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Volumn 406, Issue 4, 2011, Pages 590-594

Mode of operation and low-resolution structure of a multi-domain and hyperthermophilic endo-β-1,3-glucanase from Thermotoga petrophila

Author keywords

Capillary zone electrophoresis; Endo 1,3 glucanase; Glycoside hydrolase family 16; Hyperthermostable enzyme; Small angle X ray scattering

Indexed keywords

ENDO 1,3 BETA GLUCANASE; GLUCOSE;

EID: 79953029268     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.02.098     Document Type: Article
Times cited : (42)

References (29)
  • 1
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance. Engineering plants and enzymes for biofuels production
    • Himmel M.E., Ding S.Y., Johnson D.K., et al. Biomass recalcitrance. Engineering plants and enzymes for biofuels production. Science 2007, 315:804-807.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3
  • 2
    • 0030943791 scopus 로고    scopus 로고
    • Highly thermostable endo-1, 3-beta-glucanase (laminarinase) LamA from Thermotoga neapolitana: nucleotide sequence of the gene and characterization of the recombinant gene product
    • Zverlov V.V., Volkov I.Y., Velikodvorskaya T.V., Schwarz W.H. Highly thermostable endo-1, 3-beta-glucanase (laminarinase) LamA from Thermotoga neapolitana: nucleotide sequence of the gene and characterization of the recombinant gene product. Microbiology 1997, 143:1701-1708.
    • (1997) Microbiology , vol.143 , pp. 1701-1708
    • Zverlov, V.V.1    Volkov, I.Y.2    Velikodvorskaya, T.V.3    Schwarz, W.H.4
  • 3
    • 67650676817 scopus 로고    scopus 로고
    • X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis
    • Vasur J., Kawai R., Andersson E., et al. X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis. FEBS J. 2007, 276:3858-3869.
    • (2007) FEBS J. , vol.276 , pp. 3858-3869
    • Vasur, J.1    Kawai, R.2    Andersson, E.3
  • 5
    • 0027439791 scopus 로고
    • Purification and properties of three (1-3)-beta-d-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • M. Hrmova, G.B. Fincher, Purification and properties of three (1-3)-beta-d-glucanase isoenzymes from young leaves of barley (Hordeum vulgare), Biochem. J. (1993) 453-461.
    • (1993) Biochem. J. , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 6
    • 58849132978 scopus 로고    scopus 로고
    • Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus-structural basis of substrate recognition
    • Ilari A., Fiorillo A., Angelaccio S., et al. Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus-structural basis of substrate recognition. FEBS J. 2009, 276:1048-1058.
    • (2009) FEBS J. , vol.276 , pp. 1048-1058
    • Ilari, A.1    Fiorillo, A.2    Angelaccio, S.3
  • 7
    • 49749127692 scopus 로고    scopus 로고
    • The 1.5 A structure of endo-1, 3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1, 3-beta-glucan-binding specificity and hydrolysis Acta Crystallogr
    • Hong T.Y., Hsiao Y.T., Meng M., Li T.T. The 1.5 A structure of endo-1, 3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1, 3-beta-glucan-binding specificity and hydrolysis Acta Crystallogr. D Biol. Crystallogr. 2008, 64:964-970.
    • (2008) D Biol. Crystallogr. , vol.64 , pp. 964-970
    • Hong, T.Y.1    Hsiao, Y.T.2    Meng, M.3    Li, T.T.4
  • 8
    • 35448964363 scopus 로고    scopus 로고
    • The 1.3 A crystal structure of a novel endo-beta-1, 3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96
    • Fibriansah G., Masuda S., Koizumi N., et al. The 1.3 A crystal structure of a novel endo-beta-1, 3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96. Proteins 2007, 69:683-690.
    • (2007) Proteins , vol.69 , pp. 683-690
    • Fibriansah, G.1    Masuda, S.2    Koizumi, N.3
  • 9
    • 33644819959 scopus 로고    scopus 로고
    • Structural basis for the substrate specificity of a Bacillus 1, 3-1, 4-beta-glucanase
    • Gaiser O.J., Piotukh K., Ponnuswamy M.N., et al. Structural basis for the substrate specificity of a Bacillus 1, 3-1, 4-beta-glucanase. J. Mol. Biol. 2006, 357:1211-1225.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1211-1225
    • Gaiser, O.J.1    Piotukh, K.2    Ponnuswamy, M.N.3
  • 10
    • 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., et al. The laminarinase from thermophilic eubacterium Rhodothermus marinus conformation, Stability, and identification of active site carboxylic residues by site-directed mutagenesis. Eur. J. Biochem. 1998, 257:101-111.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 101-111
    • Krah, M.1    Misselwitz, R.2    Politz, O.3
  • 11
    • 77956268504 scopus 로고    scopus 로고
    • Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila
    • Squina F.M., Santos C.R., Ribeiro D.A., et al. Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila. Biochem. Biophys. Res. Com. 2010, 399:505-511.
    • (2010) Biochem. Biophys. Res. Com. , vol.399 , pp. 505-511
    • Squina, F.M.1    Santos, C.R.2    Ribeiro, D.A.3
  • 12
    • 33747333106 scopus 로고
    • Use od dinitrosalicilic acid reagent for determination of reducing sugar
    • Miller G.L. Use od dinitrosalicilic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 14
    • 78650509567 scopus 로고    scopus 로고
    • Et al., Functional and biophysical characterization of a hyperthermostable GH51 alpha-l-arabinofuranosidase from Thermotoga petrophila
    • Santos C.R., Squina F.M., Navarro A.M. Et al., Functional and biophysical characterization of a hyperthermostable GH51 alpha-l-arabinofuranosidase from Thermotoga petrophila. Biotech. Lett. 2010, 33:131-137.
    • (2010) Biotech. Lett. , vol.33 , pp. 131-137
    • Santos, C.R.1    Squina, F.M.2    Navarro, A.M.3
  • 15
    • 78649907582 scopus 로고    scopus 로고
    • Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1
    • Santos C.R., Meza A.N., Hoffmam Z.B., et al. Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1. Biochem. Biophys. Res. Com. 2010, 403:214-219.
    • (2010) Biochem. Biophys. Res. Com. , vol.403 , pp. 214-219
    • Santos, C.R.1    Meza, A.N.2    Hoffmam, Z.B.3
  • 16
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A., Whitmore L., Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18:211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 17
    • 0003664980 scopus 로고    scopus 로고
    • FIT2D: An Introduction and Overview. In ESRF Internal Report
    • A. P. Hammersley, FIT2D: An Introduction and Overview. In ESRF Internal Report, (1997).
    • (1997)
    • Hammersley, A.P.1
  • 19
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • Fischer H., Oliveira Neto M., Napolitano H.B., et al. Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. J. Appl. Cryst. 2010, 43:101-109.
    • (2010) J. Appl. Cryst. , vol.43 , pp. 101-109
    • Fischer, H.1    Oliveira Neto, M.2    Napolitano, H.B.3
  • 20
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 1992, 25:495-503.
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 21
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 1999, 76:2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 23
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA - a graphics system for rigid-body modeling of macromolecular complexes against solution scattering data
    • Konarev P.V., Petoukhov M.V., Svergun D.I. MASSHA - a graphics system for rigid-body modeling of macromolecular complexes against solution scattering data. J. Appl. Crystallogr. 2001, 34:527-532.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 24
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 1995, 28:768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 25
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 2005, 89:1237-1250.
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 26
    • 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 W.G.B., van der Oost J., de Vos W.M. Molecular and biochemical characterization of an endo- β-1, 3-glucanase of the Hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 1997, 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
  • 27
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody R.W. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur. Biophys. J. 1994, 23:253-262.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 28
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
    • Cantarel B.L., Coutinho P.M., Rancurel C., et al. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009, 37:D233-D238.
    • (2009) Nucleic Acids Res. , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3
  • 29
    • 68349152769 scopus 로고    scopus 로고
    • Xylan decomposition by Aspergillus clavatus endo-xylanase
    • Squina F.M., Mort A.J., Decker S.R., et al. Xylan decomposition by Aspergillus clavatus endo-xylanase. Protein Expression Purif. 2009, 68:65-71.
    • (2009) Protein Expression Purif. , vol.68 , pp. 65-71
    • Squina, F.M.1    Mort, A.J.2    Decker, S.R.3


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