메뉴 건너뛰기




Volumn 1, Issue 4, 2004, Pages 285-292

Hydrolase and glycosynthase activity of endo-1,3-β-glucanase from the thermophile Pyrococcus furiosus

Author keywords

Enzymatic synthesis; Glycosyl fluoride; Glycosylation; Glycosynthase mutant; Hydrolysis; Laminarinase; Nucleophile

Indexed keywords

BACTERIA (MICROORGANISMS); PYROCOCCUS; PYROCOCCUS FURIOSUS;

EID: 8744262925     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2004/731548     Document Type: Article
Times cited : (37)

References (36)
  • 2
    • 12444289585 scopus 로고    scopus 로고
    • Enzymatic synthesis of 4-methylumbelliferyl (1→3)-β-D- glucooligosaccharides. New substrates for β-1,3-1,4-D-glucanase
    • Borriss, R., M. Krah, H. Brumer, III et al. 2003. Enzymatic synthesis of 4-methylumbelliferyl (1→3)-β-D-glucooligosaccharides. New substrates for β-1,3-1,4-D-glucanase. Carbohydr. Res. 338:1455-1467.
    • (2003) Carbohydr. Res. , vol.338 , pp. 1455-1467
    • Borriss, R.1    Krah, M.2    Brumer III, H.3
  • 3
    • 2242491786 scopus 로고    scopus 로고
    • Persistence of tertiary structure in 7.9 M guanidinium chloride: The case of endo-β-1,3-glucanase from Pyrococcus furiosus
    • Chiaraluce, R., J. van der Oost, J.H. Lebbink, T. Kaper and V. Consalvi. 2002. Persistence of tertiary structure in 7.9 M guanidinium chloride: the case of endo-β-1,3-glucanase from Pyrococcus furiosus. Biochemistry 41:14,624-14,632.
    • (2002) Biochemistry , vol.41 , pp. 14624-14632
    • Chiaraluce, R.1    Van Der Oost, J.2    Lebbink, J.H.3    Kaper, T.4    Consalvi, V.5
  • 4
    • 0033230211 scopus 로고    scopus 로고
    • Synergistic interactions among β-laminarinase, β-1,4-glucanase, and β-glucosidase from the hyperthermophilic Archaeon Pyrococcus furiosus during hydrolysis of β-1,4-, β-1,3-, and mixed-linked polysaccharides
    • Driskill, L.E., M.W. Bauer and R.M. Kelly. 1999. Synergistic interactions among β-laminarinase, β-1,4-glucanase, and β-glucosidase from the hyperthermophilic Archaeon Pyrococcus furiosus during hydrolysis of β-1,4-, β-1,3-, and mixed-linked polysaccharides. Biotechnol. Bioeng. 66:51-60.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 51-60
    • Driskill, L.E.1    Bauer, M.W.2    Kelly, R.M.3
  • 5
    • 0035813818 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: A straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4-β-glucanases
    • Faijes, M., J.K. Fairweather, H. Driguez and A. Planas. 2001. Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: a straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4-β-glucanases. Chemistry 7:4651-4655.
    • (2001) Chemistry , vol.7 , pp. 4651-4655
    • Faijes, M.1    Fairweather, J.K.2    Driguez, H.3    Planas, A.4
  • 6
    • 0242667918 scopus 로고    scopus 로고
    • Glycosynthase activity of Bacillus licheniformis 1,3-1,4-β-glucanase mutants: Specificity, kinetics, and mechanism
    • Faijes, M., X. Perez, O. Perez and A. Planas. 2003. Glycosynthase activity of Bacillus licheniformis 1,3-1,4-β-glucanase mutants: specificity, kinetics, and mechanism. Biochemistry 42:13,304-13,318.
    • (2003) Biochemistry , vol.42 , pp. 13304-13318
    • Faijes, M.1    Perez, X.2    Perez, O.3    Planas, A.4
  • 8
    • 0038366761 scopus 로고    scopus 로고
    • Lic16a of Clostridium thermocellum, a non-cellulosomal, highly complex endo-β-1,3-glucanase bound to the outer cell surface
    • Fuchs, K.P., V.V. Zverlov, G.A. Velikodvorskaya, F. Lottspeich and W.H. Schwarz. 2003. Lic16a of Clostridium thermocellum, a non-cellulosomal, highly complex endo-β-1,3-glucanase bound to the outer cell surface. Microbiology 149:1021-1031.
    • (2003) Microbiology , vol.149 , pp. 1021-1031
    • Fuchs, K.P.1    Zverlov, V.V.2    Velikodvorskaya, G.A.3    Lottspeich, F.4    Schwarz, W.H.5
  • 9
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and P.H. Von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 10
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo-β-1,3- glucanase of the hyperthermophilic Archaeon Pyrococcus furiosus
    • Gueguen, Y., W.G. Voorhorst, J. van der Oost and W.M. de Vos. 1997. Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic Archaeon Pyrococcus furiosus. J. Biol. Chem. 272:31,258-31,264.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.2    Van Der Oost, J.3    De Vos, W.M.4
  • 11
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 12
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., H.D. Hunt, R.M. Horton, J.K. Pullen and L.R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 15
    • 0036436302 scopus 로고    scopus 로고
    • On expanding the repertoire of glycosynthases: Mutant β-galactosidases forming β-(1,6)-linkages
    • Jakeman, D.L. and S.G. Withers. 2002. On expanding the repertoire of glycosynthases: mutant β-galactosidases forming β-(1,6)-linkages. Can. J. Chem. 80:866-870.
    • (2002) Can. J. Chem. , vol.80 , pp. 866-870
    • Jakeman, D.L.1    Withers, S.G.2
  • 16
    • 0028225393 scopus 로고
    • Identification of active site carboxylic residues in Bacillus licheniformis endo-1,3-1,4-β-D-glucan 4-glucanohydrolase by site-directed mutagenesis
    • Juncosa, M., J. Pons, T. Dot, E. Querol and A. Planas. 1994. Identification of active site carboxylic residues in Bacillus licheniformis endo-1,3-1,4-β-D-glucan 4-glucanohydrolase by site-directed mutagenesis. J. Biol. Chem. 269:14,530-14,535.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14530-14535
    • Juncosa, M.1    Pons, J.2    Dot, T.3    Querol, E.4    Planas, A.5
  • 17
    • 17744396452 scopus 로고    scopus 로고
    • Characterization of β-glycosyl hydrolases from Pyrococcus furiosus
    • Kaper, T., C.H. Verhees, J.H. Lebbink et al. 2001. Characterization of β-glycosyl hydrolases from Pyrococcus furiosus. Methods Enzymol. 330:329-346.
    • (2001) Methods Enzymol. , vol.330 , pp. 329-346
    • Kaper, T.1    Verhees, C.H.2    Lebbink, J.H.3
  • 18
    • 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., R. Misselwitz, O. Politz, K.K. Thomsen, H. Welfle and R. Borriss. 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
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 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
  • 20
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for oligosaccharide synthesis
    • Mackenzie, L.F., Q. Wang, R.A.J. Warren and S.G. Withers. 1998. Glycosynthases: mutant glycosidases for oligosaccharide synthesis. J. Am. Chem. Soc. 120:5583-5584.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5583-5584
    • Mackenzie, L.F.1    Wang, Q.2    Warren, R.A.J.3    Withers, S.G.4
  • 21
    • 0030694040 scopus 로고    scopus 로고
    • Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases: Kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides
    • Malet, C. and A. Planas. 1997. Mechanism of Bacillus 1,3-1,4-β-D- glucan 4-glucanohydrolases: kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides. Biochemistry 36:13,838-13,848.
    • (1997) Biochemistry , vol.36 , pp. 13838-13848
    • Malet, C.1    Planas, A.2
  • 22
    • 0032573586 scopus 로고    scopus 로고
    • From β-glucanase to β-glucan-synthase: Glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile
    • Malet, C. and A. Planas. 1998. From β-glucanase to β-glucan-synthase: glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile. FEBS Lett. 440:208-212.
    • (1998) FEBS Lett. , vol.440 , pp. 208-212
    • Malet, C.1    Planas, A.2
  • 23
    • 0029082880 scopus 로고
    • Synthesis of 4-methylumbelliferyl-α-D-glucan oligosaccharides as specific chromophoric substrates of (1→3), (1→4)-β-D-glucan 4-glucanohydrolases
    • Malet, C., J.L. Viladot, A. Ochoa, B. Gallego, C. Brosa and A. Planas. 1995. Synthesis of 4-methylumbelliferyl-α-D-glucan oligosaccharides as specific chromophoric substrates of (1→3), (1→4)-β-D-glucan 4-glucanohydrolases. Carbohydr. Res. 274:285-301.
    • (1995) Carbohydr. Res. , vol.274 , pp. 285-301
    • Malet, C.1    Viladot, J.L.2    Ochoa, A.3    Gallego, B.4    Brosa, C.5    Planas, A.6
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G.L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 0035931580 scopus 로고    scopus 로고
    • Glycosynthases: New enzymes for oligosaccharide synthesis
    • Moracci, M., A. Trincone and M. Rossi. 2001. Glycosynthases: new enzymes for oligosaccharide synthesis. J. Mol. Catal. B Enzym. 11:155-163.
    • (2001) J. Mol. Catal. B Enzym. , vol.11 , pp. 155-163
    • Moracci, M.1    Trincone, A.2    Rossi, M.3
  • 27
    • 0036547634 scopus 로고    scopus 로고
    • α-Glucosidase mutant catalyzes "α-glycosynthase"- type reaction. Biosci
    • Okuyama, M., H. Mori, K. Watanabe, A. Kimura and S. Chiba. 2002. α-Glucosidase mutant catalyzes "α-glycosynthase"-type reaction. Biosci. Biotechnol. Biochem. 66:928-933.
    • (2002) Biotechnol. Biochem. , vol.66 , pp. 928-933
    • Okuyama, M.1    Mori, H.2    Watanabe, K.3    Kimura, A.4    Chiba, S.5
  • 28
    • 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, J.D., R.F. Sullivan and D.Y. Kobayashi. 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
  • 30
    • 0033957024 scopus 로고    scopus 로고
    • A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus. NMR analysis of enzyme reactions
    • Petersen, B.O., M. Krah, J.O. Duus and K.K. Thomsen. 2000. A transglycosylating 1,3(4)-β-glucanase from Rhodothermus marinus. NMR analysis of enzyme reactions. Eur. J. Biochem. 267:361-369.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 361-369
    • Petersen, B.O.1    Krah, M.2    Duus, J.O.3    Thomsen, K.K.4
  • 31
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-α-glucanases: Structure, function and protein engineering
    • Planas, A. 2000. Bacterial 1,3-1,4-α-glucanases: structure, function and protein engineering. Biochim. Biophys. Acta 1543:361-382.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 32
    • 0036664973 scopus 로고    scopus 로고
    • Glycosidases and glycosynthases in enzymatic synthesis of oligosaccharides. An overview
    • Planas, A. and M. Faijes. 2002. Glycosidases and glycosynthases in enzymatic synthesis of oligosaccharides. An overview. Afinidad 59:295-313.
    • (2002) Afinidad , vol.59 , pp. 295-313
    • Planas, A.1    Faijes, M.2
  • 33
    • 0034696084 scopus 로고    scopus 로고
    • A novel thermophilic glycosynthase that effects branching glycosylation
    • Trincone, A., G. Perugino, M. Rossi and M. Moracci. 2000. A novel thermophilic glycosynthase that effects branching glycosylation. Bioorg. Med. Chem. Lett. 10:365-368.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 365-368
    • Trincone, A.1    Perugino, G.2    Rossi, M.3    Moracci, M.4
  • 34
    • 0000469136 scopus 로고
    • The use of 4-methylumbelliferyl and other chromophoric glycosides in the study of cellulolytic enzymes
    • van Tilbeurgh, H., M. Claeyssens and C.K. De Bruyne. 1982. The use of 4-methylumbelliferyl and other chromophoric glycosides in the study of cellulolytic enzymes. FEBS Lett. 149:152-156.
    • (1982) FEBS Lett. , vol.149 , pp. 152-156
    • Tilbeurgh, H.1    Claeyssens, M.2    De Bruyne, C.K.3
  • 35
    • 0032508394 scopus 로고    scopus 로고
    • Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues
    • Viladot, J.L., E. De Ramon, O. Durany and A. Planas. 1998. Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues. Biochemistry 37:11,332-11,342.
    • (1998) Biochemistry , vol.37 , pp. 11332-11342
    • Viladot, J.L.1    De Ramon, E.2    Durany, O.3    Planas, A.4
  • 36
    • 0036303152 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for glycoside synthesis
    • Williams, S.J. and S.G. Withers. 2002. Glycosynthases: mutant glycosidases for glycoside synthesis. Aust. J. Chem. 55:3-12.
    • (2002) Aust. J. Chem. , vol.55 , pp. 3-12
    • Williams, S.J.1    Withers, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.