메뉴 건너뛰기




Volumn 17, Issue 4, 2010, Pages 189-195

Structural Analysis of Xylanase from Marine Thermophilic Geobacillus stearothermophilus in Tanjung Api, Poso, Indonesia

Author keywords

enzyme xylanase; Geobacillus stearothermophilus; mutation; structural analysis

Indexed keywords


EID: 84971009248     PISSN: 19783019     EISSN: 20864094     Source Type: Journal    
DOI: 10.4308/hjb.17.4.189     Document Type: Article
Times cited : (5)

References (25)
  • 1
    • 79956101481 scopus 로고    scopus 로고
    • Comparative characterization of commercially important xylanase enzymes
    • Arora, N, Banerjee, AK, Mutyala, S, Murty, S, Comparative characterization of commercially important xylanase enzymes. Bioinformation 3 (2009), 446–453.
    • (2009) Bioinformation , vol.3 , pp. 446-453
    • Arora, N.1    Banerjee, A.K.2    Mutyala, S.3    Murty, S.4
  • 3
    • 0041541782 scopus 로고    scopus 로고
    • A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes
    • Blanco, A, Díaz, P, Zueco, J, Parascandola, P, Javier, PFI, A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes. Microbiology 145 (1999), 2163–2170.
    • (1999) Microbiology , vol.145 , pp. 2163-2170
    • Blanco, A.1    Díaz, P.2    Zueco, J.3    Parascandola, P.4    Javier, P.F.I.5
  • 4
    • 0033610846 scopus 로고    scopus 로고
    • The topology of the substrate binding clefts of glycosyl hydrolase family 10 xylanases are not conserved
    • Charnock, SJ, Spurway, H, Xie, H, Beylot, MH, Virden, R, Warren, RA, Hazlewood, Gilbert, HJ, The topology of the substrate binding clefts of glycosyl hydrolase family 10 xylanases are not conserved. J Biol Chem 273 (1998), 32187–32199.
    • (1998) J Biol Chem , vol.273 , pp. 32187-32199
    • Charnock, S.J.1    Spurway, H.2    Xie, H.3    Beylot, M.H.4    Virden, R.5    Warren, R.A.6    Hazlewood7    Gilbert, H.J.8
  • 5
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins, T, Gerday, C, Feller, G, Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 29 (2005), 3–23.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 6
    • 0037323213 scopus 로고    scopus 로고
    • Bioinformatics methods to predict protein structure and function. A practical approach
    • Edwards, YJ, Cottage, A, Bioinformatics methods to predict protein structure and function. A practical approach. Mol Biotechnol 23 (2003), 139–166.
    • (2003) Mol Biotechnol , vol.23 , pp. 139-166
    • Edwards, Y.J.1    Cottage, A.2
  • 7
    • 0034727682 scopus 로고    scopus 로고
    • Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different position
    • Funahashi, J, Takano, K, Yamagata, Y, Yutani, K, Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different position. Biochemistry 39 (2000), 14448–14456.
    • (2000) Biochemistry , vol.39 , pp. 14448-14456
    • Funahashi, J.1    Takano, K.2    Yamagata, Y.3    Yutani, K.4
  • 8
    • 0343293808 scopus 로고    scopus 로고
    • An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study
    • Georis, J, Esteves, FL, Lammote-Brasseur, J, Bougnet, V, Devreese, B, Giannotta, F, Granier, B, Frere, J-M, An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study. Protein Sci 9 (2000), 466–475.
    • (2000) Protein Sci , vol.9 , pp. 466-475
    • Georis, J.1    Esteves, F.L.2    Lammote-Brasseur, J.3    Bougnet, V.4    Devreese, B.5    Giannotta, F.6    Granier, B.7    Frere, J.-M.8
  • 9
    • 0032578420 scopus 로고    scopus 로고
    • Thermophilic xylanase from Thermomyces lanuginosus: High resolution X-ray structure and modeling studies
    • Gruber, K, Klintsar, G, Hayn, M, Schlacher, A, Steiner, W, Kratky, C, Thermophilic xylanase from Thermomyces lanuginosus: High resolution X-ray structure and modeling studies. Biochemistry 37 (1998), 13475–13485.
    • (1998) Biochemistry , vol.37 , pp. 13475-13485
    • Gruber, K.1    Klintsar, G.2    Hayn, M.3    Schlacher, A.4    Steiner, W.5    Kratky, C.6
  • 10
    • 0037411739 scopus 로고    scopus 로고
    • Development in industrially thermostable enzymes: a review
    • Haki, GD, Rakshit, SK, Development in industrially thermostable enzymes: a review. Bioresource Technol 89 (2003), 17–34.
    • (2003) Bioresource Technol , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 13
    • 28644442880 scopus 로고    scopus 로고
    • Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritime MSB8
    • Ihsanawati, Kumasaka, T, Kaneko, T, Morokuma, C, Yatsunami, R, Sato, T, Nakamura, S, Tanaka, N, Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritime MSB8. Proteins 61 (2005), 999–1009.
    • (2005) Proteins , vol.61 , pp. 999-1009
    • Ihsanawati1    Kumasaka, T.2    Kaneko, T.3    Morokuma, C.4    Yatsunami, R.5    Sato, T.6    Nakamura, S.7    Tanaka, N.8
  • 15
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin, A, Alchanati, I, Shoham, Y, Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6. Appl Environ Microbiol 59 (1993), 1725–1730.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Shoham, Y.3
  • 16
    • 33744515651 scopus 로고    scopus 로고
    • Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution
    • Miyazaki, K, Takenouchi, M, Kondo, H, Noro, N, Suzuki, M, Tsuda, S, Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution. J Biol Chem 281 (2006), 10236–10242.
    • (2006) J Biol Chem , vol.281 , pp. 10236-10242
    • Miyazaki, K.1    Takenouchi, M.2    Kondo, H.3    Noro, N.4    Suzuki, M.5    Tsuda, S.6
  • 17
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: the the evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano, N, Orengo, CA, Thornton, JM, One fold with many functions: the the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J Mol Biol 321 (2002), 741–765.
    • (2002) J Mol Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 19
    • 0034661506 scopus 로고    scopus 로고
    • Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling
    • Shibuya, H, Kaneko, S, Hayashi, K, Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling. Biochem J 349 (2000), 651–656.
    • (2000) Biochem J , vol.349 , pp. 651-656
    • Shibuya, H.1    Kaneko, S.2    Hayashi, K.3
  • 22
    • 0024571667 scopus 로고
    • Species-specific variation in signal peptide design. Implications for protein secretion in foreign host
    • Von Heijne, G, Abrahamsen, L, Species-specific variation in signal peptide design. Implications for protein secretion in foreign host. FEBS Lett 244 (1989), 439–446.
    • (1989) FEBS Lett , vol.244 , pp. 439-446
    • Von Heijne, G.1    Abrahamsen, L.2
  • 23
    • 0030052194 scopus 로고    scopus 로고
    • Crystallographic observation of a covalent catalytic intermediate in a beta-glycoside
    • White, A, Tull, D, Johns, K, Withers, SG, Rose, DR, Crystallographic observation of a covalent catalytic intermediate in a beta-glycoside. Nat Struc Biol 3 (1996), 149–154.
    • (1996) Nat Struc Biol , vol.3 , pp. 149-154
    • White, A.1    Tull, D.2    Johns, K.3    Withers, S.G.4    Rose, D.R.5
  • 24
    • 33749835413 scopus 로고    scopus 로고
    • Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific
    • Wu, S, Liu, B, Zhang, X, Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific. Appl Microbiol Biotechnol 72 (2006), 1210–1216.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1210-1216
    • Wu, S.1    Liu, B.2    Zhang, X.3
  • 25
    • 33745273597 scopus 로고    scopus 로고
    • Probing the structural basis for the difference in thermostability displayed by family 10 xylanases
    • Xie, H, Flint, J, Vardakaou, M, Lakey, JH, Lewis, RJ, Gilbert, HJ, Dumon, C, Probing the structural basis for the difference in thermostability displayed by family 10 xylanases. J Mol Biol 360 (2006), 157–167.
    • (2006) J Mol Biol , vol.360 , pp. 157-167
    • Xie, H.1    Flint, J.2    Vardakaou, M.3    Lakey, J.H.4    Lewis, R.J.5    Gilbert, H.J.6    Dumon, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.