 3-glucanases associated with Aspergillus fumigatus cell wall
    • Fontaine T, Hartland RP, Diaquin M, Simenel C, Latge JP (1997b) Differential patterns of activity displayed by two exo-β-1, 3-glucanases associated with Aspergillus fumigatus cell wall. J Bacteriol 179:3154-3163
    • (1997) J Bacteriol , vol.179 , pp. 3154-3163
    • Fontaine, T.1    Hartland, R.P.2    Diaquin, M.3    Simenel, C.4    Latge, J.P.5
  • 11
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224:149-155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 12
    • 0042412981 scopus 로고    scopus 로고
    • Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum
    • Gorlach JM, Van Der Knaap E, Walton JD (1998) Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum. Appl Environ Microbiol 64:385-391
    • (1998) Appl Environ Microbiol , vol.64 , pp. 385-391
    • Gorlach, J.M.1    Van Der Knaap, E.2    Walton, J.D.3
  • 13
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo-β-1,3- glucanase of the hyperthermophilic archaeon Pyrococcus furiosus
    • Gueguen Y, Voorhorst WGB, Van Der Oost J, De Vos WM (1997) Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 272:31258-31264
    • (1997) J Biol Chem , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.B.2    Van Der Oost, J.3    De Vos, W.M.4
  • 14
    • 0030770510 scopus 로고    scopus 로고
    • Enhanced production of cellobiose dehydrogenase in cultures of Phanerochaete chrysosporium supplemented with bovine calf serum
    • Habu N, Igarashi K, Samejima M, Pettersson B, Eriksson K-EL (1997) Enhanced production of cellobiose dehydrogenase in cultures of Phanerochaete chrysosporium supplemented with bovine calf serum. Biotechnol Appl Biochem 26:97-102
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 97-102
    • Habu, N.1    Igarashi, K.2    Samejima, M.3    Pettersson, B.4    Eriksson, K.-E.L.5
  • 15
    • 0028812262 scopus 로고
    • Crystal structure and site-directed mutagenesis of Bacillus maceransendo-1,3-1,4-β-glucanase
    • Hahn M, Olsen O, Politz O, Borriss R, Heinemann U (1995a) Crystal structure and site-directed mutagenesis of Bacillus maceransendo-1,3-1,4-β- glucanase. J Biol Chem 270:3081-3088
    • (1995) J Biol Chem , vol.270 , pp. 3081-3088
    • Hahn, M.1    Olsen, O.2    Politz, O.3    Borriss, R.4    Heinemann, U.5
  • 16
    • 0028841188 scopus 로고
    • Crystal structure of Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase at 1.8 a resolution
    • Hahn M, Pons J, Planas A, Querol E, Heinemann U (1995b) Crystal structure of Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett 374:221-224
    • (1995) FEBS Lett , vol.374 , pp. 221-224
    • Hahn, M.1    Pons, J.2    Planas, A.3    Querol, E.4    Heinemann, U.5
  • 17
    • 0026055308 scopus 로고
    • A classification of glycoside hydrolases based on amino acid sequence similarities
    • Henrissat B (1991) A classification of glycoside hydrolases based on amino acid sequence similarities. Biochem J 280:309-316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 18
    • 0027225980 scopus 로고
    • New families in the classification of glycoside hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A (1993) New families in the classification of glycoside hydrolases based on amino acid sequence similarities. Biochem J 293:781-788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 19
    • 33746778907 scopus 로고    scopus 로고
    • Biochemical characterization and antifungal activity of an endo-1,3-β-glucanase of Paenibacillus sp. isolated from garden soil
    • Hong TY, Meng M (2003) Biochemical characterization and antifungal activity of an endo-1,3-β-glucanase of Paenibacillus sp. isolated from garden soil. J Biosci Bioeng 95:572-576
    • (2003) J Biosci Bioeng , vol.95 , pp. 572-576
    • Hong, T.Y.1    Meng, M.2
  • 20
    • 0038344488 scopus 로고    scopus 로고
    • Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase
    • Igarashi K, Tani T, Kawai R, Samejima M (2003) Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase. J Biosci Bioeng 95:572-576
    • (2003) J Biosci Bioeng , vol.95 , pp. 572-576
    • Igarashi, K.1    Tani, T.2    Kawai, R.3    Samejima, M.4
  • 21
    • 20444477149 scopus 로고    scopus 로고
    • Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium
    • Igarashi K, Yoshida M, Matsumura H, Nakamura N, Ohno H, Samejima M, Nishino T (2005) Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium. FEBS J 272:2869-2877
    • (2005) FEBS J , vol.272 , pp. 2869-2877
    • Igarashi, K.1    Yoshida, M.2    Matsumura, H.3    Nakamura, N.4    Ohno, H.5    Samejima, M.6    Nishino, T.7
  • 23
    • 0021946306 scopus 로고
    • Cross-breeding of selected and mutated homokaryotic strains of Phanerochaete chrysosporium K-3: New cellulase deficient strains with increased ability to degrade lignin
    • Johnsrud SC, Eriksson K-E (1985) Cross-breeding of selected and mutated homokaryotic strains of Phanerochaete chrysosporium K-3: new cellulase deficient strains with increased ability to degrade lignin. Appl Microbiol Biotechnol 21:320-327
    • (1985) Appl Microbiol Biotechnol , vol.21 , pp. 320-327
    • Johnsrud, S.C.1    Eriksson, K.-E.2
  • 24
    • 0028225393 scopus 로고
    • Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase by site-directed mutagenesis
    • Juncosa M, Pons J, Dot T, Querol E, Planas A (1994) Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-β-D- glucan 4-glucanohydrolase by site-directed mutagenesis. J Biol Chem 269:14530-14535
    • (1994) J Biol Chem , vol.269 , pp. 14530-14535
    • Juncosa, M.1    Pons, J.2    Dot, T.3    Querol, E.4    Planas, A.5
  • 25
    • 0022350618 scopus 로고
    • Changes in (1->3)-β-glucanase activities during stipe elongation in Coprinus cinereus
    • Kamada T, Fujii T, Nakagawa T, Takemaru T (1985) Changes in (1->3)-β-glucanase activities during stipe elongation in Coprinus cinereus. Curr Microbiol 12:257-260
    • (1985) Curr Microbiol , vol.12 , pp. 257-260
    • Kamada, T.1    Fujii, T.2    Nakagawa, T.3    Takemaru, T.4
  • 26
    • 0038151854 scopus 로고    scopus 로고
    • Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast Pichia pastoris
    • Kawai R, Yoshida M, Tani T, Igarashi K, Ohira T, Nagasawa H, Samejima M (2003) Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast Pichia pastoris. Biosci Biotechnol Biochem 67:1-7
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1-7
    • Kawai, R.1    Yoshida, M.2    Tani, T.3    Igarashi, K.4    Ohira, T.5    Nagasawa, H.6    Samejima, M.7
  • 27
    • 9944239242 scopus 로고    scopus 로고
    • Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1->3)-β-glucosidease from the white-rot fungus Phanerochaete chrysosporium
    • Kawai R, Igarashi K, Kitaoka M, Ishii T, Samejima M (2004) Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1->3)-β-glucosidease from the white-rot fungus Phanerochaete chrysosporium. Carbohydr Res 339:2851-2857
    • (2004) Carbohydr Res , vol.339 , pp. 2851-2857
    • Kawai, R.1    Igarashi, K.2    Kitaoka, M.3    Ishii, T.4    Samejima, M.5
  • 28
    • 0032190308 scopus 로고    scopus 로고
    • The laminarinase from thermophilic eubacterium Rhodothermus marinus conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis
    • Krah M, Misselwitz R, Politz O, Thomsen KK, Welfle H, Borriss R (1998) The laminarinase from thermophilic eubacterium Rhodothermus marinus conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis. Eur J Biochem 257:101-111
    • (1998) Eur J Biochem , vol.257 , pp. 101-111
    • Krah, M.1    Misselwitz, R.2    Politz, O.3    Thomsen, K.K.4    Welfle, H.5    Borriss, R.6
  • 29
    • 0026576254 scopus 로고
    • Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase
    • Kremer SM, Wood PM (1992) Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase. Eur J Biochem 205:133-138
    • (1992) Eur J Biochem , vol.205 , pp. 133-138
    • Kremer, S.M.1    Wood, P.M.2
  • 30
    • 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
  • 31
    • 0027772710 scopus 로고
    • Stereochemical course and structure of the products of the enzymatic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis
    • Malet C, Jimenez-Barbero J, Bernabe M, Brosa C, Planas A (1993) Stereochemical course and structure of the products of the enzymatic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis. Biochem J 296:753-758
    • (1993) Biochem J , vol.296 , pp. 753-758
    • Malet, C.1    Jimenez-Barbero, J.2    Bernabe, M.3    Brosa, C.4    Planas, A.5
  • 33
    • 0038105156 scopus 로고    scopus 로고
    • Molecular characterization and expression in Escherichia coli of three β-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7
    • Palumbo JD, Sullivan RF, Kobayashi DY (2003) Molecular characterization and expression in Escherichia coli of three β-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7. J Bacteriol 185:4362-4370
    • (2003) J Bacteriol , vol.185 , pp. 4362-4370
    • Palumbo, J.D.1    Sullivan, R.F.2    Kobayashi, D.Y.3
  • 34
    • 0033957024 scopus 로고    scopus 로고
    • A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus NMR analysis of enzyme
    • Petersen BO, Krah M, Duus DO, Thomsen KK (2000) A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus NMR analysis of enzyme. Eur J Biochem 267:361-369
    • (2000) Eur J Biochem , vol.267 , pp. 361-369
    • Petersen, B.O.1    Krah, M.2    Duus, D.O.3    Thomsen, K.K.4
  • 35
    • 0027572064 scopus 로고
    • Noncellulolytic fungal β-glucanases: Their physiology and regulation
    • Pitson SM, Seviour RJ, McDougall BM (1993) Noncellulolytic fungal β-glucanases: their physiology and regulation. Enzyme Microb Technol 15:178-192
    • (1993) Enzyme Microb Technol , vol.15 , pp. 178-192
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3
  • 36
    • 0029054781 scopus 로고
    • Purification and characterization of three extracellular (1->3)-β-D-glucan glucohydrolases from the filamentous fungus Acremonium persicinum
    • Pitson SM, Seviour RJ, McDougall BM, Woodward JR, Stone BA (1995) Purification and characterization of three extracellular (1->3)-β-D- glucan glucohydrolases from the filamentous fungus Acremonium persicinum. Biochem J 308:733-741
    • (1995) Biochem J , vol.308 , pp. 733-741
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3    Woodward, J.R.4    Stone, B.A.5
  • 37
    • 0026654729 scopus 로고
    • Formation, separation and characterization of three β-1,3-glucanases from Sclerotium glucanicum
    • Rapp P (1992) Formation, separation and characterization of three β-1,3-glucanases from Sclerotium glucanicum. Biochim Biophys Acta 1117:7-14
    • (1992) Biochim Biophys Acta , vol.1117 , pp. 7-14
    • Rapp, P.1
  • 39
    • 0027332216 scopus 로고
    • Purification and characterization of four extracellular 1,3-β-glucanases of Botrytis cinerea
    • Stahmann K-P, Schimz K-L, Sahm H (1993) Purification and characterization of four extracellular 1,3-β-glucanases of Botrytis cinerea. J Gen Microbiol 139:2833-2840
    • (1993) J Gen Microbiol , vol.139 , pp. 2833-2840
    • Stahmann, K.-P.1    Schimz, K.-L.2    Sahm, H.3
  • 41
    • 9344241402 scopus 로고    scopus 로고
    • Molecular modeling of family GH16 glycoside hydrolases: Potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the Poaceae
    • Strohmeier M, Hrmova M, Fischer M, Harvey AJ, Fincher GB, Pleiss J (2004) Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the Poaceae. Protein Sci 13:3200-3213
    • (2004) Protein Sci , vol.13 , pp. 3200-3213
    • Strohmeier, M.1    Hrmova, M.2    Fischer, M.3    Harvey, A.J.4    Fincher, G.B.5    Pleiss, J.6
  • 43
    • 20444468865 scopus 로고    scopus 로고
    • The Phanerochaete chrysosporium secretome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
    • Wymelenberg AV, Sabat G, Martinez D, Rajangam AS, Teeri TT, Gaskell J, Kersten PJ, Cullen D (2005) The Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium. J Biotechnol 118:17-34
    • (2005) J Biotechnol , vol.118 , pp. 17-34
    • Wymelenberg, A.V.1    Sabat, G.2    Martinez, D.3    Rajangam, A.S.4    Teeri, T.T.5    Gaskell, J.6    Kersten, P.J.7    Cullen, D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.